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Integrins in Cancer: From Cell Adhesion to Metastasis – Cancer Science
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format-standard has-post-thumbnail hentry category-cancer tag-cancer tag-cell-adhesion tag-cell-migration tag-extracellular-matrix tag-integrin-inhibitors tag-integrins tag-metastasis tag-tumor-microenvironment tag-tumor-progression" itemtype="https://schema.org/CreativeWork" itemscope> <div class="inside-article"> <div class="featured-image page-header-image-single "> <img width="1200" height="628" src="https://cancerscience.net/archive/wp-content/uploads/2024/10/cancer-scaled-e1728128560418.jpg" class="attachment-full size-full" alt="" itemprop="image" decoding="async" fetchpriority="high" /> </div> <header class="entry-header"> <h1 class="entry-title" itemprop="headline">Integrins in Cancer: From Cell Adhesion to Metastasis</h1> <div class="entry-meta"> <span class="posted-on"><time class="entry-date published" datetime="2024-10-05T17:13:07+05:30" itemprop="datePublished">October 5, 2024</time></span> <span class="byline">by <span class="author vcard" itemprop="author" itemtype="https://schema.org/Person" itemscope><a class="url fn n" href="https://cancerscience.net/archive/author/cancerscience/" title="View all posts by cancerscience" rel="author" itemprop="url"><span class="author-name" itemprop="name">cancerscience</span></a></span></span> </div> </header> <div class="entry-content" itemprop="text"> <h3 style="text-align: left;"><b>Introduction</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">Cancer is a complex and fatal disease involving abnormal growth of cells; it can spread and infiltrate other organs and tissues as well. Of these processes, a central core is formed that is defined by the relationship between the cancer cells and the microenvironment. Integrins are believed to be one of the most important molecules implicated in such interactions. Integrins are a family of transmembrane proteins that enable the cell to adhere to the ECM and transmit signals within the cell that regulate cell survival, differentiation, and motility. Concerning cancer, integrins have been identified in increasing evidence as significant participants in tumor progression and metastasis. In this article, the authors describe the multiple functions of integrins in cancer, starting with the simple concept of cell adhesion and moving up to the triggering of metastasis.</span></p> <h3 style="text-align: left;"><b>Integrins: Structure and Function</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">Integrins are extracellular transmembrane proteins with α and β subunits, also known as integrin a and b subunits. The integrin receptors are composed of these subunits in different combinations and each of them has different binding specificities for ligands. For the most part, integrins are transmembrane proteins that act as cell adhesion receptors and bind to ECM molecules like fibronectin, collagen, as well as laminin. Apart from their ability to bind, integrins are also identified as bi-directional signaling platforms. They convey signals from the ECM to the cell, so-called outside-in signaling and vice versa, inside-out signaling, and are involved in the control of many cellular functions, including migration, cell survival, and differentiation.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">However, this evidence explains that integrins are involved in normal tissue architecture. Integrins in healthy tissues are involved in the maintenance of the tissues’ cohesiveness as well as their ability to respond to the ECM. However, in cancer cells, these receptors are abnormally expressed, and the cell responses that they meditate on change and actively participate in tumor formation and cancer spread.