Linked Life Data

1480040

Source:http://linkedlifedata.com/resource/pubmed/id/1480040

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-2-5
pubmed:abstractText
The tissue inhibitor of metalloproteinases (TIMP, M(r) 30,000) is secreted by many cell and tissue types and has been shown to inhibit most secreted mammalian metalloproteinases. In matrix and tissue invasion assays, the inactivation or removal of TIMP enhances invasiveness. However, many of the cells that secrete TIMP also secrete other metalloproteinase inhibitors. By analysis of medium conditioned by various endothelial, mesenchymal, and neural cells on SDS-.substrate-polyacrylamide-inhibitor gels (reverse zymograms), we have detected at least three other distinct inhibitors of metalloproteinases (IMPs). Some or all of these IMPs have been detected in secretions of mouse, rabbit, sheep, and human cells and are all smaller in apparent molecular size than TIMP (IMP-1, M(r) 26,000; IMP-2, M(r) 21,000; IMP-3, M(r) 18,000). These IMPs are not proteolytic degradation products of TIMP nor do they represent nonglycosylated TIMP. The IMPs do not cross-react in the native or denatured state with any of several anti-TIMP antibodies. The IMPs appear to be regulated independently of each other and of TIMP. In vitro, the complex consisting of one of the IMPs, or TIMP, and a metalloproteinase can be dissociated into functional inhibitor and metalloproteinase. Whether this characteristic is significant in vivo is not known. IMP-2 has been purified from several sources and shares sequence homology with TIMP, suggesting that the IMPs and TIMP may constitute a gene family. The most significant characteristic of IMP-2 is that it appears to preferentially inhibit, on a mole:mole basis, the M(r) 68,000 gelatinase rather than collagenase or stromelysin.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0940-1199
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
294-8
pubmed:dateRevised
2008-2-26
pubmed:meshHeading
pubmed-meshheading:1480040-Amino Acid Sequence, pubmed-meshheading:1480040-Animals, pubmed-meshheading:1480040-Astrocytes, pubmed-meshheading:1480040-Brain Neoplasms, pubmed-meshheading:1480040-Cells, Cultured, pubmed-meshheading:1480040-Culture Media, Conditioned, pubmed-meshheading:1480040-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1480040-Endothelium, Vascular, pubmed-meshheading:1480040-Enzyme Induction, pubmed-meshheading:1480040-Fibroblasts, pubmed-meshheading:1480040-Glioma, pubmed-meshheading:1480040-Glycoproteins, pubmed-meshheading:1480040-Humans, pubmed-meshheading:1480040-Metalloendopeptidases, pubmed-meshheading:1480040-Molecular Sequence Data, pubmed-meshheading:1480040-Molecular Weight, pubmed-meshheading:1480040-Neoplasm Proteins, pubmed-meshheading:1480040-Rabbits, pubmed-meshheading:1480040-Sequence Alignment, pubmed-meshheading:1480040-Sequence Homology, Amino Acid, pubmed-meshheading:1480040-Tetradecanoylphorbol Acetate, pubmed-meshheading:1480040-Tissue Inhibitor of Metalloproteinase-2, pubmed-meshheading:1480040-Tissue Inhibitor of Metalloproteinases, pubmed-meshheading:1480040-Tumor Cells, Cultured
pubmed:year
1992
pubmed:articleTitle
Secreted inhibitors of metalloproteinases (IMPs) that are distinct from TIMP.
pubmed:affiliation
Laboratory of Radiobiology and Environmental Health, University of California, San Francisco.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.