Heterogeneity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase
The heterogeneity of human collagenases has been examined using a monoclonal antibody to neutrophil collagenase. This antibody inhibited collagenase activity and, when covalently coupled to Sepharose, bound both latent and active enzyme. Although human neutrophil collagenase was inhibited by the ant...
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| Veröffentlicht in: | The Journal of experimental medicine 1984-05, Vol.159 (5), p.1455-1463 |
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| container_end_page | 1463 |
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| container_issue | 5 |
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| container_title | The Journal of experimental medicine |
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| creator | HASTY, K. A HIBBS, M. S KANG, A. H MAINARDI, C. L |
| description | The heterogeneity of human collagenases has been examined using a monoclonal antibody to neutrophil collagenase. This antibody inhibited collagenase activity and, when covalently coupled to Sepharose, bound both latent and active enzyme. Although human neutrophil collagenase was inhibited by the antibody, the activity of human skin and rheumatoid synovial collagenase was not significantly diminished in the presence of the antibody. Competitive inhibition studies also differentiated between these collagenases. Only human neutrophil collagenase effectively blocked the antibody in a competitive enzyme-linked immunosorbent assay while skin and rheumatoid synovial collagenase again failed to interact with the antibody. The unequivocal recognition of neutrophil collagenase as an immunologically distinct entity from other collagenases supports the hypothesis that neutrophil collagenase is a separate gene product from fibroblast or synovial collagenase. |
| doi_str_mv | 10.1084/jem.159.5.1455 |
| format | Article |
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A ; HIBBS, M. S ; KANG, A. H ; MAINARDI, C. L</creator><creatorcontrib>HASTY, K. A ; HIBBS, M. S ; KANG, A. H ; MAINARDI, C. L</creatorcontrib><description>The heterogeneity of human collagenases has been examined using a monoclonal antibody to neutrophil collagenase. This antibody inhibited collagenase activity and, when covalently coupled to Sepharose, bound both latent and active enzyme. Although human neutrophil collagenase was inhibited by the antibody, the activity of human skin and rheumatoid synovial collagenase was not significantly diminished in the presence of the antibody. Competitive inhibition studies also differentiated between these collagenases. Only human neutrophil collagenase effectively blocked the antibody in a competitive enzyme-linked immunosorbent assay while skin and rheumatoid synovial collagenase again failed to interact with the antibody. The unequivocal recognition of neutrophil collagenase as an immunologically distinct entity from other collagenases supports the hypothesis that neutrophil collagenase is a separate gene product from fibroblast or synovial collagenase.</description><identifier>ISSN: 0022-1007</identifier><identifier>EISSN: 1540-9538</identifier><identifier>DOI: 10.1084/jem.159.5.1455</identifier><identifier>PMID: 6325574</identifier><identifier>CODEN: JEMEAV</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Antibodies, Monoclonal - physiology ; Arthritis, Rheumatoid - immunology ; Binding, Competitive ; Biological and medical sciences ; Cell Separation ; Cross Reactions ; Enzyme Inhibitors - physiology ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Humans ; Hydrolases ; Mice ; Microbial Collagenase - antagonists & inhibitors ; Microbial Collagenase - genetics ; Microbial Collagenase - immunology ; Microbial Collagenase - metabolism ; Neutrophils - enzymology ; Skin - enzymology ; Synovial Membrane - enzymology ; Tissue Inhibitor of Metalloproteinases</subject><ispartof>The Journal of experimental medicine, 1984-05, Vol.159 (5), p.1455-1463</ispartof><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c445t-8bbd9680cff8cbf75bd3ae01aec9637690c94fc5f4e0757bcf6490f9b3a24ae93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9697578$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6325574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HASTY, K. A</creatorcontrib><creatorcontrib>HIBBS, M. S</creatorcontrib><creatorcontrib>KANG, A. H</creatorcontrib><creatorcontrib>MAINARDI, C. L</creatorcontrib><title>Heterogeneity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase</title><title>The Journal of experimental medicine</title><addtitle>J Exp Med</addtitle><description>The heterogeneity of human collagenases has been examined using a monoclonal antibody to neutrophil collagenase. This antibody inhibited collagenase activity and, when covalently coupled to Sepharose, bound both latent and active enzyme. Although human neutrophil collagenase was inhibited by the antibody, the activity of human skin and rheumatoid synovial collagenase was not significantly diminished in the presence of the antibody. Competitive inhibition studies also differentiated between these collagenases. Only human neutrophil collagenase effectively blocked the antibody in a competitive enzyme-linked immunosorbent assay while skin and rheumatoid synovial collagenase again failed to interact with the antibody. The unequivocal recognition of neutrophil collagenase as an immunologically distinct entity from other collagenases supports the hypothesis that neutrophil collagenase is a separate gene product from fibroblast or synovial collagenase.