Source:http://linkedlifedata.com/resource/pubmed/id/10471791
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-10-14
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pubmed:databankReference | |
pubmed:abstractText |
A matrix metalloproteinase (MMP)-like gene was identified in mouse to contain a conserved MMP catalytic domain and an RRRR motif. It lacks a classic cysteine switch, but it possesses two novel motifs: a cysteine array (Cys-X(6)-Cys-X(8)-Cys-X(10)-Cys-X(3)-Cys-X(2)-Cys), and a novel Ig-fold. It is named CA-MMP after the distinct cysteine array motif, and little is known about its biochemical function. In an attempt to characterize CA-MMP activity, the full-length sequence was expressed in mammalian cells and its product found to be cell-associated without detectable secretion. In light of this unusual finding, a chimera combining the catalytic domain of CA-MMP with the prodomain of stromelysin-3 was constructed to express a fully active enzyme in mammalian cells. Purified CA-MMP catalytic domain expresses proteolytic activity against protein substrates in an MMP inhibitor sensitive fashion. Taken together, it is concluded that CA-MMP is an MMP with distinct structure, biochemical properties and evolutionary history that may define a new subclass of the MMP superfamily.
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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/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 12,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
457
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
262-70
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10471791-Amino Acid Sequence,
pubmed-meshheading:10471791-Animals,
pubmed-meshheading:10471791-Base Sequence,
pubmed-meshheading:10471791-COS Cells,
pubmed-meshheading:10471791-Cloning, Molecular,
pubmed-meshheading:10471791-Cysteine,
pubmed-meshheading:10471791-DNA, Complementary,
pubmed-meshheading:10471791-Embryo, Mammalian,
pubmed-meshheading:10471791-Exons,
pubmed-meshheading:10471791-Extracellular Matrix,
pubmed-meshheading:10471791-Introns,
pubmed-meshheading:10471791-Matrix Metalloproteinase 12,
pubmed-meshheading:10471791-Matrix Metalloproteinases,
pubmed-meshheading:10471791-Metalloendopeptidases,
pubmed-meshheading:10471791-Mice,
pubmed-meshheading:10471791-Molecular Sequence Data,
pubmed-meshheading:10471791-Sequence Homology, Amino Acid
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pubmed:year |
1999
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pubmed:articleTitle |
CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch.
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pubmed:affiliation |
Department of Pharmacology, 3-249 Millard Hall, 435 Delaware St. S.E. ,University of Minnesota, Minneapolis, MN, USA. peixx003@tc.umn.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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