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Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells

<!DOCTYPE html> <html lang="en" xmlns:mml="http://www.w3.org/1998/Math/MathML"> <head> <meta charset="utf-8"> <meta http-equiv="x-ua-compatible" content="ie=edge"> <title>Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells</title> <!-- Canonical URL --> <link href="https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.059/html" rel="canonical"></link> <!-- Preload Montserrat Fonts --> <link rel="preload" href="/assets/fonts/montserrat-v15-latin-ext_cyrillic-ext-regular.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <link rel="preload" href="/assets/fonts/montserrat-v25-latin-ext_cyrillic-ext-500.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <link rel="preload" href="/assets/fonts/montserrat-v15-latin-ext_cyrillic-ext-700.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <!-- Preload Merriweather Fonts --> <link rel="preload" href="/assets/fonts/merriweather-v30-latin-ext_cyrillic-ext-300.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <link rel="preload" href="/assets/fonts/merriweather-v22-latin-ext_cyrillic-ext-regular.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <link rel="preload" href="/assets/fonts/merriweather-v22-latin-ext_cyrillic-ext-700.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <!-- Preload Font Awesome --> <link rel="preload" href="/assets/stylesheets/fontawesome.woff2" as="font" type="font/woff2" crossorigin="anonymous"> <link rel="stylesheet" media="all" href='/assets/stylesheets/b6e95bdbb24ddbf266cc002b318c24ac-bootstrap.purged.min.css' /> <link rel="stylesheet" media="all" href='/assets/stylesheets/230ba72a089443f5e6ff20c1fc822214-main.min.css' /> <link rel="stylesheet" media="all" href='/assets/stylesheets/13761c60ba5201f465803f3005ccd7ef-fontawesome-codes.css' /> <link rel="shortcut icon" type="image/x-icon" href='/assets/images/7ceceb5f0284fef9bd38295e9cda0098-favicon.ico' /> <link rel="alternate" hreflang="en" href="https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.059/html?lang=en" /> <link rel="alternate" hreflang="de" href="https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.059/html?lang=de" /> <link rel="alternate" hreflang="x-default" href="https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.059/html" /> <!--[if le IE 11]> <script nonce="ug51z5gt8GM14Qtj1BD9Gw==" src='/assets/javascripts/2568c6be22833eac0f750ff472b3caf0-polyfill.min.js'></script> <![endif]--> <link rel="schema.dcterms" href="http://purl.org/dc/terms/"> <meta name="dcterms.rightsHolder" content="Walter de Gruyter GmbH"> <meta name="dcterms.rights" content="De Gruyter expressly reserves the right to use all content for commercial text and data mining within the meaning of Section 44b of the German Copyright Act."> <link rel="dns-prefetch" href="https://www.google-analytics.com" /> <meta name="google" content="notranslate" /> <meta name="viewport" content="width=device-width, initial-scale=1" /> <meta name="description" content="We have previously shown that PTHrP(38–94) amide restrains growth and invasion in vitro , causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231, for which tumorigenesis was also attenuated in vivo . We have also demonstrated that mid-region PTHrP gains access to the nuclear compartment of these cells and displays DNA-binding properties in vitro by recognizing targets in both cellular chromatin and isolated oligonucleotides. Here, we examined whether PTHrP(38–94) amide was able to modulate gene expression of MDA-MB231 cells, employing a combination of conventional, differential display and semi-quantitative multiplex PCR techniques. The results obtained provide first evidence that PTHrP(38–94) amide can affect gene expression in tumor cells, identifying A4-differentiation protein/PLP2 as up-regulated, and HOX7/MSX1 , COX6C , FZD6 , OXR1 and TMCO4 as down-regulated genes in treated cells, and suggest that the cytotoxic activity of the peptide can be ascribed, at least in part, to such transcriptional reprogramming."