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - physiology</subject><subject>Arthritis, Rheumatoid - immunology</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cell Separation</subject><subject>Cross Reactions</subject><subject>Enzyme Inhibitors - physiology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Mice</subject><subject>Microbial Collagenase - antagonists & inhibitors</subject><subject>Microbial Collagenase - genetics</subject><subject>Microbial Collagenase - immunology</subject><subject>Microbial Collagenase - metabolism</subject><subject>Neutrophils - enzymology</subject><subject>Skin - enzymology</subject><subject>Synovial Membrane - enzymology</subject><subject>Tissue Inhibitor of Metalloproteinases</subject><issn>0022-1007</issn><issn>1540-9538</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUGP1SAUhYnRjM_RrTsTFsZdKxRoy8bETNQxmcSNrgmll1cmLTyBTtL5Ff5kmUzzMq5cEXK-e7iHg9BbSmpKev7xFpaaClmLmnIhnqEDFZxUUrD-OToQ0jQVJaR7iV6ldEsI5Vy0F-iiZY0QHT-gP9eQIYYjeHB5w3oJ_oinddEemzDPugg6QcIjFCXlqDOMeNhwuQUzB69nrH12Qxg3nCedcYIZTHZ3MG84gglH7-7LvPYjdn5yg8tp9_ew5hhOk5ufPvUavbB6TvBmPy_Rr69ffl5dVzc_vn2_-nxTmRIhV_0wjLLtibG2N4PtxDAyDYRqMLJlXSuJkdwaYTmQTnSDsS2XxMqB6YZrkOwSfXr0Pa3DAqMBX8LN6hTdouOmgnbqX8W7SR3DnWpo3zHCi8GH3SCG3yukrBaXDJQgHsKaVE8J45TI_4KUybYVsi9g_QiaGFKKYM_bUKIeylalbFXKVkI9lF0G3j3NcMb3dov-ftd1Mnq2UXvj0hmTrSxf07O_gTO5TQ</recordid><startdate>19840501</startdate><enddate>19840501</enddate><creator>HASTY, K. A</creator><creator>HIBBS, M. S</creator><creator>KANG, A. H</creator><creator>MAINARDI, C. L</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7T5</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19840501</creationdate><title>Heterogeneity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase</title><author>HASTY, K. A ; HIBBS, M. S ; KANG, A. H ; MAINARDI, C. L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c445t-8bbd9680cff8cbf75bd3ae01aec9637690c94fc5f4e0757bcf6490f9b3a24ae93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - physiology</topic><topic>Arthritis, Rheumatoid - immunology</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cell Separation</topic><topic>Cross Reactions</topic><topic>Enzyme Inhibitors - physiology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Mice</topic><topic>Microbial Collagenase - antagonists & inhibitors</topic><topic>Microbial Collagenase - genetics</topic><topic>Microbial Collagenase - immunology</topic><topic>Microbial Collagenase - metabolism</topic><topic>Neutrophils - enzymology</topic><topic>Skin - enzymology</topic><topic>Synovial Membrane - enzymology</topic><topic>Tissue Inhibitor of Metalloproteinases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HASTY, K. A</creatorcontrib><creatorcontrib>HIBBS, M. S</creatorcontrib><creatorcontrib>KANG, A. H</creatorcontrib><creatorcontrib>MAINARDI, C. 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L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heterogeneity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase</atitle><jtitle>The Journal of experimental medicine</jtitle><addtitle>J Exp Med</addtitle><date>1984-05-01</date><risdate>1984</risdate><volume>159</volume><issue>5</issue><spage>1455</spage><epage>1463</epage><pages>1455-1463</pages><issn>0022-1007</issn><eissn>1540-9538</eissn><coden>JEMEAV</coden><abstract>The heterogeneity of human collagenases has been examined using a monoclonal antibody to neutrophil collagenase. This antibody inhibited collagenase activity and, when covalently coupled to Sepharose, bound both latent and active enzyme. Although human neutrophil collagenase was inhibited by the antibody, the activity of human skin and rheumatoid synovial collagenase was not significantly diminished in the presence of the antibody. Competitive inhibition studies also differentiated between these collagenases. Only human neutrophil collagenase effectively blocked the antibody in a competitive enzyme-linked immunosorbent assay while skin and rheumatoid synovial collagenase again failed to interact with the antibody. The unequivocal recognition of neutrophil collagenase as an immunologically distinct entity from other collagenases supports the hypothesis that neutrophil collagenase is a separate gene product from fibroblast or synovial collagenase.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>6325574</pmid><doi>10.1084/jem.159.5.1455</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of experimental medicine, 1984-05, Vol.159 (5), p.1455-1463 |
| issn | 0022-1007 1540-9538 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2187304 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Analytical, structural and metabolic biochemistry Animals Antibodies, Monoclonal - physiology Arthritis, Rheumatoid - immunology Binding, Competitive Biological and medical sciences Cell Separation Cross Reactions Enzyme Inhibitors - physiology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Mice Microbial Collagenase - antagonists & inhibitors Microbial Collagenase - genetics Microbial Collagenase - immunology Microbial Collagenase - metabolism Neutrophils - enzymology Skin - enzymology Synovial Membrane - enzymology Tissue Inhibitor of Metalloproteinases |
| title | Heterogeneity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase |
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