An Updated Inventory on Properties,Pathophysiology and Therapeutic Potential of Snake Venom Thrombin-Like Proteases

Abstract

Venom from viperidae family of snakes contains highly specific proteases affecting the blood coagulation mechanism and hence interferes with the haemostatic mechanism of victim. A special class of venom serine proteases functionally resembles with thrombin (coagulant serine proteases) is known as Snake Venom Thrombin-like Enzymes (SVTLEs). The coagulant serine proteases are able to clot fibrinogen in in vitro condition by virtue of their ability to release either fibrinopeptide A, or B or both A and B from fibrinogen however, in in vivo condition they cause defibrinogenation of plasma. Despite a high degree of similarity in primary structure, a minor variation or substitution in the subsites of the active site of the SVTLEs may lead to differences in the substrate specificity amongst these enzymes resulting in displaying different biological activity by these enzymes. The SVTLEs are mostly glycoprotein in nature however; contradictory and fragmentary data are available concerning the role of glycosylation on biological activity of these enzymes. During the last few decades, SVTLEs are subject of intensive research for their possible therapeutic application in the treatment of hyperfibrinogenemia related disorders as well as development of diagnostic reagents for clinical study. The present review provides up to date information available on structure-function properties, pathophysiology and therapeutic application of SVTLEs covering a period from 2007 to till date.