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rdf:type |
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lifeskim:mentions |
|
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pubmed:issue |
3
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pubmed:dateCreated |
1989-7-10
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pubmed:abstractText |
A potent collagenase inhibitor was purified from cells of calf aorta medial tissue maintained in culture. This molecule was characterized and identified as TIMP (Tissue Inhibitor of Metalloproteinases). Formation of a TIMP--collagenase complex was demonstrated chromatographically using pure TIMP and pure pig synovial cell collagenase. The N-terminal aminoacid sequence of TIMP was determined and, using appropriate oligonucleotide probes the human genes was cloned from a human cDNA bank. This gene was expressed in E. coli, and fully active TIMP was obtained after a denaturation renaturation process. The interest of TIMP as a model for the design of novel collagenase inhibitors is discussed.
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pubmed:language |
fre
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0369-8114
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
199-205
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2542870-Amino Acid Sequence,
pubmed-meshheading:2542870-Animals,
pubmed-meshheading:2542870-Aorta,
pubmed-meshheading:2542870-Cattle,
pubmed-meshheading:2542870-Cloning, Molecular,
pubmed-meshheading:2542870-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2542870-Enzyme Inhibitors,
pubmed-meshheading:2542870-Escherichia coli,
pubmed-meshheading:2542870-Humans,
pubmed-meshheading:2542870-Metalloendopeptidases,
pubmed-meshheading:2542870-Microbial Collagenase,
pubmed-meshheading:2542870-Molecular Sequence Data,
pubmed-meshheading:2542870-Oligonucleotide Probes,
pubmed-meshheading:2542870-Protein Denaturation,
pubmed-meshheading:2542870-Recombinant Proteins,
pubmed-meshheading:2542870-Swine,
pubmed-meshheading:2542870-Synovial Membrane,
pubmed-meshheading:2542870-Tissue Inhibitor of Metalloproteinases
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pubmed:year |
1989
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pubmed:articleTitle |
[Natural inhibitor of metalloproteinases: structural and functional study].
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pubmed:affiliation |
Rhône-Poulenc Santé (CRMA), Site de Recherche de Monts, France.
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pubmed:publicationType |
Journal Article,
English Abstract
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