</span></p> <h3 style="text-align: left;"><b>Integrins in Tumor progression</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">In the following sections, it has been described how integrins can promote tumor progression and metastasis. Among the strategies by which they do this is by promoting the survival chances of cancer cells. For instance, integrin α6β4 induces carcinoma cell’s resistance to apoptosis. This integrin plays a role in signaling a cascade that enables cancer cells to live despite their shakiness, for instance, due to hypoxia or lack of nutrients. It is, however, important during the initial stages of tumorigenesis when cells are under stress to survive the hostile tumor environment.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">Besides cell survival, integrins also support the process of cancer cells’ division. Integrins binding with ECM proteins, including laminin-5 and fibronectin, can stimulate pathways like MAPK/ERK, which mediate cell cycle advancement and cell division. This is not only observed at the primary tumor site but is highly significant for the metastatic tumor formation at distal sites.</span></p> <p></div></div> <div style="background: #f7f7f7;border: 1px solid rgba(0, 0, 0, 0.07);"> <div style="padding: 30px;"><div class="Adblock-main"> <div class="Adblock-head"> <h2>Yearwise Publication Trend on <b>“<a href="https://cancerscience.net/publication-trends/index/cancer" target="_blank" title="cancer - yearwise publication trends">cancer</a>”</b></h2> </div> </div><div class="results-container"><div class="chart-block" style="padding:15px;"> <div class="left"> <div id="results" class="results"></div> </div> <div class="right"> <div class="chart-container"><canvas id="publicationChart"></canvas></div> </div> <div class="keywordsdiv"> <div style="text-align:center;"><b>Find publication trends on relevant topics</b> </div> <span class="gp-icon icon-tags"><svg viewBox="0 0 512 512" aria-hidden="true" xmlns="http://www.w3.org/2000/svg" width="1em" height="1em"><path d="M20 39.5c-8.836 0-16 7.163-16 16v176c0 4.243 1.686 8.313 4.687 11.314l224 224c6.248 6.248 16.378 6.248 22.626 0l176-176c6.244-6.244 6.25-16.364.013-22.615l-223.5-224A15.999 15.999 0 00196.5 39.5H20zm56 96c0-13.255 10.745-24 24-24s24 10.745 24 24-10.745 24-24 24-24-10.745-24-24z"></path><path d="M259.515 43.015c4.686-4.687 12.284-4.687 16.97 0l228 228c4.686 4.686 4.686 12.284 0 16.97l-180 180c-4.686 4.687-12.284 4.687-16.97 0-4.686-4.686-4.686-12.284 0-16.97L479.029 279.5 259.515 59.985c-4.686-4.686-4.686-12.284 0-16.97z"></path></svg></span> <span id="keyword-stats"></span> </div> </div></div></div><div class="inside-article"><style> table { margin: 0 0 1.5em; 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'NA' : count; tableHTML += ` <tr> <td>${year}</td> <td>${displayCount}</td> </tr> `; }); tableHTML += '</table></div>'; resultsContainer.innerHTML = tableHTML; } function displayLineChart(statistics) { var years = Object.keys(statistics); var counts = Object.values(statistics); var ctx = document.getElementById('publicationChart').getContext('2d'); // Destroy existing chart instance if it exists if (chart !== null) { chart.destroy(); } // Create a new chart instance chart = new Chart(ctx, { type: 'line', data: { labels: years, datasets: [{ label: 'Publication Counts', data: counts, fill: false, borderColor: 'rgba(75, 192, 192, 1)', tension: 0.1 }] }, options: { scales: { y: { beginAtZero: true } }, plugins: { legend: { display: true, position: 'top' } } } }); } function displayKeywordStats(keywords) { var resultsContainer = document.getElementById('keyword-stats'); resultsContainer.innerHTML = ''; if (!keywords || keywords.length === 0) { resultsContainer.innerHTML = '<p>No data found.</p>'; return; } var keywordHTML = ''; keywords.forEach((key, index) => { let key_replace = key.replace(/ /g, '-'); key_replace = key_replace.toLowerCase(); keywordHTML += `<a href="https://cancerscience.net/publication-trends/index/${key_replace}" target="_blank" title="${key} - yearwise publication trends">${key}</a>`; if (index < keywords.length - 1) { keywordHTML += ', '; } }); resultsContainer.innerHTML = keywordHTML; } // Call the function with the PHP data var statistics = { "2014": 66840, "2015": 61469, "2016": 73480, "2017": 76541, "2018": 81798, "2019": 96895, "2020": 120093, "2021": 134618, "2022": 158304, "2023": 257686, "2024": 81109 }; var keywordsArray = ["Integrins","cancer","cell adhesion","metastasis","tumor progression","extracellular matrix","integrin inhibitors","cell migration","tumor microenvironment"]; displayResults(statistics); displayLineChart(statistics); displayKeywordStats(keywordsArray); </script></p> <h3 style="text-align: left;"><b>Integrins and Tumor Invasion</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">As is one of the characteristic features of most cancers, local infiltration through invasion into surrounding tissues involves integrins significantly. </span><span style="font-weight: 400;">Cell adhesion and movement through Integrin receptors for cell adhesion or ECM components are critical components of cell invasion in or out of tumor mass. Several of the subunits, including α6β4 and αvβ3, have been shown to enhance cell movement and invasiveness since they interact with ECM proteins and also activate intracellular signaling pathways that modulate cytoskeleton movements.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">For example, Integrin α6β4 increases the expression of metastasis-promoting factors such as S100A4, which in turn improves the invasive capability of carcinoma cells. This integrin can engage and activate Src kinase; p125FAK is phosphorylated at Y 397, followed by activation of all downstream molecules that result in cell migration and invasive abilities. However, integrin αvβ3 is overexpressed in several human cancers and has been found to mediate the tumor cell invasiveness by stimulating MM’s and consequently causing degradation of the ECM.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">This is further amplified by the function of integrins to adjust the tumor microenvironment, making invasion additional efficient. Integrins are also capable of attracting and stimulating different types of stromal cells, such as fibroblasts and immune cells, to the site of the tumor. In response to cancer-associated signals, these stromal cells release molecules that alter the properties of the ECM to promote cancer cell invasion.</span></p> <h3 style="text-align: left;"><b>Integrins in Metastasis</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">Invasion is the ability of the cells that constitute the primary tumor to penetrate through the surrounding basement membrane, while intravasation implies entry of the cells into the blood or lymphatics, and the subsequent colonization of new sites through extravasation is called metastasis; this process is the main cause of the deaths due to cancer. Since integrins participate in nearly every step of the metastatic cascade, they have been blamed for cancer detachment, invasive cancer cell proliferation, residence in foreign tissues, and angiogenesis.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">In the early steps of metastasis, cancer cells have to break away from the primary tumor mass, which incorporates the down-regulation of cell adhesion molecules and up-regulation of integrins that adhere to the ECM. Integrin αvβ3, for instance, is highly expressed in metastatic cancer cells and allows cell detachment through the activation of MMP that degrades ECM components.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">Even as cancer cells get into circulation, integrin is still instrumental in tumor cell survival and migration to distant tissues. Of these, it found that alpha 6 beta 4 enhanced the ability of CTCs to survive and activate signaling cascades that led to cell survival. In addition, other adhesion receptors like integrin αvβ3 and α4β1 help in the attachment of circulating tumor cells to endothelial cells of the blood vessels, which is essential for extravasation and formation of secondary tumor colonies.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">Integrins are also involved in the colonization of distant organs through the regulation of the relationship between tumor cells and the surrounding environment. For example, integrin αvβ3 that is presented on the tumor cell membrane can attach to ECM elements in the particular area of bone marrow and contribute to the formation of bone metastases. Second, integrins can mobilize and activate local stroma cells to secure a proper microenvironment for the implantation and growth of metastases.