Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-7-31
pubmed:abstractText
Metalloproteinases (haemorrhagic or non-haemorrhagic), disintegrins and most probably C-type lectin-related proteins are derived by the proteolysis of a common precursor protein. There is a short interdomain segment between the metalloproteinase and disintegrin domains which will be released into the venom. To determine whether this region of the molecule contributes to the biological role of the precursors or the products derived by the proteolysis of the precursors, we synthesized a peptide based on this short segment and examined its toxicity and biological activity. The synthetic peptide did not show any lethal toxicity, anticoagulant and antiplatelet effects. However, the peptide appeared to lower the blood pressure or normotensive rats upon infusion, but did not affect the blood levels of triglyceride, total cholesterol, high-density lipoproteins or low-density lipoproteins. The peptide, however, failed to exhibit any effect on spontaneously hypertensive rats and hence may not have a potential as an antihypertensive agent. Based on these results, we conclude that this interdomain segment may not contribute significantly to the biological activity of precursor proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
529-35
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Pharmacological activity of the interdomain segment between metalloproteinase and disintegrin domains.
pubmed:affiliation
Bioscience Centre, Faculty of Science, National University of Singapore, Singapore.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't