/> <meta property="og:url" content="https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.059/html"/><meta property="og:site_name" content="De Gruyter"/><meta property="og:title" content="Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells"/><meta property="og:type" content="article"/><meta property="og:locale" content="en"/><meta property="og:image" content="https://www.degruyterbrill.com/document/cover/journal_key/BCHM/product"/><meta property="og:image:type" content="image/jpeg"/><meta property="og:description" content="We have previously shown that PTHrP(38–94) amide restrains growth and invasion in vitro , causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231, for which tumorigenesis was also attenuated in vivo . We have also demonstrated that mid-region PTHrP gains access to the nuclear compartment of these cells and displays DNA-binding properties in vitro by recognizing targets in both cellular chromatin and isolated oligonucleotides. Here, we examined whether PTHrP(38–94) amide was able to modulate gene expression of MDA-MB231 cells, employing a combination of conventional, differential display and semi-quantitative multiplex PCR techniques. The results obtained provide first evidence that PTHrP(38–94) amide can affect gene expression in tumor cells, identifying A4-differentiation protein/PLP2 as up-regulated, and HOX7/MSX1 , COX6C , FZD6 , OXR1 and TMCO4 as down-regulated genes in treated cells, and suggest that the cytotoxic activity of the peptide can be ascribed, at least in part, to such transcriptional reprogramming."/><meta property="og:locale:alternate" content="de"/><meta property="article:author" content="Rosalia Sirchia"/><meta property="article:author" content="Claudio Luparello"/><meta property="article:tag" content="breast cancer"/><meta property="article:tag" content="differential display"/><meta property="article:tag" content="gene expression"/><meta property="article:tag" content="PCR"/><meta property="article:tag" content="PTHrP"/><meta property="article:published_time" content="2007-05-01"/><meta property="article:section" content="Biological Chemistry"/> <meta name="citation_firstpage" content="457" /> <meta name="citation_lastpage" content="465" /> <meta name="citation_issue" content="5" /> <meta name="citation_issn" content="1437-4315" /> <meta name="citation_language" content='en' /> <meta name="citation_volume" content="388" /> <meta name="citation_publisher" content='De Gruyter' /> <meta name="citation_keywords" content='breast cancer; differential display; gene expression; PCR; PTHrP' /> <meta name="citation_author" content="Rosalia Sirchia" /> <meta name="citation_author" content="Claudio Luparello" /> <meta name="citation_title" content='Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells' /> <meta name="citation_xml_url" content="https://www.degruyterbrill.com/document/doi/10.1515/BC.2007.059/xml" /> <meta name="citation_journal_title" content="" /> <meta name="citation_publication_date" content='2007/05/01' /> <meta name="citation_doi" content="10.1515/BC.2007.059" /> <script type="application/ld+json">{"author":[{"@type":"Person","name":"Rosalia Sirchia"},{"@type":"Person","name":"Claudio Luparello"}],"editor":[],"audience":null,"datePublished":"2007-05-01","headline":"","keywords":"keyword,keyword,keyword,keyword,keyword","isAccessibleForFree":false,"publisher":{"@type":"Organization","name":"De Gruyter"},"@context":"https://schema.org","@type":"Article","name":"Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells","image":"https://www.degruyterbrill.com/document/cover/journal_key/BCHM/thumbnail","url":"https://doi.org/10.1515/BC.2007.059"}</script> <script nonce="ug51z5gt8GM14Qtj1BD9Gw=="> // Define dataLayer and the gtag function. window.dataLayer = window.dataLayer || []; function gtag(){dataLayer.push(arguments);} function getCookieValue(name){ const regex = new RegExp(`(^| )${name}=([^;]+)`) const match = document.cookie.match(regex) if (match) { return match[2] } } // Set default consent to 'denied' as a placeholder // Determine actual values based on your own requirements const acceptCookies = getCookieValue('acceptcookies') === "true"; const defaultSettings = (acceptCookies) => ({ 'ad_storage': acceptCookies ? 