Pharmacological inhibition of the vitronectin receptor abrogates PDGF-BB-induced hepatic stellate cell migration and activation in vitro
Background/Aims Activated hepatic stellate cells (HSC) play a central role in the development of liver fibrosis. Platelet-derived growth factor (PDGF)-BB and the integrin αvβ3 mediate mesenchymal cell migration and proliferation. However, their contribution and interaction during fibrogenic activati...
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| Veröffentlicht in: | Journal of hepatology 2007-05, Vol.46 (5), p.878-887 |
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| creator | Patsenker, Eleonora Popov, Yury Wiesner, Matthias Goodman, Simon L Schuppan, Detlef |
| description | Background/Aims Activated hepatic stellate cells (HSC) play a central role in the development of liver fibrosis. Platelet-derived growth factor (PDGF)-BB and the integrin αvβ3 mediate mesenchymal cell migration and proliferation. However, their contribution and interaction during fibrogenic activation of HSC remains unclear. To this aim we investigated if PDFGF-BB and αvβ3 interact, and how far small molecular inhibitors of αvβ3 modulate PDGF-BB and serum-induced migration, proliferation and fibrogenic activation of HSC. Methods Rat and human HSC were subjected to migration and proliferation assays in the presence or absence of a peptide or a nonpeptide αvβ3 inhibitor. Activation of mitogen-activated protein kinases (ERK1/2, p38), Akt, focal adhesion kinase (FAK), paxillin and β3 integrin was evaluated by phospho-specific Western blotting. Fibrosis related transcripts were determined by quantitative real-time PCR. Results PDGF-BB-stimulated HSC migration which was blocked dose-dependently by the αvβ3 antagonists, with complete inhibition at 10−6 M. αvβ3 blockage did not affect cell viability or proliferation, while it decreased phosphorylation of FAK, paxillin, β3 integrin and p38, but not of ERK1/2 or Akt. αvβ3 inhibition led to downregulation of certain profibrogenic transcripts, while it upregulated fibrolytic MMP-13 mRNA. Conclusions Inhibition of integrin αvβ3 leads to abrogation of migration of HSC stimulated with PDGF-BB and to an antifibrogenic gene expression pattern. |
| doi_str_mv | 10.1016/j.jhep.2006.11.011 |
| format | Article |
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Platelet-derived growth factor (PDGF)-BB and the integrin αvβ3 mediate mesenchymal cell migration and proliferation. However, their contribution and interaction during fibrogenic activation of HSC remains unclear. To this aim we investigated if PDFGF-BB and αvβ3 interact, and how far small molecular inhibitors of αvβ3 modulate PDGF-BB and serum-induced migration, proliferation and fibrogenic activation of HSC. Methods Rat and human HSC were subjected to migration and proliferation assays in the presence or absence of a peptide or a nonpeptide αvβ3 inhibitor. Activation of mitogen-activated protein kinases (ERK1/2, p38), Akt, focal adhesion kinase (FAK), paxillin and β3 integrin was evaluated by phospho-specific Western blotting. Fibrosis related transcripts were determined by quantitative real-time PCR. Results PDGF-BB-stimulated HSC migration which was blocked dose-dependently by the αvβ3 antagonists, with complete inhibition at 10−6 M. αvβ3 blockage did not affect cell viability or proliferation, while it decreased phosphorylation of FAK, paxillin, β3 integrin and p38, but not of ERK1/2 or Akt. αvβ3 inhibition led to downregulation of certain profibrogenic transcripts, while it upregulated fibrolytic MMP-13 mRNA. Conclusions Inhibition of integrin αvβ3 leads to abrogation of migration of HSC stimulated with PDGF-BB and to an antifibrogenic gene expression pattern.</description><identifier>ISSN: 0168-8278</identifier><identifier>EISSN: 1600-0641</identifier><identifier>DOI: 10.1016/j.jhep.2006.11.011</identifier><identifier>PMID: 17258347</identifier><identifier>CODEN: JOHEEC</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>Akt ; Animals ; Antagonist ; Biological and medical sciences ; Cell Adhesion - drug effects ; Cell Adhesion - physiology ; Cell Movement - drug effects ; Cell Movement - physiology ; Cells, Cultured ; Cirrhosis ; Collagen ; CTGF ; Dose-Response Relationship, Drug ; Down-Regulation ; Erk ; FAK ; Fibrosis ; Focal Adhesion Kinase 1 - metabolism ; Gastroenterology and Hepatology ; Gastroenterology. Liver. Pancreas. Abdomen ; Gene expression ; Gene Expression Regulation - drug effects ; Hepatic stellate