Linked Life Data

8874799

Source:http://linkedlifedata.com/resource/pubmed/id/8874799

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-1-15
pubmed:abstractText
We biochemically characterized a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom. Flavostatin inhibited ADP-, collagen-, and thrombin receptor agonist peptide-induced platelet aggregation in human platelet-rich plasma (IC50 range: 59 to 111 nM) and blocked the binding of biotinylated human fibrinogen to purified GPIIb/IIIa with an inhibitory potency 31,000-fold higher than that of Arg-Gly-Asp-Ser (RGDS). Flavostatin strongly inhibited high-shear-stress-induced platelet aggregation in platelet-rich plasma (PRP) with an IC50 value of 188 nM. Fluorescein isothiocyanate (FITC)-conjugated flavostatin saturably bound to unstimulated and ADP-stimulated washed platelets with high affinity (Kd values: 38 and 21 nM, respectively); the corresponding number of binding sites was 86460 and 79192 per platelet. In competition experiments with several glycoprotein IIb/IIIa antagonists, the binding of FITC-conjugated flavostatin to platelets was completely inhibited by ReoPro, triflavin, TP9201, MK383 and GR144053, but not by YM207, YM337 and B6A3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Biochemical characterization of a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom.
pubmed:affiliation
Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co Ltd, Ibaraki, Japan.
pubmed:publicationType
Journal Article, In Vitro