Linked Life Data

11910182

Source:http://linkedlifedata.com/resource/pubmed/id/11910182

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-6
pubmed:dateCreated
2002-3-22
pubmed:abstractText
A novel C-lectin protein, lebecetin, was purified and characterized from the venom of Macrovipera lebetina. It is a disulfide-linked heterodimer of 15 and 16 kD. The subunits are homologous to each other and to the other snake venom proteins of the C-type (Ca(2+)-dependent) lectin superfamily. Lebecetin shows a potent inhibitory effect on whole blood and washed platelets induced by different agonists. It inhibits the agglutination of human fixed platelets in the presence of ristocetin. Lebecetin also interferes with the adhesion of IGR39 melanoma and HT29D4 adenocarcinoma cells. These two lines adhere to lebecetin used as matrix. Lebecetin is also able to strongly reduce IGR39 and HT29D4 cell adhesion to fibrinogen and laminin, but not to fibronectin and collagen types I and IV, respectively. Adhesion properties of lebecetin may thus involve integrin receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-0147
pubmed:author
pubmed:copyrightInfo
Copyright 2002 S. Karger AG, Basel
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-6
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:articleTitle
Lebecetin, a C-lectin protein from the venom of Macrovipera lebetina that inhibits platelet aggregation and adhesion of cancerous cells.
pubmed:affiliation
Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, 13 Place Pasteur, BP 74, 1001 Tunis-Belvédère, Tunisia. sameh_sarray@voila.fr
pubmed:publicationType
Journal Article