</span></p> <p></div></div> <div style="background: #f7f7f7;border: 1px solid rgba(0, 0, 0, 0.07);"> <div style="padding: 30px;"><div class="Adblock-main"> <div class="Adblock-head"> <h2>Recent Publications on <b>“<a href="https://cancerscience.net/recent-publications/index/cancer" target="_blank" rel="noopener" title="cancer - yearwise publication list">cancer</a>”</b></h2> </div> </div> <div class="pb-main"><div class="article-scroll"><div id="results_recent" class="results"></div></div><div class="keywordsdiv" style="margin: 0px 15px;margin-top:20px;"> <div style="text-align:center;"><b>Find publications on relevant topics</b> </div> <span class="gp-icon icon-tags"><svg viewBox="0 0 512 512" aria-hidden="true" xmlns="http://www.w3.org/2000/svg" width="1em" height="1em"><path d="M20 39.5c-8.836 0-16 7.163-16 16v176c0 4.243 1.686 8.313 4.687 11.314l224 224c6.248 6.248 16.378 6.248 22.626 0l176-176c6.244-6.244 6.25-16.364.013-22.615l-223.5-224A15.999 15.999 0 00196.5 39.5H20zm56 96c0-13.255 10.745-24 24-24s24 10.745 24 24-10.745 24-24 24-24-10.745-24-24z"></path><path d="M259.515 43.015c4.686-4.687 12.284-4.687 16.97 0l228 228c4.686 4.686 4.686 12.284 0 16.97l-180 180c-4.686 4.687-12.284 4.687-16.97 0-4.686-4.686-4.686-12.284 0-16.97L479.029 279.5 259.515 59.985c-4.686-4.686-4.686-12.284 0-16.97z"></path></svg></span> <span id="keyword-papers"></span> </div></div></div><div class="inside-article"> <style> .pb-main{ border: solid 1px #ccc; border-top: none; margin-bottom: 20px; padding-bottom: 25px; background:#fff; } .author-main { border: solid 1px #ccc; border-top: none; margin-bottom: 20px; padding-bottom: 25px; background:#fff; } .publication-block { padding: 10px; margin-bottom: 10px; background-color: #f9f9f9; text-align: left; background: #FFF; border-bottom: solid 1px #ccc; margin-left: 15px; margin-right: 15px; } .publication-block h3 { margin: 0 0 10px; color: #000!important; } .publication-block a { font-size: 16px !important; line-height: 1em; font-weight: 600; text-transform: none; color: #000; padding: 0px; } .publication-block a:hover{ color: #227cdc; text-decoration:underline; } .article-scroll { max-height: 445px; overflow-y: auto; overflow-x: hidden; } ::-webkit-scrollbar-track { -webkit-box-shadow: inset 0 0 6px rgba(0,0,0,0.3); background-color: #efefef; border-radius:30px; } ::-webkit-scrollbar { width: 6px; background-color: #efefef; border-radius:30px; } ::-webkit-scrollbar-thumb { background-color: #ababab; border-radius:30px; } .publication-block p { margin-bottom: .5em; font-size: 15px; color: #000; } h3 { font-size: 18px !important; margin-bottom: 20px; line-height: 1.2em; font-weight: 600; text-transform: none; } a { padding: 5px; color: #a71c49; } #keyword-papers{ margin-top: 20px; text-align: center; } </style> <script> function displayResults_recent(papers) { var resultsContainer = document.getElementById('results_recent'); if (!papers || papers.length === 0) { resultsContainer.innerHTML = '<p>No recent publications found.</p>'; return; } papers.forEach(paper => { var publicationBlock = document.createElement('div'); publicationBlock.className = 'publication-block'; var publicationHTML = ` <div style="margin-bottom: 10px;line-height: 24px;"><a href="${paper.url}" target="_blank" title="${paper.title}">${paper.title}</a></div> <p><strong>Issue Release:</strong> ${paper.publishedDate}</p> `; publicationBlock.innerHTML = publicationHTML; resultsContainer.appendChild(publicationBlock); }); } function displayKeywordPapers(keywords) { var resultsContainer = document.getElementById('keyword-papers'); resultsContainer.innerHTML = ''; if (!keywords || keywords.length === 0) { resultsContainer.innerHTML = '<p>No data found.