Degradation of type IV (basement membrane) collagen by a proteinase isolated from human polymorphonuclear leukocyte granules
A serine esterase with potent proteolytic activity against native bovine lens capsule type IV collagen was isolated and purified from extract of human polymorphonuclear leukocytes (PMN). The type IV collagenolytic activity co-purified with N-t-benzyloxycarbonyl-L-alanine nitroanilidase, and was inhi...
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| Veröffentlicht in: | The Journal of biological chemistry 1980-06, Vol.255 (11), p.5435-5441 |
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| container_title | The Journal of biological chemistry |
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| creator | Mainardi, C L Dixit, S N Kang, A H |
| description | A serine esterase with potent proteolytic activity against native bovine lens capsule type IV collagen was isolated and purified
from extract of human polymorphonuclear leukocytes (PMN). The type IV collagenolytic activity co-purified with N-t-benzyloxycarbonyl-L-alanine
nitroanilidase, and was inhibited by phenylmethanesulfonyl fluoride and N-acetyl-Ala-Ala-Ala-Ala chloromethyl ketone. In addition,
the purified enzyme had elastolytic activity, reacted with a specific antibody to PMN elastase, and, therefore, appeared to
be identical with this enzyme. A simple, reproducible assay for the detection of type IV collagenase activity using insoluble
bovine anterior lens capsule collagen was defined. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that
the enzyme released large molecular weight peptides (greater than 30,000) from the insoluble substrate. The enzyme was also
active against native, pepsin-solubilized type IV collagen; five reaction products could be identified. These data suggest
that PMN elastase may be involved in the degradation of basement membrane collagen in physiologic and pathologic states. |
| doi_str_mv | 10.1016/S0021-9258(19)70805-9 |
| format | Article |
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from extract of human polymorphonuclear leukocytes (PMN). The type IV collagenolytic activity co-purified with N-t-benzyloxycarbonyl-L-alanine
nitroanilidase, and was inhibited by phenylmethanesulfonyl fluoride and N-acetyl-Ala-Ala-Ala-Ala chloromethyl ketone. In addition,
the purified enzyme had elastolytic activity, reacted with a specific antibody to PMN elastase, and, therefore, appeared to
be identical with this enzyme. A simple, reproducible assay for the detection of type IV collagenase activity using insoluble
bovine anterior lens capsule collagen was defined. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that
the enzyme released large molecular weight peptides (greater than 30,000) from the insoluble substrate. The enzyme was also
active against native, pepsin-solubilized type IV collagen; five reaction products could be identified. These data suggest
that PMN elastase may be involved in the degradation of basement membrane collagen in physiologic and pathologic states.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)70805-9</identifier><identifier>PMID: 6989826</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Basement Membrane - analysis ; Cathepsins ; Cattle ; Collagen ; Cytoplasmic Granules - enzymology ; Humans ; Hydroxyproline - analysis ; Lens, Crystalline - analysis ; Molecular Weight ; Neutrophils - enzymology ; Pancreatic Elastase ; Peptide Fragments - analysis ; Peptide Hydrolases - blood</subject><ispartof>The Journal of biological chemistry, 1980-06, Vol.255 (11), p.5435-5441</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-931ce9d0dad6f7fb89238e6b0ab37c29ab79267f54a9b3fc44019f9b8c720f693</citedby><cites>FETCH-LOGICAL-c431t-931ce9d0dad6f7fb89238e6b0ab37c29ab79267f54a9b3fc44019f9b8c720f693</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/6989826$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mainardi, C L</creatorcontrib><creatorcontrib>Dixit, S N</creatorcontrib><creatorcontrib>Kang, A H</creatorcontrib><title>Degradation of type IV (basement membrane) collagen by a proteinase isolated from human polymorphonuclear leukocyte granules</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A serine esterase with potent proteolytic activity against native bovine lens capsule type IV collagen was isolated and purified
from extract of human polymorphonuclear leukocytes (PMN). The type IV collagenolytic activity co-purified with N-t-benzyloxycarbonyl-L-alanine
nitroanilidase, and was inhibited by phenylmethanesulfonyl fluoride and N-acetyl-Ala-Ala-Ala-Ala chloromethyl ketone. In addition,
the purified enzyme had elastolytic activity, reacted with a specific antibody to PMN elastase, and, therefore, appeared to
be identical with this enzyme. A simple, reproducible assay for the detection of type IV collagenase activity using insoluble
