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collagen</title> <meta name="description" content="Search results for: collagen"> <meta name="keywords" content="collagen"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none navbar-toggler ml-auto" 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id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="collagen"> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 216</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: collagen</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">216</span> Isolation and Characterization of Collagen from Chicken Feet</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=P.%20Hashim">P. Hashim</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20S.%20Mohd%20Ridzwan"> M. S. Mohd Ridzwan</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Bakar"> J. Bakar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II, and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chicken%20feet" title="chicken feet">chicken feet</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen" title=" collagen"> collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=papain" title=" papain"> papain</a>, <a href="https://publications.waset.org/abstracts/search?q=pepsin" title=" pepsin"> pepsin</a> </p> <a href="https://publications.waset.org/abstracts/3623/isolation-and-characterization-of-collagen-from-chicken-feet" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/3623.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">427</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">215</span> Development of Technologies for Biotransformation of Aquatic Biological Resources for the Production of Functional, Specialized, Therapeutic, Preventive, and Microbiological Products</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Kira%20Rysakova">Kira Rysakova</a>, <a href="https://publications.waset.org/abstracts/search?q=Vitaly%20Novikov"> Vitaly Novikov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> An improved method of obtaining enzymatic collagen hydrolysate from the tissues of marine hydrobionts is proposed, which allows to obtain hydrolysate without pre-isolation of pure collagen. The method can be used to isolate enzymatic collagen hydrolysate from the waste of industrial processing of Red King crab and non-traditional objects - marine holothurias. Comparative analysis of collagen hydrolysates has shown the possibility of their use in a number of nutrient media, but this requires additional optimization of their composition and biological tests on wide sets of test strains of microorganisms. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen%20hydrolysate" title="collagen hydrolysate">collagen hydrolysate</a>, <a href="https://publications.waset.org/abstracts/search?q=marine%20hydrobionts" title=" marine hydrobionts"> marine hydrobionts</a>, <a href="https://publications.waset.org/abstracts/search?q=red%20king%20crab" title=" red king crab"> red king crab</a>, <a href="https://publications.waset.org/abstracts/search?q=marine%20holothurias" title=" marine holothurias"> marine holothurias</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymes" title=" enzymes"> enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=exclusive%20HPLC" title=" exclusive HPLC"> exclusive HPLC</a> </p> <a href="https://publications.waset.org/abstracts/146190/development-of-technologies-for-biotransformation-of-aquatic-biological-resources-for-the-production-of-functional-specialized-therapeutic-preventive-and-microbiological-products" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/146190.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">169</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">214</span> Inhibitory Effects of PPARγ Ligand, KR-62980, on Collagen-Stimulated Platelet Activation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Su%20Bin%20Wang">Su Bin Wang</a>, <a href="https://publications.waset.org/abstracts/search?q=Jin%20Hee%20Ahn"> Jin Hee Ahn</a>, <a href="https://publications.waset.org/abstracts/search?q=Tong-Shin%20Chang"> Tong-Shin Chang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The peroxisome proliferator-activated receptors (PPARs) are member of nuclear receptor superfamily that act as a ligand-activated transcription factors. Although platelets lack a nucleus, previous studies have shown that PPARγ agonists, rosiglitazone, inhibited platelet activation induced by collagen. In this study, we investigated the inhibitory effects of KR-62980, a newly synthesized PPARγ agonist, on collagen receptor-stimulated platelet activation. The specific tyrosine phosphorylations of key components (Syk, Vav1, Btk and PLCγ2) for collagen receptor signaling pathways were suppressed by KR-62980. KR-62980 also attenuated downstream responses including cytosolic calcium elevation, P-selectin surface exposure, and integrin αIIbβ3 activation. PPARγ was found to associate with multiple proteins within the LAT signaling complex in collagen-stimulated platelets. This association was prevented by KR-62980, indicating a potential mechanism for PPARγ function in collagen-stimulated platelet activation. Furthermore, KR-62980 inhibited platelet aggregation and adhesion in response to collagen in vitro and prolonged in vivo thrombotic response in carotid arteries of mice. Collectively, these data suggest that KR-62980 inhibits collagen-stimulated platelet activation and thrombus formation through modulating the collagen receptor signaling pathways. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=KR-62980" title="KR-62980">KR-62980</a>, <a href="https://publications.waset.org/abstracts/search?q=PPAR%CE%B3" title=" PPARγ"> PPARγ</a>, <a href="https://publications.waset.org/abstracts/search?q=antiplatelet" title=" antiplatelet"> antiplatelet</a>, <a href="https://publications.waset.org/abstracts/search?q=thrombosis" title=" thrombosis"> thrombosis</a> </p> <a href="https://publications.waset.org/abstracts/47842/inhibitory-effects-of-ppargh-ligand-kr-62980-on-collagen-stimulated-platelet-activation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/47842.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">333</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">213</span> The Production of Collagen and Collagen Peptides from Nile Tilapia Skin Using Membrane Technology</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20Thuanthong">M. Thuanthong</a>, <a href="https://publications.waset.org/abstracts/search?q=W.%20Youravong"> W. Youravong</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Sirinupong"> N. Sirinupong</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Nile tilapia (Oreochromis niloticus) is one of fish species cultured in Thailand with a high production volume. A lot of skin is generated during fish processing. In addition, there are many research reported that fish skin contains abundant of collagen. Thus, the use of Nile tilapia skin as collagen source can increase the benefit of industrial waste. In this study, Acid soluble collagen (ASC) was extracted at 5, 15 or 25 ˚C with 0.5 M acetic acid then the acid was removed out and collagen was concentrated by ultrafiltration-diafiltration (UFDF). The triple helix collagen from UFDF process was used as substrate to produce collagen peptides by alcalase hydrolysis in an enzymatic membrane reactor (EMR) coupling with 1 kDa molecular weight cut off (MWCO) polysulfone hollow fiber membrane. The results showed that ASC extracted at high temperature (25 ˚C) with 0.5 M acetic acid for 5 h still preserved triple helix structure. In the UFDF process, the acid removal was higher than 90 % without any effect on ASC properties, particularly triple helix structure as indicated by circular dichroism spectrum. Moreover, Collagen from UFDF was used to produce collagen peptides by EMR. In EMR, collagen was pre-hydrolyzed by alcalase for 60 min before introduced to membrane separation. The EMR operation was operated for 10 h and provided a good of protein conversion stability. The results suggested that there is a successfulness of UF in application for acid removal to produce ASC with desirable preservation of its quality. In addition, the EMR was proven to be an effective process to produce low molecular weight peptides with ACE-inhibitory activity properties. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=acid%20soluble%20collagen" title="acid soluble collagen">acid soluble collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=ultrafiltration-diafiltration" title=" ultrafiltration-diafiltration"> ultrafiltration-diafiltration</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymatic%20membrane%20reactor" title=" enzymatic membrane reactor"> enzymatic membrane reactor</a>, <a href="https://publications.waset.org/abstracts/search?q=ace-inhibitory%20activity" title=" ace-inhibitory activity"> ace-inhibitory activity</a> </p> <a href="https://publications.waset.org/abstracts/31350/the-production-of-collagen-and-collagen-peptides-from-nile-tilapia-skin-using-membrane-technology" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/31350.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">477</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">212</span> Electrospun Nanofibrous Scaffolds Modified with Collagen-I and Fibronectin with LX-2 Cells to Study Liver Fibrosis in vitro</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Prativa%20Das">Prativa Das</a>, <a href="https://publications.waset.org/abstracts/search?q=Lay%20Poh%20Tan"> Lay Poh Tan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Three-dimensional microenvironment is a need to study the event cascades of liver fibrosis in vitro. Electrospun nanofibers modified with essential extracellular matrix proteins can closely mimic the random fibrous structure of native liver extracellular matrix (ECM). In this study, we fabricate a series of 3D electrospun scaffolds by wet electrospinning process modified with different ratios of collagen-I to fibronectin to achieve optimized distribution of these two ECM proteins on the fiber surface. A ratio of 3:1 of collagen-I to fibronectin was found to be optimum for surface modification of electrospun poly(lactic-co-glycolic acid) (PLGA) fibers by chemisorption process. In 3:1 collagen-I to fibronectin modified scaffolds the total protein content increased by ~2 fold compared to collagen-I modified and ~1.5 fold compared to 1:1/9:1 collagen-I to fibronectin modified scaffolds. We have cultured LX-2 cells on this scaffold over 14 days and found that LX-2 cells acquired more quiescent phenotype throughout the culture period and shown significantly lower expression of alpha smooth muscle actin and collagen-I. Thus, this system can be used as a model to study liver fibrosis by using different fibrogenic mediators in vitro. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrospinning" title="electrospinning">electrospinning</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen-I%20and%20fibronectin" title=" collagen-I and fibronectin"> collagen-I and fibronectin</a>, <a href="https://publications.waset.org/abstracts/search?q=surface%20modification%20of%20fiber" title=" surface modification of fiber"> surface modification of fiber</a>, <a href="https://publications.waset.org/abstracts/search?q=LX-2%20cells" title=" LX-2 cells"> LX-2 cells</a>, <a href="https://publications.waset.org/abstracts/search?q=liver%20fibrosis" title=" liver fibrosis"> liver fibrosis</a> </p> <a href="https://publications.waset.org/abstracts/104340/electrospun-nanofibrous-scaffolds-modified-with-collagen-i-and-fibronectin-with-lx-2-cells-to-study-liver-fibrosis-in-vitro" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/104340.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">126</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">211</span> Evaluation of Collagen Synthesis in Macrophages/Fibroblasts Co-Culture Using Polylactic Acid Particles as Stimulants</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Feng%20Ju%20Chuang">Feng Ju Chuang</a>, <a href="https://publications.waset.org/abstracts/search?q=Yu%20Wen%20Wang"> Yu Wen Wang</a>, <a href="https://publications.waset.org/abstracts/search?q=Tai%20Jung%20Hsieh"> Tai Jung Hsieh</a>, <a href="https://publications.waset.org/abstracts/search?q=Shyh%20Ming%20Kuo"> Shyh Ming Kuo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Polylactic acid is a synthetic polymer with good biocompatibility and degradability, is widely used in clinical applications. In this study, we utilized Polylactic acid particles as stimulants for macrophages and the collagen synthesis of co-cultured fibroblasts was evaluated. The results indicated that Polylactic acid particles were nontoxic to cells from 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. No obvious inflammation effect was observed (under the PLLA concentration of 1 mg/mL) after 24-h co-culture of Raw264.7 and NIH3T3 cells (from TNF-α assay). The addition of PLLA particles to the Raw264.7 and NIH3T3 co-cultures increased the synthesis of collagen, the highest collagen synthesis from the fibroblast was the 0.2 mg/mL (approximately 60% increased as compared with without addition Polylactic acid particles). Moreover, a co-axial atomization delivery device was used to percutaneously introduce Polylactic acid particles into the dermis layer and stimulating macrophages to secrete growth factors promoting fibroblasts to produce collagen. The preliminary results demonstrated the synthesis of collagen was increased mildly after the introduction of Polylactic acid particles for 28-d post implantation. The Polylactic acid particles could be successfully introduced into the dermis layer from H&E staining examination, however, the optimum concentration of Polylactic acid particles and the time-period for collagen synthesis still need to be evaluated. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen%20synthesis" title="collagen synthesis">collagen synthesis</a>, <a href="https://publications.waset.org/abstracts/search?q=macrophage" title=" macrophage"> macrophage</a>, <a href="https://publications.waset.org/abstracts/search?q=NIH3T3%20cells" title=" NIH3T3 cells"> NIH3T3 cells</a>, <a href="https://publications.waset.org/abstracts/search?q=polylactic%20acid%20particles" title=" polylactic acid particles"> polylactic acid particles</a> </p> <a href="https://publications.waset.org/abstracts/156614/evaluation-of-collagen-synthesis-in-macrophagesfibroblasts-co-culture-using-polylactic-acid-particles-as-stimulants" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/156614.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">113</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">210</span> The Role Collagen VI Plays in Heart Failure: A Tale Untold</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Summer%20Hassan">Summer Hassan</a>, <a href="https://publications.waset.org/abstracts/search?q=David%20Crossman"> David Crossman</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Myocardial fibrosis (MF) has been loosely defined as the process occurring in the pathological remodeling of the myocardium due to excessive production and deposition of extracellular matrix (ECM) proteins, including collagen. This reduces tissue compliance and accelerates progression to heart failure, as well as affecting the electrical properties of the myocytes resulting in arrhythmias. Microscopic interrogation of MF is key to understanding the molecular orchestrators of disease. It is well-established that recruitment and stimulation of myofibroblasts result in Collagen deposition and the resulting expansion in the ECM. Many types of Collagens have been identified and implicated in scarring of tissue. In a series of experiments conducted at our lab, we aim to elucidate the role collagen VI plays in the development of myocardial fibrosis and its direct impact on myocardial function. This was investigated through an animal experiment in Rats with Collagen VI knockout diseased and healthy animals as well as Collagen VI wild diseased and healthy rats. Echocardiogram assessments of these rats ensued at four-time points, followed by microscopic interrogation of the myocardium aiming to correlate the role collagen VI plays in myocardial function. Our results demonstrate a deterioration in cardiac function as represented by the ejection fraction in the knockout healthy and diseased rats. This elucidates a potential protective role that collagen-VI plays following a myocardial insult. Current work is dedicated to the microscopic characterisation of the fibrotic process in all rat groups, with the results to follow. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=heart%20failure" title="heart failure">heart failure</a>, <a href="https://publications.waset.org/abstracts/search?q=myocardial%20fibrosis" title=" myocardial fibrosis"> myocardial fibrosis</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen" title=" collagen"> collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=echocardiogram" title=" echocardiogram"> echocardiogram</a>, <a href="https://publications.waset.org/abstracts/search?q=confocal%20microscopy" title=" confocal microscopy"> confocal microscopy</a> </p> <a href="https://publications.waset.org/abstracts/159033/the-role-collagen-vi-plays-in-heart-failure-a-tale-untold" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/159033.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">82</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">209</span> Collagen Deposition in Lung Parenchyma Driven by Depletion of LYVE-1+ Macrophages Protects Emphysema and Loss of Airway Function</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yinebeb%20Mezgebu%20Dagnachew">Yinebeb Mezgebu Dagnachew</a>, <a href="https://publications.waset.org/abstracts/search?q=Hwee%20Ying%20Lim"> Hwee Ying Lim</a>, <a href="https://publications.waset.org/abstracts/search?q=Liao%20Wupeng"> Liao Wupeng</a>, <a href="https://publications.waset.org/abstracts/search?q=Sheau%20Yng%20Lim"> Sheau Yng Lim</a>, <a href="https://publications.waset.org/abstracts/search?q=Lim%20Sheng%20Jie%20Natalie"> Lim Sheng Jie Natalie</a>, <a href="https://publications.waset.org/abstracts/search?q=Veronique%20Angeli"> Veronique Angeli</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Collagen is essential for maintaining lung structure and function, and its remodeling has been associated with respiratory diseases, including chronic obstructive pulmonary disease (COPD). However, the cellular mechanisms driving collagen remodeling and the functional implications of this process in the pathophysiology of pulmonary diseases remain poorly understood. Using a mouse model of Lyve-1 expressing macrophage depletion, we found that the absence of this subpopulation of tissue-resident macrophage led to the preferential deposition of type I collagen fibers around the alveoli and bronchi in the steady state. Further analysis by polarized light microscopy revealed that the collagen fibers accumulating in the lungs depleted of Lyve-1+ macrophages were thicker and crosslinked. A decrease in MMP-9 gene expression and proteolytic activity, together with an increase in Col1a1, Timp-3 and Lox gene expression, accompanied the collagen alterations. Next, we investigated the effect of the collagen remodeling on the pathophysiology of COPD and airway function in mouse lacking Lyve-1+ macrophage exposed chronically to cigarette smoke (CS), a well-established animal model of COPD. We showed that the deposition of collagen protected mouse against the destruction of alveoli (emphysema) and bronchi thickening after CS exposure and prevented loss of airway function. Thus, we demonstrate that interstitial Lyve-1+ macrophages regulate the composition, amount, and architecture of the collagen network in the lungs and that such collagen remodeling functionally impacts the development of COPD. This study further supports the potential of targeting collagen as a promising approach to treating respiratory diseases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=lung" title="lung">lung</a>, <a href="https://publications.waset.org/abstracts/search?q=extracellular%20matrix" title=" extracellular matrix"> extracellular matrix</a>, <a href="https://publications.waset.org/abstracts/search?q=chronic%20obstructive%20pulmonary%20disease" title=" chronic obstructive pulmonary disease"> chronic obstructive pulmonary disease</a>, <a href="https://publications.waset.org/abstracts/search?q=matrix%20metalloproteinases" title=" matrix metalloproteinases"> matrix metalloproteinases</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen" title=" collagen"> collagen</a> </p> <a href="https://publications.waset.org/abstracts/187346/collagen-deposition-in-lung-parenchyma-driven-by-depletion-of-lyve-1-macrophages-protects-emphysema-and-loss-of-airway-function" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/187346.