</p>'; return; } var keywordHTML = ''; keywords.forEach((key, index) => { let key_replace = key.replace(/ /g, '-'); key_replace = key_replace.toLowerCase(); keywordHTML += `<a href="https://cancerscience.net/recent-publications/index/${key_replace}" target="_blank" title="${key} - publication list">${key}</a>`; if (index < keywords.length - 1) { keywordHTML += ', '; } }); resultsContainer.innerHTML = keywordHTML; } // Call the function with the PHP data var recent_papers = [ { "title": "Dark force rising: Reawakening and targeting of fetal-like stem cells in colorectal cancer.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38787726", "publishedDate": "2024" }, { "title": "Relationship Between Preoperative Nutritional Indicators and Postoperative Complications in Patients with Oesophageal Cancer: A Meta-Analysis.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38764305", "publishedDate": "2024" }, { "title": "Molecular profile of driver genes in lung adenocarcinomas of Brazilian patients who have never smoked: implications for targeted therapies.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38944844", "publishedDate": "2024" }, { "title": "Development of a bioluminescent homogenous nanobody-based immunoassay for the detection of prostate-specific antigen (PSA).", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38944901", "publishedDate": "2024" }, { "title": "NUAK2 Inhibitors, KHKI-01128 and KHKI-01215, Exhibit Potent Anticancer Activity Against SW480 Colorectal Cancer Cells.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38925848", "publishedDate": "2024" }, { "title": "Discovery and validation of combined biomarkers for the diagnosis of esophageal intraepithelial neoplasia and esophageal squamous cell carcinoma.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38925350", "publishedDate": "2024" }, { "title": "A self-immobilizing near-infrared fluorogenic probe for in vivo imaging of fibroblast activation protein-\u03b1.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38944939", "publishedDate": "2024" }, { "title": "Colon cancer-associated transcript 1 (CCAT1): A potential novel target in cancer therapy.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38945528", "publishedDate": "2024" }, { "title": "Adverse selection and network design under regulated plan prices: Evidence from Medicaid.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38944945", "publishedDate": "2024" }, { "title": "[Pharmacological properties and clinical development overview of pertuzumab (genetical recombination), trastuzumab (genetical recombination) and vorhyaluronidase alfa (genetical recombination) (PHESGO combination for \u200dsubcutaneous injection MA, IN)].", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38945908", "publishedDate": "2024" }, { "title": "Recent advances and molecular mechanisms of TGF-\u03b2 signaling in colorectal cancer, with focus on bioactive compounds targeting.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38945700", "publishedDate": "2024" }, { "title": "Subdivision of pT1N0 (American Joint Committee on Cancer 8th edition) distal cholangiocarcinoma for adjuvant chemotherapy consideration.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946012", "publishedDate": "2024" }, { "title": "14-3-3 Family of Proteins: Biological Implications, Molecular Interactions, and Potential Intervention in Cancer, Virus and Neurodegeneration Disorders.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946063", "publishedDate": "2024" }, { "title": "WGCNA reveals a biomarker for cancer-associated fibroblasts to predict prognosis in cervical cancer.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946034", "publishedDate": "2024" }, { "title": "The impact of hysterectomy on subsequent colonoscopy in women with Lynch Syndrome.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946231", "publishedDate": "2024" }, { "title": "From balance to imbalance: disruption of plasma glutathione concentration in micropapillary thyroid carcinoma.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946003", "publishedDate": "2024" }, { "title": "Maternal Substance Use and Childhood Cancer-Letter.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946317", "publishedDate": "2024" }, { "title": "Dense tumor-infiltrating lymphocytes (TILs) in liver metastasis from colorectal cancer are related to improved overall survival.