Linked Life Data

6098406

Source:http://linkedlifedata.com/resource/pubmed/id/6098406

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1985-4-9
pubmed:abstractText
The polymorphonuclear leukocyte contains three proteinases capable of degrading the collagenous components of the connective tissue matrix. These proteinases, gelatinase, interstitial collagenase and elastase, were found to be rapidly secreted by the neutrophil in response to soluble stimuli with maximal accumulation of the gelatinase and interstitial collagenase occurring during a 20 minute incubation. When neutrophils were stimulated with the chemotactic peptide, formyl-met-leu-phe, gelatinase was the predominant collagenolytic enzyme detected. Stimulation of neutrophils with increasing doses of the Ca++ ionophore A23187 lead to a sequential release of collagenolytic proteinases. Gelatinase release was detected at Ca++ ionophore concentrations of .05-.1 microM, while significant release of interstitial collagenase required 0.5-1 microM A23187. Elastolytic activity was detected only at high concentrations of A23187 (5-10 microM). No release of lactic acid dehydrogenase was detected indicating that the enzyme release was not due to cell death. These studies suggest that the neutrophil may modulate its collagenolytic potential by selective release of collagenolytic proteinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0174-173X
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
467-77
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Secretion of collagenolytic enzymes by human polymorphonuclear leukocytes.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.