Linked Life Data

8027075

Source:http://linkedlifedata.com/resource/pubmed/id/8027075

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1994-8-8
pubmed:abstractText
In inflamed tissue sites characterized by on-going matrix degradation, the matrix metalloproteinases are secreted as latent precursors which are capable of proteolysis only after extracellular activation. Such areas often contain locally increased numbers of mast cells capable of releasing complexes between heparin proteoglycans and fully active endopeptidases with either tryptic (tryptase) or both tryptic and chymotryptic (chymase) activity. We have examined the ability of purified human skin chymase to activate human interstitial procollagenase (matrix metalloproteinase-1) in the absence and presence of heparin, the physiologic associate of chymase. Our studies indicate that chymase activates procollagenase in a time- and concentration-dependent manner. Heparin was found to increase markedly the rate at which chymase activates procollagenase both by accelerating the cleavage of procollagenase and also by preventing its further degradation. Moreover, we found that chymase activates procollagenase directly by cleaving the Leu83-Thr84 bond, without formation of any intermediate species. This is a novel mechanism for procollagenase activation, which contrasts sharply with the activation mechanisms of other activators studied so far. The ability of chymase to activate procollagenase suggests that chymase plays an active role in matrix degradation at tissue sites where mast cells coexist with extracellular procollagenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18134-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Activation of human interstitial procollagenase through direct cleavage of the Leu83-Thr84 bond by mast cell chymase.
pubmed:affiliation
Wihuri Research Institute, Helsinki, Finland.
pubmed:publicationType
Journal Article