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946284", "publishedDate": "2024" }, { "title": "A lateral flow assay strip for simultaneous detection of miRNA and exosomes in liver cancer.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946429", "publishedDate": "2024" }, { "title": "Retraction: Hepatoma cell-derived extracellular vesicles promote liver cancer metastasis by inducing the differentiation of bone marrow stem cells through microRNA-181d-5p and the FAK\/Src pathway.", "url": "https:\/\/pubmed.ncbi.nlm.nih.gov\/38946800", "publishedDate": "2024" } ]; var keywordsArray = ["Integrins","cancer","cell adhesion","metastasis","tumor progression","extracellular matrix","integrin inhibitors","cell migration","tumor microenvironment"]; displayResults_recent(recent_papers); displayKeywordPapers(keywordsArray); </script></p> <h3 style="text-align: left;"><b>Targeting Integrins in Cancer Therapy</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">Since integrins are involved in cancer progression and metastasis, they have also attracted much attention and developed to be therapeutic targets for cancer. Several therapeutic approaches have therefore been synthesized aiming at antagonizing the function of integrin; these include monoclonal antibodies, small molecule inhibitors, and peptides that prevent integrin ligand interactions.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">Cilengitide, an αvβ3, and αvβ5 integrin-binding cyclized peptide mimetic, has been described as a potential anti-cancer agent in previous reports. Cilengitide works by antagonizing specific integrins that promote tumor growth and metastasis; these effects are especially significant in cancers particularly dependent on these particular integrins. Clinical trials have also been done concerning the use of integrin inhibitors as an adjunct to chemotherapy and radiation therapy.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">The other method is the application of integrin-blocking antibodies. For example, the antibodies to integrin α6β4 decrease the invasiveness of cancer cells as well as the formation of tumors with metastatic properties. These antibodies target Integrin-mediated signal transduction pathways that are critical for tumor cell survival and motility.</span></p> <p style="text-align: left;"><span style="font-weight: 400;">However, there is some controversy about integrin-targeted therapies today: there are still several problems. This means that integrin signaling pathways can be redundant and plastic, and this flexibility is sufficient to create resistance to therapy because the inaccessible expression of further integrins can be activated. Furthermore, integrins are expressed in normal tissues, and this creates the issue of the side effects of integrin inhibitors.</span></p> <h3 style="text-align: left;"><b>Conclusion</b></h3> <p style="text-align: left;"><span style="font-weight: 400;">Integrins participate in the progression and metastasis of tumors by focusing on the relationship between tumor cells and their surrounding environment. From cell survival and proliferation to invasion and metastasis, integrins are implicated in every step in the development of cancer. They are involved in the regulation of these processes and, as such, make good targets for therapeutic intervention. </span><span style="font-weight: 400;">So, the research on integrin function in cancer and more advanced and selective therapies aimed at integrin may help to raise the efficiency of cancer treatment.</span></p> <p></p> <p><b>References</b></p> <ol> <li>Fukuda, K., Sugihara, E., Ohta, S., Izuhara, K., Funakoshi, T., Amagai, M. and Saya, H., 2015. <a href="https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0129704">Periostin is a key niche component for wound metastasis of melanoma.</a> <i>PloS one</i>, <i>10</i>(6), p.e0129704.</li> <li>Chang, Q., Bournazou, E., Sansone, P., Berishaj, M., Gao, S.P., Daly, L., Wels, J., Theilen, T., Granitto, S., Zhang, X. and Cotari, J., 2013. <a href="https://www.sciencedirect.com/science/article/pii/S1476558613800784">The IL-6/JAK/Stat3 feed-forward loop drives tumorigenesis and metastasis.