Activation of the 92 kDa type IV collagenase by tissue kallikrein
Type IV collagenases are secreted as latent 92 and 72 kDa proenzymes which are then activated extracellularly. The mechanisms by which they are activated in vivo are not clear. We have studied the activation of porcine endothelial cell type IV collagenases by tissue and plasma kallikrein, and found...
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| Veröffentlicht in: | Journal of cellular physiology 1993-12, Vol.157 (3), p.587-593 |
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| container_title | Journal of cellular physiology |
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| creator | Desriviéres, Sylvane Lu, He Peyri, Nicole Soria, Claudine Legrand, Yves Ménashi, Suzanne |
| description | Type IV collagenases are secreted as latent 92 and 72 kDa proenzymes which are then activated extracellularly. The mechanisms by which they are activated in vivo are not clear. We have studied the activation of porcine endothelial cell type IV collagenases by tissue and plasma kallikrein, and found that tissue kallikrein was a very efficient activator of the 92 kDa type IV collagenase. Enzyme cleavage was observed at concentrations of tissue kallikrein as low as 0.1 μg/ml. Plasma kallikrein had no effect. By comparison, plasmin, which has been proposed to be the physiological activator of interstitial collagenase and stromelysin, and elastase were much less effective, and high concentrations (plasmin at 100–200 μg/ml and elastase at 20 μg/ml) were required to cause only a limited cleavage which was not associated with an increase in activity, as observed by the gelatin‐gel lysis assay. In addition tissue kallikrein was found by immunohistochemistry to be present in the extracellular matrix of the intima of porcine aortic vessel wall. These findings suggest that tissue kallikrein can be a potential activator of the 92 kDa type IV collagenase in vivo. © 1993 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/jcp.1041570319 |
| format | Article |
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The mechanisms by which they are activated in vivo are not clear. We have studied the activation of porcine endothelial cell type IV collagenases by tissue and plasma kallikrein, and found that tissue kallikrein was a very efficient activator of the 92 kDa type IV collagenase. Enzyme cleavage was observed at concentrations of tissue kallikrein as low as 0.1 μg/ml. Plasma kallikrein had no effect. By comparison, plasmin, which has been proposed to be the physiological activator of interstitial collagenase and stromelysin, and elastase were much less effective, and high concentrations (plasmin at 100–200 μg/ml and elastase at 20 μg/ml) were required to cause only a limited cleavage which was not associated with an increase in activity, as observed by the gelatin‐gel lysis assay. In addition tissue kallikrein was found by immunohistochemistry to be present in the extracellular matrix of the intima of porcine aortic vessel wall. These findings suggest that tissue kallikrein can be a potential activator of the 92 kDa type IV collagenase in vivo. © 1993 Wiley‐Liss, Inc.</description><identifier>ISSN: 0021-9541</identifier><identifier>EISSN: 1097-4652</identifier><identifier>DOI: 10.1002/jcp.1041570319</identifier><identifier>PMID: 8253870</identifier><identifier>CODEN: JCLLAX</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; Biological and medical sciences ; Blood vessels and receptors ; Cells, Cultured ; Collagenases - metabolism ; Culture Media, Conditioned - metabolism ; Endothelium, Vascular - cytology ; Endothelium, Vascular - enzymology ; Enzyme Activation ; Fibrinolysin - pharmacology ; Fundamental and applied biological sciences. Psychology ; Immunohistochemistry ; Kallikreins - pharmacology ; Pancreatic Elastase - pharmacology ; Protease Inhibitors - pharmacology ; Swine ; Tissue Kallikreins ; Vertebrates: cardiovascular system</subject><ispartof>Journal of cellular physiology, 1993-12, Vol.157 (3), p.587-593</ispartof><rights>Copyright © 1993 Wiley‐Liss, Inc.