cell ; Hepatocytes - cytology ; Hepatocytes - drug effects ; Hepatocytes - metabolism ; Humans ; Inhibitor ; Integrin ; Integrin alphaVbeta3 - antagonists & inhibitors ; Integrin alphaVbeta3 - metabolism ; Liver ; Liver - cytology ; Liver - drug effects ; Liver - growth & development ; Liver - metabolism ; Liver. Biliary tract. Portal circulation. Exocrine pancreas ; Male ; Medical sciences ; Migration ; MMP ; Myofibroblast ; Nonpeptide ; Other diseases. Semiology ; p38 ; Paxillin ; Paxillin - metabolism ; PDGF-BB ; Peptides, Cyclic - pharmacology ; Phosphoproteins - metabolism ; Platelet-Derived Growth Factor - pharmacology ; Procollagen ; Proliferation ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Tyrosine Kinases - metabolism ; Proto-Oncogene Proteins c-sis ; Rats ; Rats, Wistar ; Receptor ; RNA, Messenger - genetics ; Signal transduction ; Signal Transduction - drug effects ; TGF beta ; TIMP-1 ; Vitronectin ; αvβ3</subject><ispartof>Journal of hepatology, 2007-05, Vol.46 (5), p.878-887</ispartof><rights>European Association for the Study of the Liver</rights><rights>2006 European Association for the Study of the Liver</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-30cfda52e9ac79035276cb5ca3b27af5386817341daf1e8d1f6d7dd60991ee793</citedby><cites>FETCH-LOGICAL-c505t-30cfda52e9ac79035276cb5ca3b27af5386817341daf1e8d1f6d7dd60991ee793</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0168827806006404$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18695780$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17258347$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Patsenker, Eleonora</creatorcontrib><creatorcontrib>Popov, Yury</creatorcontrib><creatorcontrib>Wiesner, Matthias</creatorcontrib><creatorcontrib>Goodman, Simon L</creatorcontrib><creatorcontrib>Schuppan, Detlef</creatorcontrib><title>Pharmacological inhibition of the vitronectin receptor abrogates PDGF-BB-induced hepatic stellate cell migration and activation in vitro</title><title>Journal of hepatology</title><addtitle>J Hepatol</addtitle><description>Background/Aims Activated hepatic stellate cells (HSC) play a central role in the development of liver fibrosis. Platelet-derived growth factor (PDGF)-BB and the integrin αvβ3 mediate mesenchymal cell migration and proliferation. However, their contribution and interaction during fibrogenic activation of HSC remains unclear. To this aim we investigated if PDFGF-BB and αvβ3 interact, and how far small molecular inhibitors of αvβ3 modulate PDGF-BB and serum-induced migration, proliferation and fibrogenic activation of HSC. Methods Rat and human HSC were subjected to migration and proliferation assays in the presence or absence of a peptide or a nonpeptide αvβ3 inhibitor. Activation of mitogen-activated protein kinases (ERK1/2, p38), Akt, focal adhesion kinase (FAK), paxillin and β3 integrin was evaluated by phospho-specific Western blotting. Fibrosis related transcripts were determined by quantitative real-time PCR. Results PDGF-BB-stimulated HSC migration which was blocked dose-dependently by the αvβ3 antagonists, with complete inhibition at 10−6 M. αvβ3 blockage did not affect cell viability or proliferation, while it decreased phosphorylation of FAK, paxillin, β3 integrin and p38, but not of ERK1/2 or Akt. αvβ3 inhibition led to downregulation of certain profibrogenic transcripts, while it upregulated fibrolytic MMP-13 mRNA. Conclusions Inhibition of integrin αvβ3 leads to abrogation of migration of HSC stimulated with PDGF-BB and to an antifibrogenic gene expression pattern.</description><subject>Akt</subject><subject>Animals</subject><subject>Antagonist</subject><subject>Biological and medical sciences</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Movement - drug effects</subject><subject>Cell Movement - physiology</subject><subject>Cells, Cultured</subject><subject>Cirrhosis</subject><subject>Collagen</subject><subject>CTGF</subject><subject>Dose-Response Relationship, Drug</subject><subject>Down-Regulation</subject><subject>Erk</subject><subject>FAK</subject><subject>Fibrosis</subject><subject>Focal Adhesion Kinase 1 - metabolism</subject><subject>Gastroenterology and Hepatology</subject><subject>Gastroenterology. Liver. Pancreas. Abdomen</subject><subject>Gene expression</subject><subject>Gene Expression Regulation - drug effects</subject><subject>Hepatic stellate cell</subject><subject>Hepatocytes - cytology</subject><subject>Hepatocytes - drug effects</subject><subject>Hepatocytes - metabolism</subject><subject>Humans</subject><subject>Inhibitor</subject><subject>Integrin</subject><subject>Integrin alphaVbeta3 - antagonists & inhibitors</subject><subject>Integrin alphaVbeta3 - metabolism</subject><subject>Liver</subject><subject>Liver - cytology</subject><subject>Liver - drug effects</subject><subject>Liver - growth & development</subject><subject>Liver - metabolism</subject><subject>Liver. Biliary tract. Portal circulation. Exocrine pancreas</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Migration</subject><subject>MMP</subject><subject>Myofibroblast</subject><subject>Nonpeptide</subject><subject>Other diseases. Semiology</subject><subject>p38</subject><subject>Paxillin</subject><subject>Paxillin - metabolism</subject><subject>PDGF-BB</subject><subject>Peptides, Cyclic - pharmacology</subject><subject>Phosphoproteins - metabolism</subject><subject>Platelet-Derived Growth Factor - pharmacology</subject><subject>Procollagen</subject><subject>Proliferation</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins c-sis</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Receptor</subject><subject>RNA, Messenger - genetics</subject><subject>Signal transduction</subject><subject>Signal Transduction - drug effects</subject><subject>TGF beta</subject><subject>TIMP-1</subject><subject>Vitronectin</subject><subject>αvβ3</subject><issn>0168-8278</issn><issn>1600-0641</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9klGL1DAQx4so3nr6BXyQvOhb66RpmxZE8E7vFA48UJ9Dmkx3U9tkL0kX7hv4sU1vFw588GkI_Oaf4TeTZa8pFBRo834sxh3uixKgKSgtgNIn2YY2ADk0FX2abRLU5m3J27PsRQgjADDoqufZGeVl3bKKb7I_tzvpZ6nc5LZGyYkYuzO9icZZ4gYSd0gOJnpnUUVjiUeF--g8kb13WxkxkNvP11f5xUVurF4UapJGktEoEiJOUyKISpXMZuvlQ6q0msgUdjg-U-jDBy-zZ4OcAr461fPs19WXn5df85vv198uP93kqoY65gzUoGVdYicV74DVJW9UXyvJ-pLLoWZt01LOKqrlQLHVdGg017qBrqOIvGPn2btj7t67uwVDFLMJ64jSoluC4MB4yXmdwPIIKu9C8DiIvTez9PeCglj9i1Gs_sXqX1Aqkv_U9OaUvvQz6seWk_AEvD0BMiTdg5dWmfDItU1X8xYS9-HIYXJxMOhFUAZtEmzSDqLQzvx_jo__tKvJ2HXBv_Eew-gWb5NlQUUoBYgf66WshwLpepoKKvYXU6m6_A</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Patsenker, Eleonora</creator><creator>Popov, Yury</creator><creator>Wiesner, Matthias</creator><creator>Goodman, Simon L</creator><creator>Schuppan, Detlef</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20070501</creationdate><title>Pharmacological inhibition of the vitronectin receptor abrogates PDGF-BB-induced hepatic stellate cell migration and activation in vitro</title><author>Patsenker, Eleonora ; Popov, Yury ; Wiesner, Matthias ; Goodman, Simon L ; Schuppan, Detlef</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-30cfda52e9ac79035276cb5ca3b27af5386817341daf1e8d1f6d7dd60991ee793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Akt</topic><topic>Animals</topic><topic>Antagonist</topic><topic>Biological and medical sciences</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Movement - drug effects</topic><topic>Cell Movement - physiology</topic><topic>Cells, Cultured</topic><topic>Cirrhosis</topic><topic>Collagen</topic><topic>CTGF</topic><topic>Dose-Response Relationship, Drug</topic><topic>Down-Regulation</topic><topic>Erk</topic><topic>FAK</topic><topic>Fibrosis</topic><topic>Focal Adhesion Kinase 1 - metabolism</topic><topic>Gastroenterology and Hepatology</topic><topic>Gastroenterology. Liver. Pancreas. Abdomen</topic><topic>Gene expression</topic><topic>Gene Expression Regulation - drug effects</topic><topic>Hepatic stellate cell</topic><topic>Hepatocytes - cytology</topic><topic>Hepatocytes - drug effects</topic><topic>Hepatocytes - metabolism</topic><topic>Humans</topic><topic>Inhibitor</topic><topic>Integrin</topic><topic>Integrin alphaVbeta3 - antagonists & inhibitors</topic><topic>Integrin alphaVbeta3 - metabolism</topic><topic>Liver</topic><topic>Liver - cytology</topic><topic>Liver - drug effects</topic><topic>Liver - growth & development</topic><topic>Liver - metabolism</topic><topic>Liver. Biliary tract. Portal circulation. Exocrine pancreas</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Migration</topic><topic>MMP</topic><topic>Myofibroblast</topic><topic>Nonpeptide</topic><topic>Other diseases. Semiology</topic><topic>p38</topic><topic>Paxillin</topic><topic>Paxillin - metabolism</topic><topic>PDGF-BB</topic><topic>Peptides, Cyclic - pharmacology</topic><topic>Phosphoproteins - metabolism</topic><topic>Platelet-Derived Growth Factor - pharmacology</topic><topic>Procollagen</topic><topic>Proliferation</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proto-Oncogene