The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator
This study describes the binding of plasminogen and tissue-type plasminogen activator (t-PA) to the extracellular matrix proteins fibronectin and laminin. Plasminogen bound specifically and saturably to both fibronectin and laminin immobilized on microtiter wells, with Kd(app) values of 115 and 18 n...
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Veröffentlicht in: | The Journal of biological chemistry 1993-09, Vol.268 (25), p.18917-18923 |
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creator | Moser, T.L. Enghild, J.J. Pizzo, S.V. Stack, M.S. |
description | This study describes the binding of plasminogen and tissue-type plasminogen activator (t-PA) to the extracellular matrix proteins fibronectin and laminin. Plasminogen bound specifically and saturably to both fibronectin and laminin immobilized on microtiter wells, with Kd(app) values of 115 and 18 nM, respectively. Limited proteolysis by endoproteinase V8 coupled with ligand blotting analysis showed that both plasminogen and t-PA preferentially bind to a 55-kDa fibronectin fragment and a 38-kDa laminin fragment. Amino acid sequence analysis demonstrated that the 5-kDa fragment originates with the fibronectin amino terminus whereas the laminin fragment was derived from the carboxyl-terminal globular domain of the laminin A chain. Ligand blotting experiments using isolated plasminogen domains were also used to identify distinct regions of the plasminogen molecule involved in fibronectin and laminin binding. Solution phase fibronectin binding to immobilized plasminogen was mediated primarily via lysine binding site-dependent interactions with plasminogen kringles 1-4. Lysine binding site-dependent binding of soluble laminin to immobilized plasminogen kringles 1-5 as well as an additional lysine binding site-independent interaction between mini-plasminogen and the 38-kDa laminin A chain fragment were also observed. These studies demonstrate binding of plasminogen and tissue-type plasminogen activator to specific regions of the extracellular matrix glycoproteins laminin and fibronectin and provide further insight into the mechanism of regulation of plasminogen activation by components of the extracellular matrix. |
doi_str_mv | 10.1016/S0021-9258(17)46714-7 |
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Plasminogen bound specifically and saturably to both fibronectin and laminin immobilized on microtiter wells, with Kd(app) values of 115 and 18 nM, respectively. Limited proteolysis by endoproteinase V8 coupled with ligand blotting analysis showed that both plasminogen and t-PA preferentially bind to a 55-kDa fibronectin fragment and a 38-kDa laminin fragment. Amino acid sequence analysis demonstrated that the 5-kDa fragment originates with the fibronectin amino terminus whereas the laminin fragment was derived from the carboxyl-terminal globular domain of the laminin A chain. Ligand blotting experiments using isolated plasminogen domains were also used to identify distinct regions of the plasminogen molecule involved in fibronectin and laminin binding. Solution phase fibronectin binding to immobilized plasminogen was mediated primarily via lysine binding site-dependent interactions with plasminogen kringles 1-4. Lysine binding site-dependent binding of soluble laminin to immobilized plasminogen kringles 1-5 as well as an additional lysine binding site-independent interaction between mini-plasminogen and the 38-kDa laminin A chain fragment were also observed. These studies demonstrate binding of plasminogen and tissue-type plasminogen activator to specific regions of the extracellular matrix glycoproteins laminin and fibronectin and provide further insight into the mechanism of regulation of plasminogen activation by components of the extracellular matrix.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)46714-7</identifier><identifier>PMID: 8360181</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Binding Sites ; Enzyme-Linked Immunosorbent Assay ; Fibronectins - chemistry ; Fibronectins - metabolism ; Humans ; Laminin - chemistry ; Laminin - metabolism ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Plasminogen - metabolism ; Sequence Analysis ; Serine Endopeptidases - metabolism ; Tissue Plasminogen Activator - metabolism ; Trypsin - metabolism</subject><ispartof>The Journal of biological chemistry, 1993-09, Vol.268 (25), p.18917-18923</ispartof><rights>1993 © 1993 ASBMB. 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Plasminogen bound specifically and saturably to both fibronectin and laminin immobilized on microtiter wells, with Kd(app) values of 115 and 18 nM, respectively. Limited proteolysis by endoproteinase V8 coupled with ligand blotting analysis showed that both plasminogen and t-PA preferentially bind to a 55-kDa fibronectin fragment and a 38-kDa laminin fragment. Amino acid sequence analysis demonstrated that the 5-kDa fragment originates with the fibronectin amino terminus whereas the laminin fragment was derived from the carboxyl-terminal globular domain of the laminin A chain. Ligand blotting experiments using isolated plasminogen domains were also used to identify distinct regions of the plasminogen molecule involved in fibronectin and laminin binding. Solution phase fibronectin binding to immobilized plasminogen was mediated primarily via lysine binding site-dependent interactions with plasminogen kringles 1-4. Lysine binding site-dependent binding of soluble laminin to immobilized plasminogen kringles 1-5 as well as an additional lysine binding site-independent interaction between mini-plasminogen and the 38-kDa laminin A chain fragment were also observed. These studies demonstrate binding of plasminogen and tissue-type plasminogen activator to specific regions of the extracellular matrix glycoproteins laminin and fibronectin and provide further insight into the mechanism of regulation of plasminogen activation by components of the extracellular matrix.