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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
1993-7-27
|
| pubmed:abstractText |
Multiple forms of metalloproteinase inhibitors were found in the serum-free conditioned medium of the EJ-1 human bladder carcinoma cell line by reverse zymography assay with gelatinase A as the indicator enzyme. Two novel forms of inhibitor with apparent molecular masses of 18 and 22 kDa on nonreducing SDS-polyacrylamide gel electrophoresis (PAGE), together with tissue inhibitor of metalloproteinases (TIMP) and TIMP-2, were purified from the conditioned medium by a series of chromatographic steps. Structural analysis showed that the 18-kDa inhibitor is a two-chain form of TIMP-2 (tc-TIMP-2) produced by proteolytic processing, and the 22-kDa inhibitor may be a partially glycosylated form of TIMP. The purified tc-TIMP-2 was separated into a 17-kDa peptide and a small peptide of about 2.5 kDa by reducing SDS-PAGE and into four isoforms with pI 7.6, 7.3, 7.2, and 6.8 by isoelectric focusing. tc-TIMP-2 has essentially the same inhibitory activity as TIMP-2 toward gelatinase A, collagenase, stromelysin, and matrilysin. Unlike TIMP-2, however, tc-TIMP-2 does not bind to the latent precursor fo gelatinase A. Similar two-chain forms of TIMP-2 were produced by its partial digestion with trypsin or less effectively with plasmin. These results suggest that proteolytic processing of TIMP-2 plays a role in the regulation of gelatinase A activity in the extracellular matrix.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
14387-93
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8314798-Amino Acid Sequence,
pubmed-meshheading:8314798-Chromatography, High Pressure Liquid,
pubmed-meshheading:8314798-Chromatography, Ion Exchange,
pubmed-meshheading:8314798-Culture Media, Conditioned,
pubmed-meshheading:8314798-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8314798-Endopeptidases,
pubmed-meshheading:8314798-Humans,
pubmed-meshheading:8314798-Isoelectric Focusing,
pubmed-meshheading:8314798-Matrix Metalloproteinase 2,
pubmed-meshheading:8314798-Metalloendopeptidases,
pubmed-meshheading:8314798-Models, Structural,
pubmed-meshheading:8314798-Molecular Sequence Data,
pubmed-meshheading:8314798-Molecular Weight,
pubmed-meshheading:8314798-Neoplasm Proteins,
pubmed-meshheading:8314798-Peptide Fragments,
pubmed-meshheading:8314798-Protein Structure, Secondary,
pubmed-meshheading:8314798-Tissue Inhibitor of Metalloproteinase-2,
pubmed-meshheading:8314798-Tumor Cells, Cultured,
pubmed-meshheading:8314798-Urinary Bladder Neoplasms
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Purification and characterization of a two-chain form of tissue inhibitor of metalloproteinases (TIMP) type 2 and a low molecular weight TIMP-like protein.
|
| pubmed:affiliation |
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Japan.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|