</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4079-3a8329292bf2beab58bbdd7f34c07b7c4f41e24e1fcf1e3d78f21c416be9b0013</citedby><cites>FETCH-LOGICAL-c4079-3a8329292bf2beab58bbdd7f34c07b7c4f41e24e1fcf1e3d78f21c416be9b0013</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjcp.1041570319$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcp.1041570319$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3897843$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8253870$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Desriviéres, Sylvane</creatorcontrib><creatorcontrib>Lu, He</creatorcontrib><creatorcontrib>Peyri, Nicole</creatorcontrib><creatorcontrib>Soria, Claudine</creatorcontrib><creatorcontrib>Legrand, Yves</creatorcontrib><creatorcontrib>Ménashi, Suzanne</creatorcontrib><title>Activation of the 92 kDa type IV collagenase by tissue kallikrein</title><title>Journal of cellular physiology</title><addtitle>J. Cell. Physiol</addtitle><description>Type IV collagenases are secreted as latent 92 and 72 kDa proenzymes which are then activated extracellularly. The mechanisms by which they are activated in vivo are not clear. We have studied the activation of porcine endothelial cell type IV collagenases by tissue and plasma kallikrein, and found that tissue kallikrein was a very efficient activator of the 92 kDa type IV collagenase. Enzyme cleavage was observed at concentrations of tissue kallikrein as low as 0.1 μg/ml. Plasma kallikrein had no effect. By comparison, plasmin, which has been proposed to be the physiological activator of interstitial collagenase and stromelysin, and elastase were much less effective, and high concentrations (plasmin at 100–200 μg/ml and elastase at 20 μg/ml) were required to cause only a limited cleavage which was not associated with an increase in activity, as observed by the gelatin‐gel lysis assay. In addition tissue kallikrein was found by immunohistochemistry to be present in the extracellular matrix of the intima of porcine aortic vessel wall. These findings suggest that tissue kallikrein can be a potential activator of the 92 kDa type IV collagenase in vivo. © 1993 Wiley‐Liss, Inc.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood vessels and receptors</subject><subject>Cells, Cultured</subject><subject>Collagenases - metabolism</subject><subject>Culture Media, Conditioned - metabolism</subject><subject>Endothelium, Vascular - cytology</subject><subject>Endothelium, Vascular - enzymology</subject><subject>Enzyme Activation</subject><subject>Fibrinolysin - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunohistochemistry</subject><subject>Kallikreins - pharmacology</subject><subject>Pancreatic Elastase - pharmacology</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Swine</subject><subject>Tissue Kallikreins</subject><subject>Vertebrates: cardiovascular system</subject><issn>0021-9541</issn><issn>1097-4652</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1PGzEQxa2qiAbaa2-VfKi4Lfhr1-tjGiAEIorEV2-W7Yxbk83ust4A-e8xShTUE5rDjPR-b2b0EPpOySElhB09uDYNguaScKo-oQElSmaiyNlnNEgAzVQu6Be0F-MDIUQpznfRbslyXkoyQMOh68OT6UNT48bj_h9gxfD82OB-1QKe3GHXVJX5C7WJgO0K9yHGJeC5qaow7yDUX9GON1WEb5u-j25PT25GZ9n093gyGk4zJ4hUGTclZyqV9cyCsXlp7WwmPReOSCud8IICE0C98xT4TJaeUSdoYUFZQijfRwfrvW3XPC4h9noRooP0XA3NMmpZEFVwwhJ4uAZd18TYgddtFxamW2lK9FtmOmWm3zNLhh-bzUu7gNkW34SU9J8b3URnKt-Z2oW4xXipZCl4wtQaew4VrD44qs9HV_-9kK29IfbwsvWabq4LyWWu7y_H-s_1-aUcX_zSBX8FpPeSxQ</recordid><startdate>199312</startdate><enddate>199312</enddate><creator>Desriviéres, Sylvane</creator><creator>Lu, He</creator><creator>Peyri, Nicole</creator><creator>Soria, Claudine</creator><creator>Legrand, Yves</creator><creator>Ménashi, Suzanne</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><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>199312</creationdate><title>Activation of