Proteins c-sis</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Receptor</topic><topic>RNA, Messenger - genetics</topic><topic>Signal transduction</topic><topic>Signal Transduction - drug effects</topic><topic>TGF beta</topic><topic>TIMP-1</topic><topic>Vitronectin</topic><topic>αvβ3</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Patsenker, Eleonora</creatorcontrib><creatorcontrib>Popov, Yury</creatorcontrib><creatorcontrib>Wiesner, Matthias</creatorcontrib><creatorcontrib>Goodman, Simon L</creatorcontrib><creatorcontrib>Schuppan, Detlef</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of hepatology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Patsenker, Eleonora</au><au>Popov, Yury</au><au>Wiesner, Matthias</au><au>Goodman, Simon L</au><au>Schuppan, Detlef</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pharmacological inhibition of the vitronectin receptor abrogates PDGF-BB-induced hepatic stellate cell migration and activation in vitro</atitle><jtitle>Journal of hepatology</jtitle><addtitle>J Hepatol</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>46</volume><issue>5</issue><spage>878</spage><epage>887</epage><pages>878-887</pages><issn>0168-8278</issn><eissn>1600-0641</eissn><coden>JOHEEC</coden><abstract>Background/Aims Activated hepatic stellate cells (HSC) play a central role in the development of liver fibrosis. Platelet-derived growth factor (PDGF)-BB and the integrin αvβ3 mediate mesenchymal cell migration and proliferation. However, their contribution and interaction during fibrogenic activation of HSC remains unclear. To this aim we investigated if PDFGF-BB and αvβ3 interact, and how far small molecular inhibitors of αvβ3 modulate PDGF-BB and serum-induced migration, proliferation and fibrogenic activation of HSC. Methods Rat and human HSC were subjected to migration and proliferation assays in the presence or absence of a peptide or a nonpeptide αvβ3 inhibitor. Activation of mitogen-activated protein kinases (ERK1/2, p38), Akt, focal adhesion kinase (FAK), paxillin and β3 integrin was evaluated by phospho-specific Western blotting. Fibrosis related transcripts were determined by quantitative real-time PCR. Results PDGF-BB-stimulated HSC migration which was blocked dose-dependently by the αvβ3 antagonists, with complete inhibition at 10−6 M. αvβ3 blockage did not affect cell viability or proliferation, while it decreased phosphorylation of FAK, paxillin, β3 integrin and p38, but not of ERK1/2 or Akt. αvβ3 inhibition led to downregulation of certain profibrogenic transcripts, while it upregulated fibrolytic MMP-13 mRNA. Conclusions Inhibition of integrin αvβ3 leads to abrogation of migration of HSC stimulated with PDGF-BB and to an antifibrogenic gene expression pattern.</abstract><cop>Oxford</cop><pub>Elsevier B.V</pub><pmid>17258347</pmid><doi>10.1016/j.jhep.2006.11.011</doi><tpages>10</tpages></addata></record> |
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| subjects | Akt Animals Antagonist Biological and medical sciences Cell Adhesion - drug effects Cell Adhesion - physiology Cell Movement - drug effects Cell Movement - physiology Cells, Cultured Cirrhosis Collagen CTGF Dose-Response Relationship, Drug Down-Regulation Erk FAK Fibrosis Focal Adhesion Kinase 1 - metabolism Gastroenterology and Hepatology Gastroenterology. Liver. Pancreas. Abdomen Gene expression Gene Expression Regulation - drug effects Hepatic stellate cell Hepatocytes - cytology Hepatocytes - drug effects Hepatocytes - metabolism Humans Inhibitor Integrin Integrin alphaVbeta3 - antagonists & inhibitors Integrin alphaVbeta3 - metabolism Liver Liver - cytology Liver - drug effects Liver - growth & development Liver - metabolism Liver. Biliary tract. Portal circulation. Exocrine pancreas Male Medical sciences Migration MMP Myofibroblast Nonpeptide Other diseases. Semiology p38 Paxillin Paxillin - metabolism PDGF-BB Peptides, Cyclic - pharmacology Phosphoproteins - metabolism Platelet-Derived Growth Factor - pharmacology Procollagen Proliferation Protein-Serine-Threonine Kinases - metabolism Protein-Tyrosine Kinases - metabolism Proto-Oncogene Proteins c-sis Rats Rats, Wistar Receptor RNA, Messenger - genetics Signal transduction Signal Transduction - drug effects TGF beta TIMP-1 Vitronectin αvβ3 |
| title | Pharmacological inhibition of the vitronectin receptor abrogates PDGF-BB-induced hepatic stellate cell migration and activation in vitro |
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