</a> <i>Neoplasia</i>, <i>15</i>(7), pp.848-IN45.</li> <li>Kim, T.H., Kim, H.I., Soung, Y.H., Shaw, L.A. and Chung, J., 2009. <a href="https://aacrjournals.org/mcr/article/7/10/1605/181408/Integrin-6-4-Signals-Through-Src-to-Increase">Integrin (α6β4) signals through Src to increase expression of S100A4, a metastasis-promoting factor: implications for cancer cell invasion.</a> <i>Molecular Cancer Research</i>, <i>7</i>(10), pp.1605-1612.</li> <li>Chen, M., Sinha, M., Luxon, B.A., Bresnick, A.R. and O’Connor, K.L., 2009. <a href="https://www.jbc.org/article/S0021-9258(19)82164-6/fulltext">Integrin α6β4 controls the expression of genes associated with cell motility, invasion, and metastasis, including S100A4/metastasin.</a> <i>Journal of Biological Chemistry</i>, <i>284</i>(3), pp.1484-1494.</li> <li>Zhao, Y., Bachelier, R., Treilleux, I., Pujuguet, P., Peyruchaud, O., Baron, R., Clément-Lacroix, P. and Clézardin, P., 2007. <a href="https://aacrjournals.org/cancerres/article/67/12/5821/533044/Tumor-v-3-Integrin-Is-a-Therapeutic-Target-for">Tumor αvβ3 integrin is a therapeutic target for breast cancer bone metastases.</a> <i>Cancer research</i>, <i>67</i>(12), pp.5821-5830.</li> <li>Bäuerle, T., Komljenovic, D., Merz, M., Berger, M.R., Goodman, S.L. and Semmler, W., 2011. <a href="https://onlinelibrary.wiley.com/doi/abs/10.1002/ijc.25563">Cilengitide inhibits progression of experimental breast cancer bone metastases as imaged noninvasively using VCT, MRI and DCE‐MRI in a longitudinal in vivo study.</a> <i>International journal of cancer</i>, <i>128</i>(10), pp.2453-2462.</li> <li>Nikolopoulos, S.N., Blaikie, P., Yoshioka, T., Guo, W., Puri, C., Tacchetti, C. and Giancotti, F.G., 2005. <a href="https://www.tandfonline.com/doi/abs/10.1128/mcb.25.14.6090-6102.2005">Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-κB, causing defects in epidermal growth and migration.</a> <i>Molecular and cellular biology</i>, <i>25</i>(14), pp.6090-6102.</li> <li>Sroka, T.C., Marik, J., Pennington, M.E., Lam, K.S. and Cress, A.E., 2006. <a href="https://www.tandfonline.com/doi/abs/10.4161/cbt.5.11.3461">The minimum element of a synthetic peptide required to block prostate tumor cell migration.</a> <i>Cancer biology & therapy</i>, <i>5</i>(11), pp.1556-1562.</li> </ol> <p></div></div> <div style="background: #f7f7f7;border: 1px solid rgba(0, 0, 0, 0.07);"> <div style="padding: 30px;"><div class="Adblock-main"> <div class="Adblock-head"> <h2>Top Experts on “<b style="color:#000;font-size:22px;">cancer</b>“</h2> </div> </div><div class="author-main"><div id="results_author"></div><div style="text-align: center;"><a class="register-button" href="https://cancerscience.net/expert-search" target="_blank" rel="noopener">Find experts on any field</a></div></div><div class="inside-article" style="background: none;border: none;box-shadow: none;margin-top: -70px;"> <style> .author-block { padding: 15px; margin-bottom: 10px; text-align: left; font-size: 15px; line-height: 1.2; background: #FFF; border-bottom: solid 1px #ccc; margin-left: 15px; margin-right: 15px; } .author-block h3 { margin: 0 0 10px; color: #227cdc; } .author-block p { margin: 5px 0; } .author-b { display: flex; justify-content: space-between; flex-wrap: wrap; margin-bottom:10px; } .author-b .ainfo { flex: 1 1 30%; box-sizing: border-box; text-align: left; background: #dcdcdc; padding: 7px 14px; border-radius: 5px; margin-top: 3px; margin-right: 10px; } @media (max-width: 768px) { .author-b .ainfo { flex: 1 1 100%; margin: 10px 0; } } </style> <script> function displayResults_author(authors) { var resultsContainer = document.getElementById('results_author'); resultsContainer.innerHTML = ''; if (!authors || Object.keys(authors).length === 0) { resultsContainer.innerHTML = '<p>No authors found.</p>'; return; } Object.values(authors).slice(0, 10).forEach(author => { var authorBlock = document.createElement('div'); authorBlock.className = 'author-block'; 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