the 92 kDa type IV collagenase by tissue kallikrein</title><author>Desriviéres, Sylvane ; Lu, He ; Peyri, Nicole ; Soria, Claudine ; Legrand, Yves ; Ménashi, Suzanne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4079-3a8329292bf2beab58bbdd7f34c07b7c4f41e24e1fcf1e3d78f21c416be9b0013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood vessels and receptors</topic><topic>Cells, Cultured</topic><topic>Collagenases - metabolism</topic><topic>Culture Media, Conditioned - metabolism</topic><topic>Endothelium, Vascular - cytology</topic><topic>Endothelium, Vascular - enzymology</topic><topic>Enzyme Activation</topic><topic>Fibrinolysin - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunohistochemistry</topic><topic>Kallikreins - pharmacology</topic><topic>Pancreatic Elastase - pharmacology</topic><topic>Protease Inhibitors - pharmacology</topic><topic>Swine</topic><topic>Tissue Kallikreins</topic><topic>Vertebrates: cardiovascular system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Desriviéres, Sylvane</creatorcontrib><creatorcontrib>Lu, He</creatorcontrib><creatorcontrib>Peyri, Nicole</creatorcontrib><creatorcontrib>Soria, Claudine</creatorcontrib><creatorcontrib>Legrand, Yves</creatorcontrib><creatorcontrib>Ménashi, Suzanne</creatorcontrib><collection>Istex</collection><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 cellular physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Desriviéres, Sylvane</au><au>Lu, He</au><au>Peyri, Nicole</au><au>Soria, Claudine</au><au>Legrand, Yves</au><au>Ménashi, Suzanne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of the 92 kDa type IV collagenase by tissue kallikrein</atitle><jtitle>Journal of cellular physiology</jtitle><addtitle>J. Cell. Physiol</addtitle><date>1993-12</date><risdate>1993</risdate><volume>157</volume><issue>3</issue><spage>587</spage><epage>593</epage><pages>587-593</pages><issn>0021-9541</issn><eissn>1097-4652</eissn><coden>JCLLAX</coden><abstract>Type IV collagenases are secreted as latent 92 and 72 kDa proenzymes which are then activated extracellularly. The mechanisms by which they are activated in vivo are not clear. We have studied the activation of porcine endothelial cell type IV collagenases by tissue and plasma kallikrein, and found that tissue kallikrein was a very efficient activator of the 92 kDa type IV collagenase. Enzyme cleavage was observed at concentrations of tissue kallikrein as low as 0.1 μg/ml. Plasma kallikrein had no effect. By comparison, plasmin, which has been proposed to be the physiological activator of interstitial collagenase and stromelysin, and elastase were much less effective, and high concentrations (plasmin at 100–200 μg/ml and elastase at 20 μg/ml) were required to cause only a limited cleavage which was not associated with an increase in activity, as observed by the gelatin‐gel lysis assay. In addition tissue kallikrein was found by immunohistochemistry to be present in the extracellular matrix of the intima of porcine aortic vessel wall. These findings suggest that tissue kallikrein can be a potential activator of the 92 kDa type IV collagenase in vivo. © 1993 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>8253870</pmid><doi>10.1002/jcp.1041570319</doi><tpages>7</tpages></addata></record> |
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| subjects | Animals Biological and medical sciences Blood vessels and receptors Cells, Cultured Collagenases - metabolism Culture Media, Conditioned - metabolism Endothelium, Vascular - cytology Endothelium, Vascular - enzymology Enzyme Activation Fibrinolysin - pharmacology Fundamental and applied biological sciences. Psychology Immunohistochemistry Kallikreins - pharmacology Pancreatic Elastase - pharmacology Protease Inhibitors - pharmacology Swine Tissue Kallikreins Vertebrates: cardiovascular system |
| title | Activation of the 92 kDa type IV collagenase by tissue kallikrein |
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