Linked Life Data

9437193

Source:http://linkedlifedata.com/resource/pubmed/id/9437193

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1998-2-3
pubmed:abstractText
Triflavin, a 7.5-kD cysteine-rich polypeptide purified from Trimeresurus favoviridis snake venom, belongs to a family of Arg-Gly-Asp-(RGD)-containing peptides, termed disintegrins. In this study, aggregating human platelets dose-dependently induced vasoconstriction in de-endothelialized isolated rat thoracic aortas. At 5x10(7) cells per milliliter, platelets induced a peak tension averaging 65 +/- 7.2% of the tension induced by phenylephrine (10 mumol/L). The relative effectiveness of RGD-containing peptides (including venom peptides triflavin and trigramin, small RGD synthetic peptides Gly-Arg-Gly-Asp-Ser [GRGDS], Gly-Arg-Gly-Asp-Phe [GRGDF], and Gly-Arg-Gly-Asp-Ser-Pro-Lys [GRGDSPK]) was examined by testing the inhibitory effect on aggregating platelet-induced vasoconstriction in de-endothelialized aorta. Triflavin (1 mumol/L) significantly inhibited the platelet-induced vasoconstriction, whereas neither trigramin (10 mumol/L) nor small RGD peptides (2 mmol/L) (i.e., GRGDS, GRGDF, and GRGDSPK) showed any significant effect. The release of serotonin and the formation of thromboxane A2 from aggregating platelets were both significantly inhibited by triflavin (2 mumol/L), whereas trigramin and small RGD-containing peptides showed no significant effect. On scanning electron micrographs of de-endothelialized aorta, aggregating platelets adhered to the subendothelium, with loss of their discoid shape, to form irregular spheres with pseudopod extensions. Triflavin (2 mumol/L) markedly reduced the adhesion of platelets to the subendothelium in the same aorta. Furthermore, RGD-containing peptides (including triflavin, trigramin, and small RGD-containing peptides) inhibited the adhesion of 10 micrograms/mL collagen-activated platelets to extracellular matrices (i.e., fibronectin, vitronectin, and von Willebrand factor). It is concluded that the marked ability of triflavin to inhibit aggregating platelet-induced vasoconstriction in de-endothelialized aorta compared with other RGD-containing peptides (including trigramin), may be due at least partly to triflavin's efficiently preventing the activation of platelets subsequent to inhibition of serotonin release and thromboxane A2 formation. However, the different abilities of triflavin compared with other RGD-containing peptides was not related to the ability to inhibit adhesion of platelets to extracellular matrices. Therefore, from the results of this study, it appears that triflavin may be a useful therapeutic agent for the treatment of thromboembolism and its associated angiospasm.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1079-5642
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3461-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9437193-Animals, pubmed-meshheading:9437193-Aorta, pubmed-meshheading:9437193-Blood Platelets, pubmed-meshheading:9437193-Cell Adhesion, pubmed-meshheading:9437193-Collagen, pubmed-meshheading:9437193-Crotalid Venoms, pubmed-meshheading:9437193-Disintegrins, pubmed-meshheading:9437193-Endothelium, Vascular, pubmed-meshheading:9437193-Extracellular Matrix Proteins, pubmed-meshheading:9437193-Female, pubmed-meshheading:9437193-Humans, pubmed-meshheading:9437193-Male, pubmed-meshheading:9437193-Microscopy, Electron, Scanning, pubmed-meshheading:9437193-Oligopeptides, pubmed-meshheading:9437193-Peptides, pubmed-meshheading:9437193-Platelet Aggregation, pubmed-meshheading:9437193-Rats, pubmed-meshheading:9437193-Rats, Sprague-Dawley, pubmed-meshheading:9437193-Serotonin, pubmed-meshheading:9437193-Thromboxane B2, pubmed-meshheading:9437193-Vasoconstriction
pubmed:year
1997
pubmed:articleTitle
Triflavin inhibits platelet-induced vasoconstriction in de-endothelialized aorta.
pubmed:affiliation
Graduate Institute of Medical Sciences, Taipei Medical College, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't