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Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase
Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl fluoride (PhCH2SO2F) but not by EDTA. The...
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Published in: | The Journal of biological chemistry 1980-12, Vol.255 (24), p.12006-12010 |
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creator | Mainardi, C L Hasty, D L Seyer, J M Kang, A H |
description | Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage
through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl
fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid
synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis
indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established
cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively
depleted from the matrix by this enzyme. |
doi_str_mv | 10.1016/S0021-9258(19)70234-8 |
format | article |
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through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl
fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid
synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis
indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established
cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively
depleted from the matrix by this enzyme.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)70234-8</identifier><identifier>PMID: 6254989</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Amino Acids - analysis ; Collagen ; Humans ; Liver Cirrhosis - metabolism ; Microbial Collagenase - metabolism ; Neutrophils - enzymology ; Pancreatic Elastase - blood ; Substrate Specificity</subject><ispartof>The Journal of biological chemistry, 1980-12, Vol.255 (24), p.12006-12010</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-2ae5cfea0d266f4e1d77c42384467a40f75521a05494cebcd195ef143f9467993</citedby><cites>FETCH-LOGICAL-c380t-2ae5cfea0d266f4e1d77c42384467a40f75521a05494cebcd195ef143f9467993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6254989$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mainardi, C L</creatorcontrib><creatorcontrib>Hasty, D L</creatorcontrib><creatorcontrib>Seyer, J M</creatorcontrib><creatorcontrib>Kang, A H</creatorcontrib><title>Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage
through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl
fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid
synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis
indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established
cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively
depleted from the matrix by this enzyme.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Collagen</subject><subject>Humans</subject><subject>Liver Cirrhosis - metabolism</subject><subject>Microbial Collagenase - metabolism</subject><subject>Neutrophils - enzymology</subject><subject>Pancreatic Elastase - blood</subject><subject>Substrate Specificity</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><recordid>eNo9kEtLw0AUhQdRaq3-hMIsRHQRnWeSWUrxUSi4qIK4GSbTO0006cRMouTfmz7wbu7inHPv4UNoSsktJTS-WxLCaKSYTK-pukkI4yJKj9CYkpRHXNL3YzT-t5yisxA-yTBC0REaxUwKlaox-ljWYAtXWGxLMD9mDdg7nHeV2eC2rwHP53NsfVkOygZn_UGqfdlXvqlzv-m2wQaX0H1527eAoTShNQHO0YkzZYCLw56gt8eH19lztHh5ms_uF5HlKWkjZkBaB4asWBw7AXSVJFYwngoRJ0YQl0jJqCFDYWEhsyuqJDgquFODQSk-QVf7u3XjvzsIra6KYGGovAHfBZ1ILgXlbDDKvdE2PoQGnK6bojJNrynRW6Z6x1RvgWmq9I6pTofc9PCgyypY_acOEAf9cq_nxTr_LRrQWeFtDpVmUmomNGWExPwPIeZ-XQ</recordid><startdate>19801225</startdate><enddate>19801225</enddate><creator>Mainardi, C L</creator><creator>Hasty, D L</creator><creator>Seyer, J M</creator><creator>Kang, A H</creator><general>American Society for Biochemistry and Molecular Biology</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>19801225</creationdate><title>Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase</title><author>Mainardi, C L ; Hasty, D L ; Seyer, J M ; Kang, A H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-2ae5cfea0d266f4e1d77c42384467a40f75521a05494cebcd195ef143f9467993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Collagen</topic><topic>Humans</topic><topic>Liver Cirrhosis - metabolism</topic><topic>Microbial Collagenase - metabolism</topic><topic>Neutrophils - enzymology</topic><topic>Pancreatic Elastase - blood</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mainardi, C L</creatorcontrib><creatorcontrib>Hasty, D L</creatorcontrib><creatorcontrib>Seyer, J M</creatorcontrib><creatorcontrib>Kang, A H</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mainardi, C L</au><au>Hasty, D L</au><au>Seyer, J M</au><au>Kang, A H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1980-12-25</date><risdate>1980</risdate><volume>255</volume><issue>24</issue><spage>12006</spage><epage>12010</epage><pages>12006-12010</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage
through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl
fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid
synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis
indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established
cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively
depleted from the matrix by this enzyme.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6254989</pmid><doi>10.1016/S0021-9258(19)70234-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | ScienceDirect® |
subjects | Amino Acid Sequence Amino Acids - analysis Collagen Humans Liver Cirrhosis - metabolism Microbial Collagenase - metabolism Neutrophils - enzymology Pancreatic Elastase - blood Substrate Specificity |
title | Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase |
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