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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
45
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pubmed:dateCreated |
1996-12-30
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pubmed:abstractText |
Vertebrate collagenases, matrix metalloproteinases (MMPs), cleave type I collagen at a single helical locus. We show here that rodent interstitial collagenases (MMP-13), but not human fibroblast collagenase (MMP-1), cleave type I collagen at an additional aminotelopeptide locus. Collagenase cDNAs and chimeric constructs in pET-3d, juxtaposing MMP-13 sequences amino-terminal to the active site in the catalytic domain and MMP-1 sequences carboxyl-terminal and vice versa, were expressed in Escherichia coli. Assays utilized collagen from wild type (+/+) mice or mice that carry a targeted mutation (r/r) that encodes substitutions in alpha1(I) chains that prevent collagenase cleavage at the helical locus. MMP-13 and chimeric molecules that contained the MMP-13 sequences amino-terminal to the active site cleaved (+/+) collagen at the helical locus and cleaved cross-linked (r/r) collagen in the aminotelopeptide (beta components converted to alpha chains). Human MMP-1 and chimeric MMP-1/MMP-13 with MMP-1 sequences amino-terminal to the active site cleaved collagen at the helical locus but not in the aminotelopeptide. All activities were inhibited by TIMP-1, 1,10-phenanthroline, and EDTA. Sequences in the distal two-thirds of the catalytic domain determine the aminotelopeptide-degrading capacity of MMP-13.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/collagen type I trimeric...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28509-15
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8910479-Amino Acid Sequence,
pubmed-meshheading:8910479-Animals,
pubmed-meshheading:8910479-Collagen,
pubmed-meshheading:8910479-Collagen Type I,
pubmed-meshheading:8910479-Collagenases,
pubmed-meshheading:8910479-Enzyme Inhibitors,
pubmed-meshheading:8910479-Fibroblasts,
pubmed-meshheading:8910479-Glycoproteins,
pubmed-meshheading:8910479-Humans,
pubmed-meshheading:8910479-Matrix Metalloproteinase 1,
pubmed-meshheading:8910479-Mice,
pubmed-meshheading:8910479-Molecular Sequence Data,
pubmed-meshheading:8910479-Mutagenesis, Site-Directed,
pubmed-meshheading:8910479-Peptides,
pubmed-meshheading:8910479-Rats,
pubmed-meshheading:8910479-Tissue Inhibitor of Metalloproteinases
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pubmed:year |
1996
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pubmed:articleTitle |
Different collagenase gene products have different roles in degradation of type I collagen.
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pubmed:affiliation |
Department of Medicine, Harvard Medical School and the Arthritis Unit, Massachusetts General Hospital, Boston, Massachusetts 02114, USA. kranes@A1.mgh.harvard.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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