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protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells</h1> <div class="subtitle-dgb"></div> <ul class="contributors-dgb"> <li class="contributors-AUTHOR"> <span class="contributor-dgb"> <span class="displayName">Rosalia Sirchia</span> <contributor-popdown name="Rosalia Sirchia" position="1" email="" affiliations="Dipartimento di Biologia Cellulare e dello Sviluppo, Università di Palermo, I-90128 Palermo, Italy" > </contributor-popdown> </span> and <span class="contributor-dgb"> <span class="displayName">Claudio Luparello</span> <contributor-popdown name="Claudio Luparello" position="2" email="" affiliations="Dipartimento di Biologia Cellulare e dello Sviluppo, Università di Palermo, I-90128 Palermo, Italy" > </contributor-popdown> </span> </li> </ul> <div class="container-bottom-aligned"> <div class="publicationDate-dgb"> <span class="semibold-product-text">Published/Copyright:</span> <span class="normal-product-text">May 1, 2007</span> </div> </div> </div></div> </div> 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Gruyter' data-contentName='Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells' data-doi='10.1515/BC.2007.059' data-parentIdentifier='BCHM' data-parentName='Biological Chemistry' data-languages='en' ></div> <div class="modal" id="citationsModal" tabindex="-1" role="dialog" aria-label='Cite this' aria-hidden="true"> <div class="modal-dialog modal-dialog-centered modal-lg" role="document"> <div class="modal-content bg-white"> <div class="modal-body"> <button type="button" class="btn-close float-end btn-modal-close" data-bs-dismiss="modal" aria-label='Close'></button> <div id="citations"> <div class="row pb-2"> <div class="col"> <div class="text-dark fw-bold">Cite this article</div> </div> </div> <div class="row p-2"> <div class="col-lg-auto ps-4 mb-3 mb-lg-0"> <ul class="nav d-flex flex-lg-column" id="citationSelector" role="tablist"> <li class="nav-item py-1" role="presentation"> <a class="nav-link citations py-0 font-size-14 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"Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells" <i>Biological Chemistry</i>, vol. 388, no. 5, 2007, pp. 457-465. <a href='https://doi.org/10.1515/BC.2007.059'>https://doi.org/10.1515/BC.2007.059</a></div> <div class="tab-pane fade " id="APA" role="tabpanel" aria-labelledby="APA-tab">Sirchia, R. & Luparello, C. (2007). Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells. <i>Biological Chemistry</i>, <i>388</i>(5), 457-465. <a href='https://doi.org/10.1515/BC.2007.059'>https://doi.org/10.1515/BC.2007.059</a></div> <div class="tab-pane fade " id="Harvard" role="tabpanel" aria-labelledby="Harvard-tab">Sirchia, R. and Luparello, C. (2007) Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells. Biological Chemistry, Vol. 388 (Issue 5), pp. 457-465. <a href='https://doi.org/10.1515/BC.2007.059'>https://doi.org/10.1515/BC.2007.059</a></div> <div class="tab-pane fade " id="Chicago" role="tabpanel" aria-labelledby="Chicago-tab">Sirchia, Rosalia and Luparello, Claudio. "Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells" <i>Biological Chemistry</i> 388, no. 5 (2007): 457-465. <a href='https://doi.org/10.1515/BC.2007.059'>https://doi.org/10.1515/BC.2007.059</a></div> <div class="tab-pane fade " id="Vancouver" role="tabpanel" aria-labelledby="Vancouver-tab">Sirchia R, Luparello C. Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells. <i>Biological Chemistry</i>. 