Platelet aggregation and exogenous factors from animal sources.
Platelet aggregation plays a crucial role in thrombosis. This review describes exogenous factors isolated from various animal sources, including venoms and the salivary glands that interfere in platelet aggregation. Some of these factors induce platelet aggregation or agglutination, whereas others inhibit platelet aggregation. These proteins range from small molecular weight peptides to large proteins. Some of these proteins exhibit various enzymatic activities, while others are nonenzymatic. These exogenous factors affect platelet aggregation by various mechanisms and thus they have been classified based on their mechanism of action. Many of these proteins have evolved through both convergent and divergent evolution. For example, platelet aggregation inhibitors, which interfere in the interactions between fibrinogen and its receptor, the glycoprotein IIb/IIIa complex, show extreme structural diversity but they share the common functional site of Arg-Gly-Asp (RGD) tripeptide segment. On the other hand, C-type lectin related proteins exhibit diverse biological effects by interacting with different proteins, but share common structural scaffold. Thus the mechanistic and structure-function studies of these exogenous proteins have contributed significantly to the understanding of molecular mechanisms of platelet aggregation and to the development of potent antiplatelet agents, respectively. A number of new exogenous factors have been identified recently and the search is still on for novel factors that interfere with platelet aggregation. Further studies in this area will help in the development of novel strategies for treating cardiovascular and hematological disorders.
Kini
R Manjunatha
RM
Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543. dbskinim@nus.edu.sg
D000818:Animals; D001685:Biological Factors / Q000737:chemistry* / Q000494:pharmacology*; D019483:Disintegrins / Q000737:chemistry / Q000494:pharmacology; D004546:Elapid Venoms / Q000737:chemistry / Q000201:enzymology; D006384:Hemagglutination / Q000187:drug effects; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000494:pharmacology; D010974:Platelet Aggregation / Q000187:drug effects*; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D012469:Salivary Glands / Q000201:enzymology / Q000378:metabolism; D014757:Viper Venoms / Q000737:chemistry / Q000201:enzymology
D001685:Biological Factors; D019483:Disintegrins; D004546:Elapid Venoms; D037102:Lectins; D010975:Platelet Aggregation Inhibitors; D014757:Viper Venoms