Contribution of the α8 Integrin Chain to the Expression of Extracellular Matrix Components
Abstract In the kidney, the α8 integrin chain (itga8) is expressed in mesenchymal cells and is upregulated in fibrotic disease. We hypothesized that itga8 mediates a profibrotic phenotype of renal cells by promoting extracellular matrix and cytokine expression. Genetic itga8 deficiency caused comple...
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| Veröffentlicht in: | Cell communication & adhesion 2014-04, Vol.21 (2), p.89-98 |
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| creator | Volkert, Gudrun Jahn, Angelika Dinkel, Christina Fahlbusch, Fabian Zürn, Christina Hilgers, Karl F. Rascher, Wolfgang Hartner, Andrea Marek, Ines |
| description | Abstract
In the kidney, the α8 integrin chain (itga8) is expressed in mesenchymal cells and is upregulated in fibrotic disease. We hypothesized that itga8 mediates a profibrotic phenotype of renal cells by promoting extracellular matrix and cytokine expression. Genetic itga8 deficiency caused complex changes in matrix expression patterns in mesangial and smooth-muscle cells, with the only concordant effect in both cell types being a reduction of collagen III expression. Silencing of itga8 with siRNA led to a decline of matrix turnover with repression of matrix metalloproteinases and reduction of matrix production. In contrast, de novo expression of itga8 in tubular epithelial cells resulted in reduced collagen synthesis. Overexpression of itga8 in fibroblasts did not change the expression of matrix molecules or regulators of matrix turnover. Thus, the influence of itga8 on the expression of matrix components was not uniform and celltype dependent. Itga8 seems unlikely to exert overall profibrotic effects in renal cells. |
| doi_str_mv | 10.3109/15419061.2013.876012 |
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In the kidney, the α8 integrin chain (itga8) is expressed in mesenchymal cells and is upregulated in fibrotic disease. We hypothesized that itga8 mediates a profibrotic phenotype of renal cells by promoting extracellular matrix and cytokine expression. Genetic itga8 deficiency caused complex changes in matrix expression patterns in mesangial and smooth-muscle cells, with the only concordant effect in both cell types being a reduction of collagen III expression. Silencing of itga8 with siRNA led to a decline of matrix turnover with repression of matrix metalloproteinases and reduction of matrix production. In contrast, de novo expression of itga8 in tubular epithelial cells resulted in reduced collagen synthesis. Overexpression of itga8 in fibroblasts did not change the expression of matrix molecules or regulators of matrix turnover. Thus, the influence of itga8 on the expression of matrix components was not uniform and celltype dependent. Itga8 seems unlikely to exert overall profibrotic effects in renal cells.</description><identifier>ISSN: 1541-9061</identifier><identifier>EISSN: 1543-5180</identifier><identifier>DOI: 10.3109/15419061.2013.876012</identifier><identifier>PMID: 24460181</identifier><language>eng</language><publisher>England: Informa Healthcare</publisher><subject>Animals ; Blotting, Western ; Cells, Cultured ; Collagen Type III - genetics ; Collagen Type III - metabolism ; Cytokines - genetics ; Cytokines - metabolism ; extracellular matrix ; Extracellular Matrix - metabolism ; Fibroblasts - cytology ; Fibroblasts - metabolism ; fibrosis ; Glomerular Mesangium - cytology ; Glomerular Mesangium - metabolism ; Humans ; Integrin alpha Chains - antagonists & inhibitors ; Integrin alpha Chains - physiology ; integrins ; Kidney Tubules - cytology ; Kidney Tubules - metabolism ; mesenchymal cells ; Mice ; Mice, Knockout ; Muscle, Smooth, Vascular - cytology ; Muscle, Smooth, Vascular - metabolism ; NIH 3T3 Cells ; Phenotype ; Rats ; Real-Time Polymerase Chain Reaction ; renal cells ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - genetics ; RNA, Small Interfering - genetics ; α8 integrin deficiency</subject><ispartof>Cell communication & adhesion, 2014-04, Vol.21 (2), p.89-98</ispartof><rights>2014 Informa Healthcare USA, Inc. 