2007;388(5): 457-465. <a href='https://doi.org/10.1515/BC.2007.059'>https://doi.org/10.1515/BC.2007.059</a></div> <div class="d-flex justify-content-center"><span id="citationCopied" aria-hidden="true">Copied to clipboard</span></div> </div> <div class="d-flex justify-content-between mt-2"> <div><a href="#" id="citationCopy" class="font-size-14">Copy to clipboard</a></div> <div> <span class="font-size-14">Download:</span> <a title='Download in BibTeX format' aria-label='Download in BibTeX format' class="ms-1 font-size-14" href="/document/doi/10.1515/BC.2007.059/machineReadableCitation/BibTeX">BibTeX</a> <a title='Download in EndNote format' aria-label='Download in EndNote format' class="ms-1 font-size-14" href="/document/doi/10.1515/BC.2007.059/machineReadableCitation/EndNote">EndNote</a> <a title='Download in RIS format' aria-label='Download in RIS format' class="ms-1 font-size-14" href="/document/doi/10.1515/BC.2007.059/machineReadableCitation/RIS">RIS</a> </div> </div> </div> </div> </div> </div> </div> </div> </div> <div class="abstract-container desktop"> <div id="text-container"> <div xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" xmlns:dgpm="http://degruyter.com/resources/fetched-pubmed-id" class="contentWrapper"><div class="article" lang="en"><div class="abstract"><h2 class="subheading">Abstract</h2><p>We have previously shown that PTHrP(38–94) amide restrains growth and invasion <em>in vitro</em>, causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231, for which tumorigenesis was also attenuated <em>in vivo</em>. We have also demonstrated that mid-region PTHrP gains access to the nuclear compartment of these cells and displays DNA-binding properties <em>in vitro</em> by recognizing targets in both cellular chromatin and isolated oligonucleotides. Here, we examined whether PTHrP(38–94) amide was able to modulate gene expression of MDA-MB231 cells, employing a combination of conventional, differential display and semi-quantitative multiplex PCR techniques. The results obtained provide first evidence that PTHrP(38–94) amide can affect gene expression in tumor cells, identifying <em>A4-differentiation protein/PLP2</em> as up-regulated, and <em>HOX7/MSX1</em>, <em>COX6C</em>, <em>FZD6</em>, <em>OXR1</em> and <em>TMCO4</em> as down-regulated genes in treated cells, and suggest that the cytotoxic activity of the peptide can be ascribed, at least in part, to such transcriptional reprogramming.</p></div><div class="keywords mb-3">Keywords: <a href="/search?query=keywordValues%3A%28%22breast%20cancer%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">breast cancer</a>; <a href="/search?query=keywordValues%3A%28%22differential%20display%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">differential display</a>; <a href="/search?query=keywordValues%3A%28%22gene%20expression%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">gene expression</a>; <a href="/search?query=keywordValues%3A%28%22PCR%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">PCR</a>; <a href="/search?query=keywordValues%3A%28%22PTHrP%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">PTHrP</a></div><section class="authorNotes"><hr></hr><div class="correspondingAuthor">Corresponding author <span xmlns:xlink="http://www.w3.org/1999/xlink" class="email" xlink:href="mailto:clupar@tin.it">clupar@tin.it</span></div><hr></hr></section><div class="contrib-group"></div><div class="publicationDates mb-3"><div class="receivedDate"><span class="label-received"><span><strong>Received: </strong></span></span>2006-11-30</div><div class="acceptedDate"><span class="label-accepted"><span><strong>Accepted: </strong></span></span>2007-2-14</div><div class="publishedOnlineDate"><span class="label-publishedOnline"><span><strong>Published Online: </strong></span></span>2007-05-01</div></div><div class="copyrightStatement"><p>©2007 by Walter de Gruyter Berlin New York</p></div></div></div> </div> </div> <div class="dgb-alert desktop" role="alert"> <div id="noAccessReasonSpinner"> <div class="spinner-border text-primary" role="status"></div> </div> <div id="noAccessReasonContent"> <div class="noAccessHeadline"> <span class="fa fas fa-block noAccessIcon"></span> <span class="noAccessTitle">You are currently not able to access this content.