Linked Life Data

10614996

Source:http://linkedlifedata.com/resource/pubmed/id/10614996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2000-3-2
pubmed:abstractText
The recent discovery of tissue prokallikrein (TproK) on the cell surface of human neutrophils prompted this study to test the sensitivity of the kallikrein precursor to proteolysis by neutrophil-derived elastase and cathepsin G. Purified recombinant human TproK was readily degraded by cathepsin G via distinct cleavage sites into two major fragments of 5 and 8 kDa which are devoid of enzymatic activity. Leukocyte elastase caused a rapid conversion of TproK into [des-Ile1]-TK, a differentially processed tissue kallikrein (TK) isoform with truncated N-terminus that appeared to be resistant to further cleavage by elastase. Kinetic data demonstrated the cleavage of amidolytic kallikrein substrates and the release of kinin from HMW kininogen, but the single amino acid deletion results in a severe reduction of catalytic activity for [des-Ile1]-TK compared to the mature enzyme. These in vitro observations support the possibility that the inter-relationships among TproK and neutrophil proteinases may provide a sensitive regulatory system to balance the kallikrein-kinin cascade during inflammatory events.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0162-3109
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-101
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Different susceptibility of human tissue prokallikrein to cleavage by neutrophil proteinases.
pubmed:affiliation
Institute for Biochemistry, Darmstadt University of Technology, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't