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">37</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">208</span> Re-Differentiation Effect of Sesquiterpene Farnesol on De-Differentiated Rabbit Chondrocytes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Chun%20Hsien%20Wu">Chun Hsien Wu</a>, <a href="https://publications.waset.org/abstracts/search?q=Guan%20Xuan%20Wu"> Guan Xuan Wu</a>, <a href="https://publications.waset.org/abstracts/search?q=Hsia%20Ying%20Cheng"> Hsia Ying Cheng</a>, <a href="https://publications.waset.org/abstracts/search?q=Shyh%20Ming%20Kuo"> Shyh Ming Kuo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Articular cartilage is composed of chondrocytes and extracellular matrix, such as collagen fibers, glycosaminoglycans, etc., which play an important role in lubricating and cushion joint activities. The phenotypic expression and metabolic activity of chondrocytes are extremely important in maintaining the functions of articular cartilage. In in vitro passaged culture of chondrocytes, chondrocytes gradually lose their original cell phenotype and morphology, which is called dedifferentiation. After continuous passaged culture of chondrocytes or induction by inflammatory factor IL-1, chondrocytes changed their phenotype and morphology. Also, the extracellular matrix type II collagen and GAG secretion were significantly reduced, while type I and X collagen were synthesized. Farnesol is an anti-inflammatory and antioxidant sesquiterpene compound that has the specific property of promoting collagen production. The purpose of this study was to investigate whether farnesol could restore the original type II collagen synthesis and, furthermore, the mechanisms of farnesol on the synthesis of type II collagen from the de-differentiated chondrocytes. The obtained results showed that the de-differentiated chondrocytes significantly restored to secret type II collagen and GAG (2.5-folds increases), and the secretion of collagen I and X and PGE2 synthesis were also significantly reduced after being treated with farnesol, indicating that farnesol had a restoration/re-differentiation effect on de-differentiated chondrocytes. The de-differentiated chondrocytes exhibited decreased expression of PPAR-γ and upregulated TGF-β expression to increase the MMP-13 expression. Higher expression of MMP-13 caused chondrocytes to secret type X collagen. On the contrary, increasing the expression of PPAR-γ would benefit the production of type II collagen. As shown, the PPAR-γ expression increased, and MMP-13 expression decreased after being treated with farnesol, indicating a possible signal pathway of farnesol to restore the production of type II collagen. However, more detailed mechanisms still need to evaluate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chondrocytes" title="chondrocytes">chondrocytes</a>, <a href="https://publications.waset.org/abstracts/search?q=de-differentiation" title=" de-differentiation"> de-differentiation</a>, <a href="https://publications.waset.org/abstracts/search?q=farnesol" title=" farnesol"> farnesol</a>, <a href="https://publications.waset.org/abstracts/search?q=re-differentiation" title=" re-differentiation"> re-differentiation</a> </p> <a href="https://publications.waset.org/abstracts/156619/re-differentiation-effect-of-sesquiterpene-farnesol-on-de-differentiated-rabbit-chondrocytes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/156619.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">125</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">207</span> Collagen Hydrogels Cross-Linked by Squaric Acid</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Joanna%20Skopinska-Wisniewska">Joanna Skopinska-Wisniewska</a>, <a href="https://publications.waset.org/abstracts/search?q=Anna%20Bajek"> Anna Bajek</a>, <a href="https://publications.waset.org/abstracts/search?q=Marta%20Ziegler-Borowska"> Marta Ziegler-Borowska</a>, <a href="https://publications.waset.org/abstracts/search?q=Alina%20Sionkowska"> Alina Sionkowska</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Hydrogels are a class of materials widely used in medicine for many years. Proteins, such as collagen, due to the presence of a large number of functional groups are easily wettable by polar solvents and can create hydrogels. The supramolecular network capable to swelling is created by cross-linking of the biopolymers using various reagents. Many cross-linking agents has been tested for last years, however, researchers still are looking for a new, more secure reactants. Squaric acid, 3,4-dihydroxy 3-cyclobutene 1,2- dione, is a very strong acid, which possess flat and rigid structure. Due to the presence of two carboxyl groups the squaric acid willingly reacts with amino groups of collagen. The main purpose of this study was to investigate the influence of addition of squaric acid on the chemical, physical and biological properties of collagen materials. The collagen type I was extracted from rat tail tendons and 1% solution in 0.1M acetic acid was prepared. The samples were cross-linked by the addition of 5%, 10% and 20% of squaric acid. The mixtures of all reagents were incubated 30 min on magnetic stirrer and then dialyzed against deionized water. The FTIR spectra show that the collagen structure is not changed by cross-linking by squaric acid. Although the mechanical properties of the collagen material deteriorate, the temperature of thermal denaturation of collagen increases after cross-linking, what indicates that the protein network was created. The lyophilized collagen gels exhibit porous structure and the pore size decreases with the higher addition of squaric acid. Also the swelling ability is lower after the cross-linking. The in vitro study demonstrates that the materials are attractive for 3T3 cells. The addition of squaric acid causes formation of cross-ling bonds in the collagen materials and the transparent, stiff hydrogels are obtained. The changes of physicochemical properties of the material are typical for cross-linking process, except mechanical properties – it requires further experiments. However, the results let us to conclude that squaric acid is a suitable cross-linker for protein materials for medicine and tissue engineering. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=squaric%20acid" title=" squaric acid"> squaric acid</a>, <a href="https://publications.waset.org/abstracts/search?q=cross-linking" title=" cross-linking"> cross-linking</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrogel" title=" hydrogel"> hydrogel</a> </p> <a href="https://publications.waset.org/abstracts/20061/collagen-hydrogels-cross-linked-by-squaric-acid" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/20061.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">388</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">206</span> Angiogenic Potential of Collagen Based Biomaterials Implanted on Chick Embryo Chorioallantoic Membrane as Alternative Microenvironment for in Vitro and in Vivo Angiogenesis Assays</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Anca%20Maria%20Cimpean">Anca Maria Cimpean</a>, <a href="https://publications.waset.org/abstracts/search?q=Serban%20Comsa"> Serban Comsa</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Chick embryo chorioallantoic membrane (CAM) is a well vascularised in vivo experimental model used as a platform for testing the behavior of different implants inserted on it from tumor fragments to therapeutic agents or various biomaterials. Five types of collagen-based biomaterials with 2D and 3D structure (MotifMesh, Optimaix2D, Optimaix3D, Dual Layer Collagen and Xenoderm) were implanted on CAM and continuously evaluated by stereomicroscope for up to 5 days post-implant with an emphasis of their ability to requisite and develop new blood vessels (BVs) followed by microscopic analysis. MotifMEsh did not induce any angiogenic response lacking to be invaded by BVs from the CAM, but it induced intense inflammatory response necrosis and fibroblastic reaction around the implant. Optimaix2D has good adherence. CAM with minimal or no inflammatory reaction, a good integration of the CAM between the collagen mesh’s fibers, consistent adhesion of the cells to the collagen fibers,and a good ability to form pseudo-vascular channels filled with cells. Optimaix3D induced the highest angiogenic effects on CAM. The material shows good integration on CAM. The collagen fibers of the material show the ability to organize themselves into linear and tubular structures. It is possible to see blood elements, especially at the periphery of the implant. Dual-layer collagen behaves similar to Optimaix 3D, while Xenoderm induced a moderate angiogenic effect on CAM. Based on these data, we may conclude that collagen-based materials have variable ability to requisite and develop new blood vessels. A proper selection of collagen-based biomaterial scaffolds may crucially influence the acquisition and development of blood vessels during angiogenesis assays. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chick%20embryo%20chorioallantoic%20membrane" title="chick embryo chorioallantoic membrane">chick embryo chorioallantoic membrane</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen%20scaffolds" title=" collagen scaffolds"> collagen scaffolds</a>, <a href="https://publications.waset.org/abstracts/search?q=blood%20vessels" title=" blood vessels"> blood vessels</a>, <a href="https://publications.waset.org/abstracts/search?q=vascular%20microenvironment" title=" vascular microenvironment"> vascular microenvironment</a> </p> <a href="https://publications.waset.org/abstracts/143642/angiogenic-potential-of-collagen-based-biomaterials-implanted-on-chick-embryo-chorioallantoic-membrane-as-alternative-microenvironment-for-in-vitro-and-in-vivo-angiogenesis-assays" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/143642.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">193</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">205</span> The Collagen and Glycosaminoglycnas Isolated from Salmo Salar Skin</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Beata%20Kaczmarek-Szczepa%C5%84ska">Beata Kaczmarek-Szczepańska</a>, <a href="https://publications.waset.org/abstracts/search?q=Lidia%20Zasada"> Lidia Zasada</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Marine collagens such as fish skin, bone, cartilage, and scales, including both marine vertebrates and invertebrates sources, are more bioavailable compared to bovine or porcine collagen and have a higher absorption capability and more rapid bloodstream circulation due to their low molecular weight and small particle size. Fish skin may be used as a source of bioactive compounds. The advantage is that fish skin is a by-product of the food industry. The subject of the study is a lyophilizate consisting of a mixture of compounds from the group of glycosaminoglycans and collagen obtained as a result of processing fish skins. Bioactive compounds may find biomedical use in the production of dressing materials for wounds or in tissue engineering for the production of scaffolds for cells. Collagen and glycosaminoglycans were isolated from Salmo salar skin. The final mixture was obtained by the freeze-drying method. In the obtained lyophilizate, the content of amino acids was studied as well as the presence of polysaccharides. The studies showed the presence of glycine, proline, and hydroxyproline, which are the main amino acids of collagen. The HPLC analysis showed the presence of glucose which is a product of polysaccharides hydrolyzation and then reduction of glucuronic acid. It may be assumed that the lyophilizate contains both collagen and polysaccharide, which is probably hyaluronic acid. Acknowledgment: This work was carried out as a result of research project no. TANGO-V-A/0020/2021 financed by the National Centre for Research and Development. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=glycosaminoglycans" title=" glycosaminoglycans"> glycosaminoglycans</a>, <a href="https://publications.waset.org/abstracts/search?q=bioactive%20compounds" title=" bioactive compounds"> bioactive compounds</a>, <a href="https://publications.waset.org/abstracts/search?q=fish%20skin" title=" fish skin"> fish skin</a> </p> <a href="https://publications.waset.org/abstracts/153105/the-collagen-and-glycosaminoglycnas-isolated-from-salmo-salar-skin" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/153105.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">114</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">204</span> Characteristics of Smoked Edible Film Made from Myofibril, Collagen and Carrageenan</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Roike%20Iwan%20Montolalu">Roike Iwan Montolalu</a>, <a href="https://publications.waset.org/abstracts/search?q=Henny%20Adeleida%20Dien"> Henny Adeleida Dien</a>, <a href="https://publications.waset.org/abstracts/search?q=Feny%20Mentang"> Feny Mentang</a>, <a href="https://publications.waset.org/abstracts/search?q=Kristhina%20P.%20Rahael"> Kristhina P. Rahael</a>, <a href="https://publications.waset.org/abstracts/search?q=Tomy%20Moga"> Tomy Moga</a>, <a href="https://publications.waset.org/abstracts/search?q=Ayub%20Meko"> Ayub Meko</a>, <a href="https://publications.waset.org/abstracts/search?q=Siegfried%20Berhimpon"> Siegfried Berhimpon </a> </p> <p class="card-text"><strong>Abstract:</strong></p> In the last 20 years, packaging materials derived from petrochemicals polymers were widely used as packaging materials. This due to various advantages such as flexible, strong, transparent, and the price is relatively cheap. However, the plastic polymer also has various disadvantages, such as the transmission monomer contamination into the material to be packed, and waste is non-biodegradable. Edible film (EF) is an up to date materials, generated after the biodegradable packaging materials. The advantages of the EF materials, is the materials can be eat together with food, and the materials can be applied as a coating materials for a widely kind of foods especially snack foods. The aims of this research are to produce and to analyze the characteristics of smoked EF made from carrageenan, myofibril and collagen of Black Marlin (Makaira indica) industrial waste. Smoked EF made with an addition of 0.8 % smoke liquid. Three biopolymers i.e. carrageenan, myofibril, and collagen were used as treatments, and homogenate for 1 hours at speed of 1500 rpm. The analysis carried out on the pH and physical properties i.e. thickness, solubility, tensile strength, % elongation, and water vapor transmission rate (WVTR), as well as on the sensory characteristics of texture i.e. wateriness, firmness, elasticity, hardness, and juiciness of the coated products. The result shown that the higher the concentration the higher the thickness of EF, where as for myofibril proteins appeared higher than carrageenan and collagen. Both of collagen and myofibril shown that concentration of 6% was most soluble, while for carrageenan were in concentration of 2 to 2.5%. For tensile strength, carrageenan was significantly higher than myofibril and collagen; while for elongation, collagen film more elastic than carragenan and myofibril protein. Water vapor transmission rate, shown that myofibril protein film lower than carrageenan and collagen film. From sensory assessment of texture, carrageenan has a high elasticity and juiciness, while collagen and myofibril have a high in firmness and hardness. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=edible%20film" title="edible film">edible film</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen" title=" collagen"> collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=myofibril" title=" myofibril"> myofibril</a>, <a href="https://publications.waset.org/abstracts/search?q=carrageenan" title=" carrageenan"> carrageenan</a> </p> <a href="https://publications.waset.org/abstracts/33009/characteristics-of-smoked-edible-film-made-from-myofibril-collagen-and-carrageenan" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/33009.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">429</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">203</span> Optimization of Extraction Conditions and Characteristics of Scale collagen From Sardine: Sardina pilchardus</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=F.%20Bellali">F. Bellali</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Kharroubi"> M. Kharroubi</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Loutfi"> M. Loutfi</a>, <a href="https://publications.waset.org/abstracts/search?q=N.Bourhim"> N.Bourhim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In Morocco, fish processing industry is an important source income for a large amount of byproducts including skins, bones, heads, guts and scales. Those underutilized resources particularly scales contain a large amount of proteins and calcium. Scales from Sardina plichardus resulting from the transformation operation have the potential to be used as raw material for the collagen production. Taking into account this strong expectation of the regional fish industry, scales sardine upgrading is well justified. In addition, political and societal demands for sustainability and environment-friendly industrial production systems, coupled with the depletion of fish resources, drive this trend forward. Therefore, fish scale used as a potential source to isolate collagen has a wide large of applications in food, cosmetic and bio medical industry. The main aim of this study is to isolate and characterize the acid solubilize collagen from sardine fish scale, Sardina pilchardus. Experimental design methodology was adopted in collagen processing for extracting optimization. The first stage of this work is to investigate the optimization conditions of the sardine scale deproteinization on using response surface methodology (RSM). The second part focus on the demineralization with HCl solution or EDTA. Moreover, the last one is to establish the optimum condition for the isolation of collagen from fish scale by solvent extraction. The basic principle of RSM is to determinate model equations that describe interrelations between the independent variables and the dependent variables. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sardina%20pilchardus" title="Sardina pilchardus">Sardina pilchardus</a>, <a href="https://publications.waset.org/abstracts/search?q=scales" title=" scales"> scales</a>, <a href="https://publications.waset.org/abstracts/search?q=valorization" title=" valorization"> valorization</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen%20extraction" title=" collagen extraction"> collagen extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology "> response surface methodology </a> </p> <a href="https://publications.waset.org/abstracts/16533/optimization-of-extraction-conditions-and-characteristics-of-scale-collagen-from-sardine-sardina-pilchardus" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16533.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">415</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">202</span> The Role of Estradiol-17β and Type IV Collagen on the Regulation and Expression Level Of C-Erbb2 RNA and Protein in SKOV-3 Ovarian Cancer Cell Line </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Merry%20Meryam%20Martgrita">Merry Meryam Martgrita</a>, <a href="https://publications.waset.org/abstracts/search?q=Marselina%20Irasonia%20Tan"> Marselina Irasonia Tan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> One of several aggresive cancer is cancer that overexpress c-erbB2 receptor along with the expression of estrogen receptor. Components of extracellular matrix play an important role to increase cancer cells proliferation, migration and invasion. Both components can affect cancer development by regulating the signal transduction pathways in cancer cells. In recent research, SKOV-3 ovarian cancer cell line, that overexpress c-erbB2 receptor was cultured on type IV collagen and treated with estradiol-17β, to reveal the role of both components on RNA and protein level of c-erbB2 receptor. In this research we found a modulation phenomena of increasing and decreasing of c-erbB2 RNA level and a stabilisation phenomena of c-erbB2 protein expression due to estradiol-17β and type IV collagen. It seemed that estradiol-17β has an important role to increase c-erbB2 transcription and the stability of c-erbB2 protein expression. Type IV collagen has an opposite role. It blocked c-erbB2 transcription when it bound to integrin receptor in SKOV-3 cells. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=c-erbB2" title="c-erbB2">c-erbB2</a>, <a href="https://publications.waset.org/abstracts/search?q=estradiol-17%CE%B2" title=" estradiol-17β"> estradiol-17β</a>, <a href="https://publications.waset.org/abstracts/search?q=SKOV-3" title=" SKOV-3"> SKOV-3</a>, <a href="https://publications.waset.org/abstracts/search?q=type%20IV%20collagen" title=" type IV collagen"> type IV collagen</a> </p> <a href="https://publications.waset.org/abstracts/27964/the-role-of-estradiol-17v-and-type-iv-collagen-on-the-regulation-and-expression-level-of-c-erbb2-rna-and-protein-in-skov-3-ovarian-cancer-cell-line" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27964.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">284</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">201</span> Arothron Stellatus Fish Skin Collagen Based Composite Biosheet Incorporated with Mupirocin as a Potential Dermal Substitute for Skin Tissue Regeneration </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Giriprasath%20Ramanathan">Giriprasath Ramanathan</a>, <a href="https://publications.waset.org/abstracts/search?q=Sivakumar%20Singaravelu"> Sivakumar Singaravelu</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20D.%20Raja"> M. D. Raja</a>, <a href="https://publications.waset.org/abstracts/search?q=Uma%20Tirichurapalli%20Sivagnanam"> Uma Tirichurapalli Sivagnanam</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Collagen is the abundant protein found in the skin of the animal body that has been designed to provide adequate structural support for the adhesion of cells. The dressing material widely used for tissue engineering and biomedical application has to posses good swelling and biological property for the absorption of exudates and cell proliferation. Acid solubilised collagen from the fish skin of the Arothron stellatus was extracted. The collagen with hydroxypropyl and carboxy methyl cellulose has the better biological property to enhance the healing efficiency. The inter property of collagen with interesting perspectives in the tissue engineering process leads to the development of biomaterial with natural polymer with biologically derived collagen. Keeping this as an objective, the composite biomaterial was fabricated to improve the wound healing and biological properties. In this study the collagen from Arothron stellatus fish skin (ACO) was uniformly blended separately with hydroxypropyl methyl cellulose (HPMC) and carboxyl methyl cellulose (CMC) as biosheets. The casted biosheets were impregnated with mupirocin to get rid of infection from the microbes. Further, the results obtained from differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), tensile studies and biocompatibility of the biosheets were assessed. The swelling, porosity and degradation of the casted biosheets were studied to make the biosheets as a suitable wound dressing material. ACO-HPMC and ACO-CMC biosheets both showed good results, but ACO-HPMC biosheet showed better results than ACO-CMC and hence it can be used as a potential dermal substitute in skin tissue engineering. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=arothron%20stellatus" title="arothron stellatus">arothron stellatus</a>, <a href="https://publications.waset.org/abstracts/search?q=biocompatibility" title=" biocompatibility"> biocompatibility</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen" title=" collagen"> collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=tensile%20strenght" title=" tensile strenght "> tensile strenght </a> </p> <a href="https://publications.waset.org/abstracts/27492/arothron-stellatus-fish-skin-collagen-based-composite-biosheet-incorporated-with-mupirocin-as-a-potential-dermal-substitute-for-skin-tissue-regeneration" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27492.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">321</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">200</span> Pufferfish Skin Collagens and Their Role in Inflation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Kirti">Kirti</a>, <a href="https://publications.waset.org/abstracts/search?q=Samanta%20Sekhar%20Khora"> Samanta Sekhar Khora</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Inflation serves different purposes in different organisms and adds beauty to their behavioral attributes. Pufferfishes are also known as blowfish, swellfish, and globefish due to their remarkable ability to puff themselves up like a balloon when threatened. This ability to inflate can be correlated with anatomical features that are unique to pufferfishes. Pufferfish skin provides a rigid framework to support the body contents and a flexible covering to allow whatever changes are necessary for remarkable inflation mechanism. Skin, the outer covering of animals is made up of collagen fibers arranged in more or less ordered arrays. The ventral skin of pufferfish stretches more than dorsal skin during inflation. So, this study is of much of the interest in comparing the structure and mechanical properties of these two skin regions. The collagen fibers were found to be arranged in different ordered arrays for ventral and dorsal skin and concentration of fibers were also found to be different for these two skin parts. Scanning electron microscopy studies of the ventral skin showed a unidirectional arrangement of the collagen fibers, which provide more stretching capacity. Dorsal skin, on the other hand, has an orthogonal arrangement of fibers. This provides more stiffness to the ventral skin at the time of inflation. In this study, the possible role of collagen fibers was determined which significantly contributed to the remarkable inflation mechanism of pufferfishes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=histology" title=" histology"> histology</a>, <a href="https://publications.waset.org/abstracts/search?q=inflation" title=" inflation"> inflation</a>, <a href="https://publications.waset.org/abstracts/search?q=pufferfish" title=" pufferfish"> pufferfish</a>, <a href="https://publications.waset.org/abstracts/search?q=scanning%20electron%20microscopy" title=" scanning electron microscopy"> scanning electron microscopy</a>, <a href="https://publications.waset.org/abstracts/search?q=Small-Angle%20X-Ray%20Scattering%20%28SAXS%29" title=" Small-Angle X-Ray Scattering (SAXS)"> Small-Angle X-Ray Scattering (SAXS)</a>, <a href="https://publications.waset.org/abstracts/search?q=transmission%20electron%20microscopy" title=" transmission electron microscopy"> transmission electron microscopy</a> </p> <a href="https://publications.waset.org/abstracts/85346/pufferfish-skin-collagens-and-their-role-in-inflation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/85346.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">317</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">199</span> Collagen Gel in Hip Cartilage Repair: in vivo Preliminary Study</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20Bajek">A. Bajek</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Skopinska-Wisniewska"> J. Skopinska-Wisniewska</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Rynkiewicz"> A. Rynkiewicz</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Jundzill"> A. Jundzill</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Bodnar"> M. Bodnar</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Marszalek"> A. Marszalek</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20Drewa"> T. Drewa</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Traumatic injury and age-related degenerative diseases associated with cartilage are major health problems worldwide. The articular cartilage is comprised of a relatively small number of cells, which have a relatively slow rate of turnover. Therefore, damaged articular cartilage has a limited capacity for self-repair. New clinical methods have been designed to achieve better repair of injured cartilage. However, there is no treatment that enables full restoration of it. The aim of this study was to evaluate how collagen gel with bone marrow mesenchymal stem cells (MSCs) and collagen gel alone will influence on the hip cartilage repair after injury. Collagen type I was isolated from rats’ tails and cross-linked with N-hydroxysuccinimide in 24-hour process. MSCs were isolated from rats’ bone marrow. The experiments were conducted according to the guidelines for animal experiments of Ethics Committee. Fifteen 8-week-old Wistar rats were used in this study. All animals received hip joint surgery with a total of 30 created cartilage defects. Then, animals were randomly divided into three groups and filled, respectively, with collagen gel (group 1), collagen gel cultured with MSCs (group II) or left untreated as a control (control group). Immunohistochemy and radiological evaluation was carried out 11 weeks post implantation. It has been proved that the surface of the matrix is non-toxic, and its porosity promotes cell adhesion and growth. However, the in vivo regeneration process was poor. We observed the low integration rate of biomaterial. Immunohistochemical evaluation of cartilage after 11 weeks of treatment showed low II and high X collagen expression in two tested groups in comparison to the control one, in which we observed the high II collagen expression. What is more, after radiological analysis, we observed the best regeneration process in control group. The biomaterial construct and mesenchymal stem cells, as well as the use of the biomaterial itself was not sufficient to regenerate the hip cartilage surfaces. These results suggest that the collagen gel based biomaterials, even with MSCs, are not satisfactory in repar of hip cartilage defect. However, additional evaluation is needed to confirm these results. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collafen%20gel" title="collafen gel">collafen gel</a>, <a href="https://publications.waset.org/abstracts/search?q=MSCs" title=" MSCs"> MSCs</a>, <a href="https://publications.waset.org/abstracts/search?q=cartilage%20repair" title=" cartilage repair"> cartilage repair</a>, <a href="https://publications.waset.org/abstracts/search?q=hip%20cartilage" title=" hip cartilage"> hip cartilage</a> </p> <a href="https://publications.waset.org/abstracts/20063/collagen-gel-in-hip-cartilage-repair-in-vivo-preliminary-study" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/20063.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">455</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">198</span> In Vitro and in Vivo Evaluation of Nano Collagen Molecules to Enhance Mesenchymal Stem Cells Differentiate into Insulin Producing Cells</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Chin-Tsu%20Ma">Chin-Tsu Ma</a>, <a href="https://publications.waset.org/abstracts/search?q=Yi-Jhen%20Wu"> Yi-Jhen Wu</a>, <a href="https://publications.waset.org/abstracts/search?q=Hsia%20Ying%20Cheng"> Hsia Ying Cheng</a>, <a href="https://publications.waset.org/abstracts/search?q=Han%20Hsiang%20Huang"> Han Hsiang Huang</a>, <a href="https://publications.waset.org/abstracts/search?q=Shyh%20Ming%20Kuo"> Shyh Ming Kuo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The use of specific molecules including nutrients and pharmacological agents has been tried in modulation of stem cells differentiation (MSCs) to insulin producing cells. The aim of this study is to investigate the ability of nano collagen molecules (nutrient or scaffold) to enhance the MSCs differentiation into insulin-producing cells in combination with nicotinamide and exendin-4 (pharmacological agents) in vitro and in vivo. The results demonstrated that the cells exhibit morphologically islet-like clusters after treatment with nano collagen molecules, nicotinamide and exendin-4. MSCs extra treated with nano collagen molecules showed significant increases in Nkx6.1 and insulin mRNA expression at 14-d and 21-d culture compared with those merely treated with nicotinamide and exendin-4. Early 7-day elevation in PDX-1 mRNA expression was observed. Furthermore, the MSCs exposed to nano collagen molecules produced the highest secretion of insulin (p ＜ 0.05). Type-2 diabetes induced by high-fat diet and low dose of streptozotocin in rat model was built in this study. This rat exhibited higher food intake, water intake, lower glucose tolerance, lower-insulin tolerance, and higher HbA1C (significant increases, p ＜ 0.01) as compared with the normal rat that demonstrated the model of type-2 diabetes was successfully built. Biopsy examinations also showed that obvious destruction of islet. After injection of differentiated MSCs into the destructed pancreas of diabetes rat, more regenerated islet were observed at the rats that treated with nano collagen molecules and exhibited much lower HbA1C as compared with the normal rat and diabetes rat after 4 weeks (significant deceases, p ＜ 0.001). These results indicate that the culturing MSCs with nano collagen molecules, nicotinamide, and exendin-4 are beneficial for MSCs differentiation into islet-like cells. These nano collagen molecules may lead to alternations or up-regulation of gene expression and influence the differentiated outcomes induced by nicotinamide and exendin-4. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=nano%20collagen%20molecules" title="nano collagen molecules">nano collagen molecules</a>, <a href="https://publications.waset.org/abstracts/search?q=nicotinamide" title=" nicotinamide"> nicotinamide</a>, <a href="https://publications.waset.org/abstracts/search?q=MSCs" title=" MSCs"> MSCs</a>, <a href="https://publications.waset.org/abstracts/search?q=diabetes" title=" diabetes"> diabetes</a> </p> <a href="https://publications.waset.org/abstracts/30467/in-vitro-and-in-vivo-evaluation-of-nano-collagen-molecules-to-enhance-mesenchymal-stem-cells-differentiate-into-insulin-producing-cells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30467.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">410</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">197</span> Comparative Wound Healing Potential of Mitracarpus villosus Ointment and Honey in Diabetic Albino Rats by Collagen Assessment</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bawa%20Inalegwu">Bawa Inalegwu</a>, <a href="https://publications.waset.org/abstracts/search?q=Jacob%20A.%20Jato"> Jacob A. Jato</a>, <a href="https://publications.waset.org/abstracts/search?q=Ovye%20Akyengo"> Ovye Akyengo</a>, <a href="https://publications.waset.org/abstracts/search?q=John%20Akighir"> John Akighir</a> </p> <p class="card-text"><strong>Abstract:</strong></p> All humans will experience some type of wound in every lifetime. Most wounds heal quickly with little or no attention but, many people suffer from wounds that are complex and/or persistent therefore posing a burden. This study was designed to assess the efficacy of Mitrcarpus villous ointment against honey in diabetic rats. To achieve this, percentage wound closure and collagen assessments were used to express treatment efficacy. Results show that on day 21, rats treated with M. villosus ointment had the highest percentage closure (94.5%) while honey treated and non-treated recorded 90.0% and 83.3% respectively. Similarly, a significant difference (p < 0.05) was observed on day 21 in the total collagen deposited in wounds of diabetic rats (10.57 ± 0.7) and M. villous ointment treated wounds (11.77 ± 0.4) as compared with the non-treated diabetic rats. M. villosus ointment was efficacious in healing wounds in diabetic rats and heals wound faster than honey and may hold potential for wound healing in diabetes mellitus sufferers. However, the wound healing mechanism of this ointment <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=diabetic%20rats" title=" diabetic rats"> diabetic rats</a>, <a href="https://publications.waset.org/abstracts/search?q=honey" title=" honey"> honey</a>, <a href="https://publications.waset.org/abstracts/search?q=Mitracarpus%20villosus" title=" Mitracarpus villosus"> Mitracarpus villosus</a>, <a href="https://publications.waset.org/abstracts/search?q=ointment" title=" ointment"> ointment</a>, <a href="https://publications.waset.org/abstracts/search?q=wound%20healing" title=" wound healing"> wound healing</a> </p> <a href="https://publications.waset.org/abstracts/139065/comparative-wound-healing-potential-of-mitracarpus-villosus-ointment-and-honey-in-diabetic-albino-rats-by-collagen-assessment" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/139065.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">199</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">196</span> The Impact of Lipids on Lung Fibrosis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=G.%20Wojcik">G. Wojcik</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Gindlhuber"> J. Gindlhuber</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Syarif"> A. Syarif</a>, <a href="https://publications.waset.org/abstracts/search?q=K.%20Hoetzenecker"> K. Hoetzenecker</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20Bohm"> P. Bohm</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20Vesely"> P. Vesely</a>, <a href="https://publications.waset.org/abstracts/search?q=V.%20Biasin"> V. Biasin</a>, <a href="https://publications.waset.org/abstracts/search?q=G.%20Kwapiszewska"> G. Kwapiszewska</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Pulmonary fibrosis is a rare disease where uncontrolled wound healing processes damage the lung structure. Intensive changes within the extracellular matrix (ECM) and its interaction with fibroblasts have a major role in pulmonary fibrosis development. Among others, collagen is one of the main components of the ECM, and it is important for lung structure. In IPF, constant production of collagen by fibroblast, through TGFβ1-SMAD2/3 pathways, leads to an uncontrolled deposition of matrix and hence lung remodeling. Abnormal changes in lipid production, alterations in fatty acids (FAs) metabolism, enhanced oxidative stress, and lipid peroxidation in fibrotic lung and fibrotic fibroblasts have been reported; however, the interplay between the collagen and lipids is not yet established. One of the FAs influx regulators is Angiopoietin-like 4 (ANGPTL4), which inhibits lipoprotein lipase work, decreasing the availability of FAs. We hypothesized that altered lipid composition or availability could have the capability to influence the phenotype of different fibroblast populations in the lung and hence influence lung fibrosis. To prove our hypothesis, we aim to investigate lipids and their influence on human, animal, and in vitro levels. In the bleomycin model, treatment with the well-known metabolic drugs Rosiglitazone or Metformin significantly lower collagen production. Similar results were noticed in ANGPTL4 KO animals, where the KO of ANGPTL4 leads to an increase of FAs availability and lower collagen deposition after the bleomycin challenge. Currently, we study the treatment of different FAs on human lung para fibroblasts (hPF) isolated from donors. To understand the lipid composition, we are collecting human lung tissue from donors and pulmonary fibrosis patients for Liquid chromatography-mass spectrometry. In conclusion, our results suggest the lipid influence on collagen deposition during lung fibrosis, but further research needs to be conducted to understand the matter of this relationship. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=fibroblasts" title=" fibroblasts"> fibroblasts</a>, <a href="https://publications.waset.org/abstracts/search?q=lipidomics" title=" lipidomics"> lipidomics</a>, <a href="https://publications.waset.org/abstracts/search?q=lung" title=" lung"> lung</a>, <a href="https://publications.waset.org/abstracts/search?q=pulmonary%20fibrosis" title=" pulmonary fibrosis"> pulmonary fibrosis</a> </p> <a href="https://publications.waset.org/abstracts/167033/the-impact-of-lipids-on-lung-fibrosis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/167033.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">84</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">195</span> The Using of Hybrid Superparamagnetic Magnetite Nanoparticles (Fe₃O₄)- Graphene Oxide Functionalized Surface with Collagen, to Target the Cancer Stem Cell</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ahmed%20Khalaf%20Reyad%20Raslan">Ahmed Khalaf Reyad Raslan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cancer stem cells (CSCs) describe a class of pluripotent cancer cells that behave analogously to normal stem cells in their ability to differentiate into the spectrum of cell types observed in tumors. The de-differentiation processes, such as an epithelial-mesenchymal transition (EMT), are known to enhance cellular plasticity. Here, we demonstrate a new hypothesis to use hybrid superparamagnetic magnetite nanoparticles (Fe₃O₄)- graphene oxide functionalized surface with Collagen to target the cancer stem cell as an early detection tool for cancer. We think that with the use of magnetic resonance imaging (MRI) and the new hybrid system would be possible to track the cancer stem cells. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hydrogel" title="hydrogel">hydrogel</a>, <a href="https://publications.waset.org/abstracts/search?q=alginate" title=" alginate"> alginate</a>, <a href="https://publications.waset.org/abstracts/search?q=reduced%20graphene%20oxide" title=" reduced graphene oxide"> reduced graphene oxide</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen" title=" collagen"> collagen</a> </p> <a href="https://publications.waset.org/abstracts/145693/the-using-of-hybrid-superparamagnetic-magnetite-nanoparticles-fe3o4-graphene-oxide-functionalized-surface-with-collagen-to-target-the-cancer-stem-cell" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/145693.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">145</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">194</span> D-Lysine Assisted 1-Ethyl-3-(3-Dimethylaminopropyl)Carbodiimide / N-Hydroxy Succinimide Initiated Crosslinked Collagen Scaffold with Controlled Structural and Surface Properties</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=G.%20Krishnamoorthy">G. Krishnamoorthy</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Anandhakumar"> S. Anandhakumar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The effect of D-Lysine (D-Lys) on collagen with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide(EDC)/N-hydroxysuccinimide(NHS) initiated cross linking using experimental and modelling tools are evaluated. The results of the Coll-D-Lys-EDC/NHS scaffold also indicate an increase in the tensile strength (TS), percentage of elongation (% E), denaturation temperature (Td), and decrease the decomposition rate compared to L-Lys-EDC/NHS. Scanning electron microscopic (SEM) and atomic force microscopic (AFM) analyses revealed a well ordered with properly oriented and well-aligned structure of scaffold. The D-Lys stabilizes the scaffold against degradation by collagenase than L-Lys. The cell assay showed more than 98% fibroblast viability (NIH3T3) and improved cell adhesions, protein adsorption after 72h of culture when compared with native scaffold. Cell attachment after 74h was robust, with cytoskeletal analysis showing that the attached cells were aligned along the fibers assuming a spindle-shape appearance, despite, gene expression analyses revealed no apparent alterations in mRNA levels, although cell proliferation was not adversely affected. D-Lysine (D-Lys) plays a pivotal role in the self-assembly and conformation of collagen ﬁbrils. The D-Lys assisted EDC/NHS initiated cross-linking induces the formation of an carboxamide by the activation of the side chain -COOH group, followed by aminolysis of the O-iso acylurea intermediates by the -NH2 groups are directly joined via an isopeptides bond. This leads to the formation of intra- and inter-helical cross links. Modeling studies indicated that D-Lys bind with collagen-like peptide (CLP) through multiple H-bonding and hydrophobic interactions. Orientational changes in collagenase on CLP-D-Lys are observed which may decrease its accessibility to degradation and stabilize CLP against the action of the former. D-Lys has lowest binding energy and improved fibrillar-assembly and staggered alignment without the undesired structural stiffness and aggregations. The proteolytic machinery is not well equipped to deal with Coll-D-Lys than Coll-L-Lys scaffold. The information derived from the present study could help in designing collagenolytically stable heterochiral collagen based scaffold for biomedical applications. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=collagenase" title=" collagenase"> collagenase</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen%20like%20peptide" title=" collagen like peptide"> collagen like peptide</a>, <a href="https://publications.waset.org/abstracts/search?q=D-lysine" title=" D-lysine"> D-lysine</a>, <a href="https://publications.waset.org/abstracts/search?q=heterochiral%20collagen%20scaffold" title=" heterochiral collagen scaffold"> heterochiral collagen scaffold</a> </p> <a href="https://publications.waset.org/abstracts/34488/d-lysine-assisted-1-ethyl-3-3-dimethylaminopropylcarbodiimide-n-hydroxy-succinimide-initiated-crosslinked-collagen-scaffold-with-controlled-structural-and-surface-properties" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/34488.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">391</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">193</span> Collagen Scaffold Incorporated with Macrotyloma uniflorum Plant Extracts as a–Burn/Wound Dressing Material, in Vitro and in Vivo Evaluation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Thangavelu%20Muthukumar">Thangavelu Muthukumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Thotapalli%20Parvathaleswara%20Sastry"> Thotapalli Parvathaleswara Sastry</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Collagen is the most abundantly available connective tissue protein, which is being used as a biomaterial for various biomedical applications. Presently, fish wastes are disposed improperly which is causing serious environmental pollution resulting in offensive odour. Fish scales are promising source of Type I collagen. Medicinal plants have been used since time immemorial for treatment of various ailments of skin and dermatological disorders especially cuts, wounds, and burns. Developing biomaterials from the natural sources which are having wound healing properties within the search of a common man is the need of hour, particularly in developing and third world countries. With these objectives in view we have developed a wound dressing material containing fish scale collagen (FSC) incorporated with Macrotyloma uniflorum plant extract (PE). The wound dressing composite was characterized for its physiochemical properties using conventional methods. SEM image revealed that the composite has fibrous and porous surface which helps in transportation of oxygen as well as absorbing wound fluids. The biomaterial has shown 95% biocompatibility with required mechanical strength and has exhibited antimicrobial properties. This biomaterial has been used as a wound dressing material in experimental wounds of rats. The healing pattern was evaluated by macroscopic observations, panimetric studies, biochemical, histopathological observations. The results showed faster healing pattern in the wounds treated with CSPE compared to the other composites used in this study and untreated control. These experiments clearly suggest that CSPE can be used as wound/burn dressing materials. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=wound%20dressing" title=" wound dressing"> wound dressing</a>, <a href="https://publications.waset.org/abstracts/search?q=Macrotyloma%20uniflorum" title=" Macrotyloma uniflorum"> Macrotyloma uniflorum</a>, <a href="https://publications.waset.org/abstracts/search?q=burn%20dressing" title=" burn dressing"> burn dressing</a> </p> <a href="https://publications.waset.org/abstracts/4243/collagen-scaffold-incorporated-with-macrotyloma-uniflorum-plant-extracts-as-a-burnwound-dressing-material-in-vitro-and-in-vivo-evaluation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/4243.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">417</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">192</span> A Constitutive Model of Ligaments and Tendons Accounting for Fiber-Matrix Interaction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ratchada%20Sopakayang">Ratchada Sopakayang</a>, <a href="https://publications.waset.org/abstracts/search?q=Gerhard%20A.%20Holzapfel"> Gerhard A. Holzapfel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this study, a new constitutive model is developed to describe the hyperelastic behavior of collagenous tissues with a parallel arrangement of collagen fibers such as ligaments and tendons. The model is formulated using a continuum approach incorporating the structural changes of the main tissue components: collagen fibers, proteoglycan-rich matrix and fiber-matrix interaction. The mechanical contribution of the interaction between the fibers and the matrix is simply expressed by a coupling term. The structural change of the collagen fibers is incorporated in the constitutive model to describe the activation of the fibers under tissue straining. Finally, the constitutive model can easily describe the stress-stretch nonlinearity which occurs when a ligament/tendon is axially stretched. This study shows that the interaction between the fibers and the matrix contributes to the mechanical tissue response. Therefore, the model may lead to a better understanding of the physiological mechanisms of ligaments and tendons under axial loading. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=constitutive%20model" title="constitutive model">constitutive model</a>, <a href="https://publications.waset.org/abstracts/search?q=fiber-matrix" title=" fiber-matrix"> fiber-matrix</a>, <a href="https://publications.waset.org/abstracts/search?q=hyperelasticity" title=" hyperelasticity"> hyperelasticity</a>, <a href="https://publications.waset.org/abstracts/search?q=interaction" title=" interaction"> interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=ligament" title=" ligament"> ligament</a>, <a href="https://publications.waset.org/abstracts/search?q=tendon" title=" tendon"> tendon</a> </p> <a href="https://publications.waset.org/abstracts/67881/a-constitutive-model-of-ligaments-and-tendons-accounting-for-fiber-matrix-interaction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/67881.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">299</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">191</span> Visualizing Matrix Metalloproteinase-2 Activity Using Extracellular Matrix-Immobilized Fluorescence Resonance Energy Transfer Bioprobe in Cancer Cells</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hawon%20Lee">Hawon Lee</a>, <a href="https://publications.waset.org/abstracts/search?q=Young-Pil%20Kim"> Young-Pil Kim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Visualizing matrix metalloproteinases (MMPs) activity is necessary for understanding cancer metastasis because they are implicated in cell migration and invasion by degrading the extracellular matrix (ECM). While much effort has been made to sense the MMP activity, but extracellularly long-term monitoring of MMP activity still remains challenging. Here, we report a collagen-bound fluorescent bioprobe for the detection of MMP-2 activity in the extracellular environment. This bioprobe consists of ECM-immobilized part (including collagen-bound protein) and MMP-sensing part (including peptide substrate linked with fluorescence resonance energy transfer (FRET) coupler between donor green fluorescent protein (GFP) and acceptor TAMRA dye), which was constructed through intein-mediated self-splicing conjugation. Upon being immobilized on the collagen-coated surface, this bioprobe enabled efficient long-lasting observation of MMP-2 activity in the cultured cells without affecting cell growth and viability. As a result, the FRET ratio (acceptor/donor) decreased as the MMP2 activity increased in cultured cancer cells. Furthermore, unlike wild-type MMP-2, mutated MMP-2 expression (Y580A in the hemopexin region) gave rise to lowering the secretion of MMP-2 in HeLa. Conclusively, our method is anticipated to find applications for tracing and visualizing enzyme activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=collagen" title="collagen">collagen</a>, <a href="https://publications.waset.org/abstracts/search?q=ECM" title=" ECM"> ECM</a>, <a href="https://publications.waset.org/abstracts/search?q=FRET" title=" FRET"> FRET</a>, <a href="https://publications.waset.org/abstracts/search?q=MMP" title=" MMP"> MMP</a> </p> <a href="https://publications.waset.org/abstracts/72824/visualizing-matrix-metalloproteinase-2-activity-using-extracellular-matrix-immobilized-fluorescence-resonance-energy-transfer-bioprobe-in-cancer-cells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72824.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">202</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">190</span> The Glycitin and 38 Combination Inhibit the UV-Induced Wrinkle Fomation in Human Primary Fibroblast</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Manh%20Tin%20Ho">Manh Tin Ho</a>, <a href="https://publications.waset.org/abstracts/search?q=Phorl%20Sophors"> Phorl Sophors</a>, <a href="https://publications.waset.org/abstracts/search?q=Ga%20Young%20Seo"> Ga Young Seo</a>, <a href="https://publications.waset.org/abstracts/search?q=Young%20Mee%20Kim"> Young Mee Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Youngho%20Lim"> Youngho Lim</a>, <a href="https://publications.waset.org/abstracts/search?q=Moonjae%20Cho"> Moonjae Cho</a> </p> <p class="card-text"><strong>Abstract:</strong></p> UV radiation in sunlight is one of the most potential factor induced skin ageing and photocarcinogenesis. UV may induce the melanin production and wrinkle formation. Recently, the natural secondary compounds have been reported that had the beneficial protective effects from UV light. In this study, we investigated the effects of two different compounds, glycitin and 38, on human dermal fibroblast. We first only treated the 38 on melanocyte cell to test the proliferation inhibition of 38 on this cell line. Then, we induced the combination of glycitin and 38 on human dermal fibroblast in 48h and investigate the proliferation, collagen production and the metalloproteinase family expression. The 38 alone could inhibit the proliferation of melanocyte which indicated the reduction of melanin production. The combination of glycitin and 38 truly increased the fibroblast proliferation and even they could recover the UV-induced and H2O2-induced damaged fibroblast proliferation. The co-treatment also promoted the collagen IV expression significantly and accelerated the total collagen secretion. In addition, metalloproteinase (MMPs) family such as MMP1, MMP2, MMP7 was down-regulated in transcriptional level. In conclusion, the combination of glycitin and 38 has induced the fibroblast proliferation even when it was damaged by UV exposure and H2O2, whereas augmented collagen production and inhibited the MMPs caused the wrinkle formation and decreased the melanocyte proliferation, suggested an potential UV-protective therapy. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=UV%20radiation" title="UV radiation">UV radiation</a>, <a href="https://publications.waset.org/abstracts/search?q=wrinkle" title=" wrinkle"> wrinkle</a>, <a href="https://publications.waset.org/abstracts/search?q=ageing" title=" ageing"> ageing</a>, <a href="https://publications.waset.org/abstracts/search?q=glycitin" title=" glycitin"> glycitin</a>, <a href="https://publications.waset.org/abstracts/search?q=dermal%20fibroblast" title=" dermal fibroblast"> dermal fibroblast</a> </p> <a href="https://publications.waset.org/abstracts/12751/the-glycitin-and-38-combination-inhibit-the-uv-induced-wrinkle-fomation-in-human-primary-fibroblast" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/12751.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">237</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">189</span> Rapid and Easy Fabrication of Collagen-Based Biocomposite Scaffolds for 3D Cell Culture</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Esra%20Turker">Esra Turker</a>, <a href="https://publications.waset.org/abstracts/search?q=Umit%20Hakan%20Yildiz"> Umit Hakan Yildiz</a>, <a href="https://publications.waset.org/abstracts/search?q=Ahu%20Arslan%20Yildiz"> Ahu Arslan Yildiz</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The key of regenerative medicine is mimicking natural three dimensional (3D) microenvironment of tissues by utilizing appropriate biomaterials. In this study, a synthetic biodegradable polymer; poly (L-lactide-co-ε-caprolactone) (PLLCL) and a natural polymer; collagen was used to mimic the biochemical structure of the natural extracellular matrix (ECM), and by means of electrospinning technique the real physical structure of ECM has mimicked. PLLCL/Collagen biocomposite scaffolds enables cell attachment, proliferation and nutrient transport through fabrication of micro to nanometer scale nanofibers. Biocomposite materials are commonly preferred due to limitations of physical and biocompatible properties of natural and synthetic materials. Combination of both materials improves the strength, degradation and biocompatibility of scaffold. Literature studies have shown that collagen is mostly solved with heavy chemicals, which is not suitable for cell culturing. To overcome this problem, a new approach has been developed in this study where polyvinylpyrrolidone (PVP) is used as co-electrospinning agent. PVP is preferred due to its water solubility, so PLLCL/collagen biocomposite scaffold can be easily and rapidly produced. Hydrolytic and enzymatic biodegradation as well as mechanical strength of scaffolds were examined in vitro. Cell adhesion, proliferation and cell morphology characterization studies have been performed as well. Further, on-chip drug screening analysis has been performed over 3D tumor models. Overall, the developed biocomposite scaffold was used for 3D tumor model formation and obtained results confirmed that developed model could be used for drug screening studies to predict clinical efficacy of a drug. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biomaterials" title="biomaterials">biomaterials</a>, <a href="https://publications.waset.org/abstracts/search?q=3D%20cell%20culture" title=" 3D cell culture"> 3D cell culture</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20screening" title=" drug screening"> drug screening</a>, <a href="https://publications.waset.org/abstracts/search?q=electrospinning" title=" electrospinning"> electrospinning</a>, <a href="https://publications.waset.org/abstracts/search?q=lab-on-a-chip" title=" lab-on-a-chip"> lab-on-a-chip</a>, <a href="https://publications.waset.org/abstracts/search?q=tissue%20engineering" title=" tissue engineering"> tissue engineering</a> </p> <a href="https://publications.waset.org/abstracts/84837/rapid-and-easy-fabrication-of-collagen-based-biocomposite-scaffolds-for-3d-cell-culture" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/84837.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">312</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">188</span> Characterization of Natural Polymers for Guided Bone Regeneration Applications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Benedetta%20Isella">Benedetta Isella</a>, <a href="https://publications.waset.org/abstracts/search?q=Aleksander%20Drinic"> Aleksander Drinic</a>, <a href="https://publications.waset.org/abstracts/search?q=Alissa%20Heim"> Alissa Heim</a>, <a href="https://publications.waset.org/abstracts/search?q=Phillip%20Czichowski"> Phillip Czichowski</a>, <a href="https://publications.waset.org/abstracts/search?q=Lisa%20Lauts"> Lisa Lauts</a>, <a href="https://publications.waset.org/abstracts/search?q=Hans%20Leemhuis"> Hans Leemhuis</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Introduction: Membranes for guided bone regeneration are essential to perform a barrier function between the soft and the regenerating bone tissue. Bioabsorbable membranes are desirable in this field as they do not require a secondary surgery for removal, decreasing patient surgical risk. Collagen was the first bioabsorbable alternative introduced on the market, but its degradation time may be too fast to guarantee bone regeneration, and optimisation is needed. Silk fibroin, being biocompatible, slowly bioabsorbable, and processable into different scaffold types, could be a promising alternative. Objectives: The objective is to compare the general performance of a silk fibroin membrane for guided bone regeneration to current collagen alternatives developing suitable standardized tests for the mechanical and morphological characterization. Methods: Silk fibroin and collagen-based membranes were compared from the morphological and chemical perspective, with techniques such as SEM imaging and from the mechanical point of view with techniques such as tensile and suture retention strength (SRS) tests. Results: Silk fibroin revealed a high degree of reproducibility in surface density. The SRS of silk fibroin (0.76 ± 0.04 N), although lower than collagen, was still comparable to native tissues such as the internal mammary artery (0.56 N), and the same can be extended to general mechanical behaviour in tensile tests. The SRS could be increased by an increase in thickness. Conclusion: Silk fibroin is a promising material in the field of guided bone regeneration, covering the interesting position of not being considered a product containing cells or tissues of animal origin from the regulatory perspective and having longer degradation times with respect to collagen. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=guided%20bone%20regeneration" title="guided bone regeneration">guided bone regeneration</a>, <a href="https://publications.waset.org/abstracts/search?q=mechanical%20characterization" title=" mechanical characterization"> mechanical characterization</a>, <a href="https://publications.waset.org/abstracts/search?q=membrane" title=" membrane"> membrane</a>, <a href="https://publications.waset.org/abstracts/search?q=silk%20fibroin" title=" silk fibroin"> silk fibroin</a> </p> <a href="https://publications.waset.org/abstracts/187400/characterization-of-natural-polymers-for-guided-bone-regeneration-applications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/187400.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">42</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">187</span> Egg Yolk Peptide Stimulated Osteogenic Gene Expression</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hye%20Kyung%20Kim">Hye Kyung Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Myung-Gyou%20Kim"> Myung-Gyou Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Kang-Hyun%20Leem"> Kang-Hyun Leem </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Postmenopausal osteoporosis is characterized by low bone density which leads to increased bone fragility and greater susceptibility to fracture. Current treatments for osteoporosis are dominated by drugs that inhibit bone resorption although they also suppress bone formation that may contribute to pathogenesis of osteonecrosis. To restore the extensive bone loss, there is a great need for anabolic treatments that induce osteoblasts to build new bone. Pre-osteoblastic cells produce proteins of the extra-cellular matrix, including type I collagen at first, and then to successively produce alkaline phosphatase (ALP) and osteocalcin during differentiation to osteoblasts. Finally, osteoblasts deposit calcium. Present study investigated the effects of egg yolk peptide (EYP) on osteogenic activities and bone matrix gene expressions in human osteoblastic MG-63 cells. The effects of EYP on cell proliferation, alkaline phosphatase (ALP) activity, collagen synthesis, and mineralization were measured. The expression of osteogenic genes including COL1A1 (collagen, type I, alpha 1), ALP, BGLAP (osteocalcin), and SPP1 (secreted phosphoprotein 1, osteopontin) were measured by quantitative realtime PCR. EYP dose-dependently increased MG-63 cell proliferation, ALP activity, collagen synthesis, and calcium deposition. Furthermore, COL1A1, ALP, and SPP1 gene expressions were increased by EYP treatment. Present study suggested that EYP treatment enhanced osteogenic activities and increased bone matrix osteogenicgenes. These results could provide a mechanistic explanation for the bone-strengthening effects of EYP. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=egg%20yolk%20peptide" title="egg yolk peptide">egg yolk peptide</a>, <a href="https://publications.waset.org/abstracts/search?q=osteoblastic%20MG-63%20cells" title=" osteoblastic MG-63 cells"> osteoblastic MG-63 cells</a>, <a href="https://publications.waset.org/abstracts/search?q=alkaline%20phosphatase" title=" alkaline phosphatase"> alkaline phosphatase</a>, <a href="https://publications.waset.org/abstracts/search?q=collagen%20synthesis" title=" collagen synthesis"> collagen synthesis</a>, <a href="https://publications.waset.org/abstracts/search?q=osteogenic%20genes" title=" osteogenic genes"> osteogenic genes</a>, <a href="https://publications.waset.org/abstracts/search?q=COL1A1" title=" COL1A1"> COL1A1</a>, <a href="https://publications.waset.org/abstracts/search?q=osteocalcin" title=" osteocalcin"> osteocalcin</a>, <a href="https://publications.waset.org/abstracts/search?q=osteopontin" title=" osteopontin"> osteopontin</a> </p> <a href="https://publications.waset.org/abstracts/11286/egg-yolk-peptide-stimulated-osteogenic-gene-expression" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/11286.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">388</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=collagen&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=collagen&page=3">3</a></li> <li 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