</span> </div> <span id="noAccessReason"></span> <div class="noAccessButtons"> <div class="dgb-iframe-container"> <iframe id="seamlessAccessButton" src="/seamlessaccess/button?live=true&amp;target=https%3A%2F%2Fwww.degruyterbrill.com%2Flogin%2Fcallback%3FredirectTarget%3D%252Fdocument%252Fdoi%252F10.1515%252FBC.2007.059%252Fhtml" title="Seamless access button iframe" class="dgb-seamless-access-iframe" scrolling="no"> </iframe> </div> </div> </div> </div> <section id="dgb-accordion" class="mobile-accordion"> <div class="dgb-accordion-item pdfView"> <h2 class="dgb-accordion-header"> <button class="dgb-accordion-button ga_journal_article_accordion" type="button" aria-expanded="false" data-target="#articleAbstractView"> Abstract </button> </h2> <div id="articleAbstractView" class="dgb-accordion-content"> <div class="abstract-container mobile"> <div id="text-container"> <div xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" xmlns:dgpm="http://degruyter.com/resources/fetched-pubmed-id" class="contentWrapper"><div class="article" lang="en"><div class="abstract"><h2 class="subheading">Abstract</h2><p>We have previously shown that PTHrP(38–94) amide restrains growth and invasion <em>in vitro</em>, causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231, for which tumorigenesis was also attenuated <em>in vivo</em>. We have also demonstrated that mid-region PTHrP gains access to the nuclear compartment of these cells and displays DNA-binding properties <em>in vitro</em> by recognizing targets in both cellular chromatin and isolated oligonucleotides. Here, we examined whether PTHrP(38–94) amide was able to modulate gene expression of MDA-MB231 cells, employing a combination of conventional, differential display and semi-quantitative multiplex PCR techniques. The results obtained provide first evidence that PTHrP(38–94) amide can affect gene expression in tumor cells, identifying <em>A4-differentiation protein/PLP2</em> as up-regulated, and <em>HOX7/MSX1</em>, <em>COX6C</em>, <em>FZD6</em>, <em>OXR1</em> and <em>TMCO4</em> as down-regulated genes in treated cells, and suggest that the cytotoxic activity of the peptide can be ascribed, at least in part, to such transcriptional reprogramming.</p></div><div class="keywords mb-3">Keywords: <a href="/search?query=keywordValues%3A%28%22breast%20cancer%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">breast cancer</a>; <a href="/search?query=keywordValues%3A%28%22differential%20display%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">differential display</a>; <a href="/search?query=keywordValues%3A%28%22gene%20expression%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">gene expression</a>; <a href="/search?query=keywordValues%3A%28%22PCR%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">PCR</a>; <a href="/search?query=keywordValues%3A%28%22PTHrP%22%29%20AND%20journalKey%3A%28%22BCHM%22%29&amp;documentVisibility=all&amp;documentTypeFacet=article" class="ga_keyword">PTHrP</a></div><section class="authorNotes"><hr></hr><div class="correspondingAuthor">Corresponding author <span xmlns:xlink="http://www.w3.org/1999/xlink" class="email" xlink:href="mailto:clupar@tin.it">clupar@tin.it</span></div><hr></hr></section><div class="contrib-group"></div><div class="publicationDates mb-3"><div class="receivedDate"><span class="label-received"><span><strong>Received: </strong></span></span>2006-11-30</div><div 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href="/document/doi/10.1515/BC.2007.054/html"> The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains </a> </li> <li class=" contentProductPageResult"> <a class="articleTocEntry" data-doi="10.1515/BC.2007.060" href="/document/doi/10.1515/BC.2007.060/html"> Two α subunits and one β subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish <em>Danio rerio</em> </a> </li> <li class=" contentProductPageResult"> <a class="articleTocEntry" data-doi="10.1515/BC.2007.055" href="/document/doi/10.1515/BC.2007.055/html"> Increase in kinins on post-exercise hypotension in normotensive and hypertensive volunteers </a> </li> <li class=" contentProductPageResult"> <a class="articleTocEntry" data-doi="10.1515/BC.2007.053" href="/document/doi/10.1515/BC.2007.053/html"> Inhibition of cathepsin L-like proteases by cathepsin V propeptide </a> </li> <li class=" contentProductPageResult"> <a 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