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fibronectins - chemistry</subject><subject>Fibronectins - metabolism</subject><subject>Humans</subject><subject>Laminin - chemistry</subject><subject>Laminin - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Plasminogen - metabolism</subject><subject>Sequence Analysis</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Tissue Plasminogen Activator - metabolism</subject><subject>Trypsin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUc1uFSEUJkZTr9VHaDILY3QxCsPAwMqYxr-kiQtr4o4wcOYOZgauwNT2DfrYMp2bJl2VzQl8P4fzHYTOCH5PMOEffmLckFo2TLwl3buWd6StuydoR7CgNWXk91O0u6c8Ry9S-oPLaSU5QSeCckwE2aHbyxEquM5RG5imZdKxmnWO7ro6xJDB-VRNenbe-Up7Ww2uj8GDyeVugs-61N556_y-smHWK38IsRqXWfvqMOlUtGEPmzq7lBZ4-FysrnQO8SV6NugpwatjPUW_vny-PP9WX_z4-v3800VtWiFyDVhazfQAusHdYLFuWqBWDp1mTFjOCfSUWUkbzGVBTC-4YBQY4ZRhOxB6it5svmW-vwukrGaX1tm1h7Ak1THZtELSQmQb0cSQUoRBHaKbdbxRBKt1A-puA2qNV5FO3W1AdUV3dmyw9DPYe9Ux8oK_3vDR7cd_LoLqXTAjzKrhQjVMESHJavNxo0EJ48pBVMk48AZskZisbHCPfOQ__2KlWQ</recordid><startdate>19930905</startdate><enddate>19930905</enddate><creator>Moser, T.L.</creator><creator>Enghild, J.J.</creator><creator>Pizzo, S.V.</creator><creator>Stack, M.S.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>19930905</creationdate><title>The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator</title><author>Moser, T.L. ; Enghild, J.J. ; Pizzo, S.V. ; Stack, M.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-e09da5afea207fd0a24e3d9f7a558d661eb35d9320694e3cb86853e516350df13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fibronectins - chemistry</topic><topic>Fibronectins - metabolism</topic><topic>Humans</topic><topic>Laminin - chemistry</topic><topic>Laminin - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Plasminogen - metabolism</topic><topic>Sequence Analysis</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Tissue Plasminogen Activator - metabolism</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moser, T.L.</creatorcontrib><creatorcontrib>Enghild, J.J.</creatorcontrib><creatorcontrib>Pizzo, S.V.</creatorcontrib><creatorcontrib>Stack, M.S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moser, T.L.</au><au>Enghild, J.J.</au><au>Pizzo, S.V.</au><au>Stack, M.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-09-05</date><risdate>1993</risdate><volume>268</volume><issue>25</issue><spage>18917</spage><epage>18923</epage><pages>18917-18923</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>This study describes the binding of plasminogen and tissue-type plasminogen activator (t-PA) to the extracellular matrix proteins fibronectin and laminin. Plasminogen bound specifically and saturably to both fibronectin and laminin immobilized on microtiter wells, with Kd(app) values of 115 and 18 nM, respectively. Limited proteolysis by endoproteinase V8 coupled with ligand blotting analysis showed that both plasminogen and t-PA preferentially bind to a 55-kDa fibronectin fragment and a 38-kDa laminin fragment. Amino acid sequence analysis demonstrated that the 5-kDa fragment originates with the fibronectin amino terminus whereas the laminin fragment was derived from the carboxyl-terminal globular domain of the laminin A chain. Ligand blotting experiments using isolated plasminogen domains were also used to identify distinct regions of the plasminogen molecule involved in fibronectin and laminin binding. Solution phase fibronectin binding to immobilized plasminogen was mediated primarily via lysine binding site-dependent interactions with plasminogen kringles 1-4. Lysine binding site-dependent binding of soluble laminin to immobilized plasminogen kringles 1-5 as well as an additional lysine binding site-independent interaction between mini-plasminogen and the 38-kDa laminin A chain fragment were also observed. These studies demonstrate binding of plasminogen and tissue-type plasminogen activator to specific regions of the extracellular matrix glycoproteins laminin and fibronectin and provide further insight into the mechanism of regulation of plasminogen activation by components of the extracellular matrix.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8360181</pmid><doi>10.1016/S0021-9258(17)46714-7</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Binding Sites Enzyme-Linked Immunosorbent Assay Fibronectins - chemistry Fibronectins - metabolism Humans Laminin - chemistry Laminin - metabolism Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - metabolism Plasminogen - metabolism Sequence Analysis Serine Endopeptidases - metabolism Tissue Plasminogen Activator - metabolism Trypsin - metabolism |
title | The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator |
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