Poster 209.  Congresso da Sociedade Brasileira de Toxinologia, 8., Symposium of the Pan American Section of the International Society on Toxinology, 8., 2004, Angra dos Reis, Brasil.  Abstracts...  J. Venom. Anim. Toxins incl.Trop. Dis., 2004, 10, 3, p.568.

 

 

A Disintegrin from the Venom of the Trans-Pecos Copperhead (Agkistrodon contortrix pictigaster) Inhibiting Platelet Aggregation and Cancer Cell Adhesion

 

G López1, EE Sánchez1,2 , JA Galán1, A Rodríguez-Acosta2, JC Pérez1

 

1 Natural Toxins Research Center (NTRC), Texas A&M University-Kingsville, Kingsville, Tx 78363 USA; 2 Universidad Central de Venezuela, Instituto de Medicina Tropical, Sección se Inmunoquímica, Caracas 1041, Venezuela

 

A disintegrin having a molecular weight of 13.5kDa has been isolated from the venom of the Trans-Pecos Copperhead (Agkistrodon contortrix pictigaster). Disintegrins are low molecular weight, cysteine-rich peptides, and many are found in snake venom. Disintegrins contain a common three sequence binding site which acts as an antagonist against platelet aggregation and cell adhesion. To date, over 90 disintegrins have been identified primarily from snake venoms. Initial fractionation of the crude venom was done by cation exchange chromatography. Further separation of the active fraction was done by reverse phase C18 chromatography. Fraction 10 (ACP100-10) inhibited ADP-induced platelet aggregation and platelet retraction in whole human blood by a Chrono-Log Aggregometer and a Sonoclot® Coagulation and Platelet Function Analyzer, respectively. ACP100-10 was also a very important inhibitor of tumor cell (T24, human urinary bladder carcinoma) adhesion to fibronectin.

 

Correspondence to: kaees00@tamuk.edu