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-ce762397e9451a2926b600a907a7900bdd48d41e6f119612bb9bbb0d76b673603</citedby><cites>FETCH-LOGICAL-c399t-ce762397e9451a2926b600a907a7900bdd48d41e6f119612bb9bbb0d76b673603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.3109/15419061.2013.876012$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.3109/15419061.2013.876012$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>314,776,780,27481,27903,27904,59119,59120,61194,61195</link.rule.ids><linktorsrc>$$Uhttps://www.tandfonline.com/doi/abs/10.3109/15419061.2013.876012$$EView_record_in_Taylor_&_Francis$$FView_record_in_$$GTaylor_&_Francis</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24460181$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Volkert, Gudrun</creatorcontrib><creatorcontrib>Jahn, Angelika</creatorcontrib><creatorcontrib>Dinkel, Christina</creatorcontrib><creatorcontrib>Fahlbusch, Fabian</creatorcontrib><creatorcontrib>Zürn, Christina</creatorcontrib><creatorcontrib>Hilgers, Karl F.</creatorcontrib><creatorcontrib>Rascher, Wolfgang</creatorcontrib><creatorcontrib>Hartner, Andrea</creatorcontrib><creatorcontrib>Marek, Ines</creatorcontrib><title>Contribution of the α8 Integrin Chain to the Expression of Extracellular Matrix Components</title><title>Cell communication & adhesion</title><addtitle>Cell Commun Adhes</addtitle><description>Abstract
In the kidney, the α8 integrin chain (itga8) is expressed in mesenchymal cells and is upregulated in fibrotic disease. We hypothesized that itga8 mediates a profibrotic phenotype of renal cells by promoting extracellular matrix and cytokine expression. Genetic itga8 deficiency caused complex changes in matrix expression patterns in mesangial and smooth-muscle cells, with the only concordant effect in both cell types being a reduction of collagen III expression. Silencing of itga8 with siRNA led to a decline of matrix turnover with repression of matrix metalloproteinases and reduction of matrix production. In contrast, de novo expression of itga8 in tubular epithelial cells resulted in reduced collagen synthesis. Overexpression of itga8 in fibroblasts did not change the expression of matrix molecules or regulators of matrix turnover. Thus, the influence of itga8 on the expression of matrix components was not uniform and celltype dependent. Itga8 seems unlikely to exert overall profibrotic effects in renal cells.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cells, Cultured</subject><subject>Collagen Type III - genetics</subject><subject>Collagen Type III - metabolism</subject><subject>Cytokines - genetics</subject><subject>Cytokines - metabolism</subject><subject>extracellular matrix</subject><subject>Extracellular Matrix - metabolism</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - metabolism</subject><subject>fibrosis</subject><subject>Glomerular Mesangium - cytology</subject><subject>Glomerular Mesangium - metabolism</subject><subject>Humans</subject><subject>Integrin alpha Chains - antagonists & inhibitors</subject><subject>Integrin alpha Chains - physiology</subject><subject>integrins</subject><subject>Kidney Tubules - cytology</subject><subject>Kidney Tubules - metabolism</subject><subject>mesenchymal cells</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Muscle, Smooth, Vascular - cytology</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>NIH 3T3 Cells</subject><subject>Phenotype</subject><subject>Rats</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>renal cells</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Small Interfering - genetics</subject><subject>α8 integrin deficiency</subject><issn>1541-9061</issn><issn>1543-5180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtO5DAQhi00iPcNEMpyNmmqHOfhDaNR1DwkEBtYsbDsxKGDEruxHdEci4twJhK6QWLDxrbKX_1V-gg5RpglCPwUU4YcMpxRwGRW5Bkg3SJ7YzmJUyzgz-cb44nZJfvePwFQCizdIbuUsREvcI88lNYE16ohtNZEtonCQkfvb0V0ZYJ-dK2JyoUcz2A_f-arpdPeb9j5KjhZ6a4bOumiGzkGraLS9ktrtAn-kGw3svP6aHMfkPvz-V15GV_fXlyV_6_jKuE8xJXOM5rwXHOWoqScZioDkBxymXMAVdesqBnqrEHkGVKluFIK6nzk8iSD5ID8XecunX0etA-ib_20ljTaDl5gCgVnCaMTytZo5az3Tjdi6dpeuleBICat4kurmLSKtdax7WQzYVC9rr-bvjyOwL810JrGul6-WNfVIsjXzrrGSVO1for_dcTZj4SFll1YVNJp8WQHZ0aBv-_4Ad4_meQ</recordid><startdate>201404</startdate><enddate>201404</enddate><creator>Volkert, Gudrun</creator><creator>Jahn, Angelika</creator><creator>Dinkel, Christina</creator><creator>Fahlbusch, Fabian</creator><creator>Zürn, Christina</creator><creator>Hilgers, Karl F.