bovine anterior lens capsule collagen was defined. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that
the enzyme released large molecular weight peptides (greater than 30,000) from the insoluble substrate. The enzyme was also
active against native, pepsin-solubilized type IV collagen; five reaction products could be identified. These data suggest
that PMN elastase may be involved in the degradation of basement membrane collagen in physiologic and pathologic states.</description><subject>Animals</subject><subject>Basement Membrane - analysis</subject><subject>Cathepsins</subject><subject>Cattle</subject><subject>Collagen</subject><subject>Cytoplasmic Granules - enzymology</subject><subject>Humans</subject><subject>Hydroxyproline - analysis</subject><subject>Lens, Crystalline - analysis</subject><subject>Molecular Weight</subject><subject>Neutrophils - enzymology</subject><subject>Pancreatic Elastase</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Hydrolases - blood</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE9v1DAQxS0EKtvCR6hkCQm1h4AnjpP4iFoKlSpx4I-4WbYz3gRiO9iJUCQ-PNnuqnOZw3szb-ZHyCWwd8Cgfv-VsRIKWYr2CuR1w1omCvmM7IC1vOACfj4nuyfLS3Ke8y-2VSXhjJzVspVtWe_Iv1vcJ93peYiBRkfndUJ6_4NeGZ3RY5ipR2-SDnhNbRxHvcdAzUo1nVKccQibjQ45jnrGjroUPe0XrwOd4rj6mKY-hsWOqBMdcfkd7Toj3RLDMmJ-RV44PWZ8feoX5Pvdx283n4uHL5_ubz48FLbiMBeSg0XZsU53tWucaWXJW6wN04Y3tpTaNLKsGycqLQ13tqoYSCdNa5uSuVryC_L2uHe7-c-CeVZ-yBa3bwLGJatGABMM-GYUR6NNMeeETk1p8DqtCpg6UFeP1NUBqQKpHqmrQ8DlKWAxHrunqRPmTX9z1Pth3_8dEiozRNujV6UQCkCJigv-HwXSi8E</recordid><startdate>19800610</startdate><enddate>19800610</enddate><creator>Mainardi, C L</creator><creator>Dixit, S N</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>19800610</creationdate><title>Degradation of type IV (basement membrane) collagen by a proteinase isolated from human polymorphonuclear leukocyte granules</title><author>Mainardi, C L ; Dixit, S N ; Kang, A H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-931ce9d0dad6f7fb89238e6b0ab37c29ab79267f54a9b3fc44019f9b8c720f693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Animals</topic><topic>Basement Membrane - analysis</topic><topic>Cathepsins</topic><topic>Cattle</topic><topic>Collagen</topic><topic>Cytoplasmic Granules - enzymology</topic><topic>Humans</topic><topic>Hydroxyproline - analysis</topic><topic>Lens, Crystalline - analysis</topic><topic>Molecular Weight</topic><topic>Neutrophils - enzymology</topic><topic>Pancreatic Elastase</topic><topic>Peptide Fragments - analysis</topic><topic>Peptide Hydrolases - blood</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mainardi, C L</creatorcontrib><creatorcontrib>Dixit, S N</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>Dixit, S N</au><au>Kang, A H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Degradation of type IV (basement membrane) collagen by a proteinase isolated from human polymorphonuclear leukocyte granules</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1980-06-10</date><risdate>1980</risdate><volume>255</volume><issue>11</issue><spage>5435</spage><epage>5441</epage><pages>5435-5441</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A serine esterase with potent proteolytic activity against native bovine lens capsule type IV collagen was isolated and purified
from extract of human polymorphonuclear leukocytes (PMN). The type IV collagenolytic activity co-purified with N-t-benzyloxycarbonyl-L-alanine
nitroanilidase, and was inhibited by phenylmethanesulfonyl fluoride and N-acetyl-Ala-Ala-Ala-Ala chloromethyl ketone. In addition,
the purified enzyme had elastolytic activity, reacted with a specific antibody to PMN elastase, and, therefore, appeared to
be identical with this enzyme. A simple, reproducible assay for the detection of type IV collagenase activity using insoluble
bovine anterior lens capsule collagen was defined. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that
the enzyme released large molecular weight peptides (greater than 30,000) from the insoluble substrate. The enzyme was also
active against native, pepsin-solubilized type IV collagen; five reaction products could be identified. These data suggest
that PMN elastase may be involved in the degradation of basement membrane collagen in physiologic and pathologic states.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6989826</pmid><doi>10.1016/S0021-9258(19)70805-9</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1980-06, Vol.255 (11), p.5435-5441 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Basement Membrane - analysis Cathepsins Cattle Collagen Cytoplasmic Granules - enzymology Humans Hydroxyproline - analysis Lens, Crystalline - analysis Molecular Weight Neutrophils - enzymology Pancreatic Elastase Peptide Fragments - analysis Peptide Hydrolases - blood |
| title | Degradation of type IV (basement membrane) collagen by a proteinase isolated from human polymorphonuclear leukocyte granules |
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