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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1995-3-29
|
| pubmed:abstractText |
Serine proteinase inhibitors play a major role in the turnover of connective tissues. In this study, we isolated and determined partial amino-terminal amino acid sequence of trypsin/elastase/plasmin inhibitors (M(r) 33,000 and 31,000) from the extracellular matrix of SV40-transformed human skin fibroblasts. The antitrypsin activity of the inhibitors was monitored by substrate reverse zymography. Polyclonal antisera to alpha 1-antitrypsin, alpha 1-antichymotrypsin, alpha 2-antiplasmin, inter-alpha-trypsin inhibitor, plasminogen activator inhibitors-1 and -2, and a monoclonal antibody to protease nexin-1 did not label the 33-, 31-, and 27-kDa inhibitors. A computer search for amino acid sequence homology indicated that the 31-kDa inhibitor is novel. In contrast, the sequence of the 33-kDa inhibitor shared 70 to 90% homology with the amino-terminal sequence of a recently characterized 32-kDa trypsin/tissue factor inhibitor called tissue factor pathway inhibitor-2. The 33- and 31-kDa inhibitors bind to heparin-Sepharose and were recovered from the affinity beads as well as from the t12 FB extracellular matrix with 1 M NaCl. Based on these results, we propose that the extracellular matrix of human mesenchymal cells sequester a family of novel serine proteinase inhibitors.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0003-9861
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
317
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
311-4
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:7872799-Amino Acid Sequence,
pubmed-meshheading:7872799-Cell Line, Transformed,
pubmed-meshheading:7872799-Extracellular Matrix,
pubmed-meshheading:7872799-Fibroblasts,
pubmed-meshheading:7872799-Humans,
pubmed-meshheading:7872799-Molecular Sequence Data,
pubmed-meshheading:7872799-Sequence Homology, Amino Acid,
pubmed-meshheading:7872799-Serine Proteinase Inhibitors,
pubmed-meshheading:7872799-Skin
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Novel extracellular matrix-associated serine proteinase inhibitors from human skin fibroblasts.
|
| pubmed:affiliation |
Department of Dermatology, Northwestern University Medical School, Northwestern University, Chicago, Illinois 60611.
|
| pubmed:publicationType |
Journal Article
|