</creator><creator>Rascher, Wolfgang</creator><creator>Hartner, Andrea</creator><creator>Marek, Ines</creator><general>Informa Healthcare</general><general>Taylor & Francis</general><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>201404</creationdate><title>Contribution of the α8 Integrin Chain to the Expression of Extracellular Matrix Components</title><author>Volkert, Gudrun ; Jahn, Angelika ; Dinkel, Christina ; Fahlbusch, Fabian ; Zürn, Christina ; Hilgers, Karl F. ; Rascher, Wolfgang ; Hartner, Andrea ; Marek, Ines</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-ce762397e9451a2926b600a907a7900bdd48d41e6f119612bb9bbb0d76b673603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cells, Cultured</topic><topic>Collagen Type III - genetics</topic><topic>Collagen Type III - metabolism</topic><topic>Cytokines - genetics</topic><topic>Cytokines - metabolism</topic><topic>extracellular matrix</topic><topic>Extracellular Matrix - metabolism</topic><topic>Fibroblasts - cytology</topic><topic>Fibroblasts - metabolism</topic><topic>fibrosis</topic><topic>Glomerular Mesangium - cytology</topic><topic>Glomerular Mesangium - metabolism</topic><topic>Humans</topic><topic>Integrin alpha Chains - antagonists & inhibitors</topic><topic>Integrin alpha Chains - physiology</topic><topic>integrins</topic><topic>Kidney Tubules - cytology</topic><topic>Kidney Tubules - metabolism</topic><topic>mesenchymal cells</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Muscle, Smooth, Vascular - cytology</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>NIH 3T3 Cells</topic><topic>Phenotype</topic><topic>Rats</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>renal cells</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Small Interfering - genetics</topic><topic>α8 integrin deficiency</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Volkert, Gudrun</creatorcontrib><creatorcontrib>Jahn, Angelika</creatorcontrib><creatorcontrib>Dinkel, Christina</creatorcontrib><creatorcontrib>Fahlbusch, Fabian</creatorcontrib><creatorcontrib>Zürn, Christina</creatorcontrib><creatorcontrib>Hilgers, Karl F.</creatorcontrib><creatorcontrib>Rascher, Wolfgang</creatorcontrib><creatorcontrib>Hartner, Andrea</creatorcontrib><creatorcontrib>Marek, Ines</creatorcontrib><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>Cell communication & adhesion</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Volkert, Gudrun</au><au>Jahn, Angelika</au><au>Dinkel, Christina</au><au>Fahlbusch, Fabian</au><au>Zürn, Christina</au><au>Hilgers, Karl F.</au><au>Rascher, Wolfgang</au><au>Hartner, Andrea</au><au>Marek, Ines</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Contribution of the α8 Integrin Chain to the Expression of Extracellular Matrix Components</atitle><jtitle>Cell communication & adhesion</jtitle><addtitle>Cell Commun Adhes</addtitle><date>2014-04</date><risdate>2014</risdate><volume>21</volume><issue>2</issue><spage>89</spage><epage>98</epage><pages>89-98</pages><issn>1541-9061</issn><eissn>1543-5180</eissn><abstract>Abstract
In the kidney, the α8 integrin chain (itga8) is expressed in mesenchymal cells and is upregulated in fibrotic disease. We hypothesized that itga8 mediates a profibrotic phenotype of renal cells by promoting extracellular matrix and cytokine expression. Genetic itga8 deficiency caused complex changes in matrix expression patterns in mesangial and smooth-muscle cells, with the only concordant effect in both cell types being a reduction of collagen III expression. Silencing of itga8 with siRNA led to a decline of matrix turnover with repression of matrix metalloproteinases and reduction of matrix production. In contrast, de novo expression of itga8 in tubular epithelial cells resulted in reduced collagen synthesis. Overexpression of itga8 in fibroblasts did not change the expression of matrix molecules or regulators of matrix turnover. Thus, the influence of itga8 on the expression of matrix components was not uniform and celltype dependent. Itga8 seems unlikely to exert overall profibrotic effects in renal cells.</abstract><cop>England</cop><pub>Informa Healthcare</pub><pmid>24460181</pmid><doi>10.3109/15419061.2013.876012</doi><tpages>10</tpages></addata></record> |
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| subjects | Animals Blotting, Western Cells, Cultured Collagen Type III - genetics Collagen Type III - metabolism Cytokines - genetics Cytokines - metabolism extracellular matrix Extracellular Matrix - metabolism Fibroblasts - cytology Fibroblasts - metabolism fibrosis Glomerular Mesangium - cytology Glomerular Mesangium - metabolism Humans Integrin alpha Chains - antagonists & inhibitors Integrin alpha Chains - physiology integrins Kidney Tubules - cytology Kidney Tubules - metabolism mesenchymal cells Mice Mice, Knockout Muscle, Smooth, Vascular - cytology Muscle, Smooth, Vascular - metabolism NIH 3T3 Cells Phenotype Rats Real-Time Polymerase Chain Reaction renal cells Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - genetics RNA, Small Interfering - genetics α8 integrin deficiency |
| title | Contribution of the α8 Integrin Chain to the Expression of Extracellular Matrix Components |
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