A novel anticoagulant purified from fish protein hydrolysate inhibits factor XIIa and platelet aggregation.
A novel fish protein having anticoagulant and antiplatelet properties was enzymatically extracted from the marine fish, yellowfin sole (Limanda aspera) and purified to homogeneity producing an overall purification fold of 206.6. MALDI-TOF mass spectroscopic and SDS-PAGE analysis identified the purified protein as 12.01 kDa single-chain monomeric protein. It inhibited the activated coagulation factor XII (FXIIa) by forming an inactive complex regardless of Zn2+ mediation, and was named, yellowfin sole anticoagulant protein (YAP). In addition, YAP act to antagonize platelet membrane glycoprotein integrin, to arrest platelet aggregation. However, YAP was not able to block the adhesion of platelets to collagen, which mediate via major collagen receptors, GPIa/IIa on platelet membrane. Furthermore, YAP did not possess plasminogen activator-like activity to activate fibrinolysis. In fact, our findings indicate that YAP binds with FXIIa and platelet membrane integrins to inhibit thrombosis in vitro.
Rajapakse
Niranjan
N
Department of Chemistry, Pukyong National University, Daeyon-3-Dong, Nam-Gu, Busan 608-737, Korea.
Jung
Won-Kyo
WK
Mendis
Eresha
E
Moon
Sung-Hoon
SH
Kim
Se-Kwon
SK
D000818:Animals; D019774:Blood Coagulation Factor Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology*; D001792:Blood Platelets / Q000502:physiology*; D015956:Factor XIIa / Q000037:antagonists & inhibitors*; D005342:Fibrinolysis / Q000187:drug effects; D005399:Fishes; D006801:Humans; D010974:Platelet Aggregation / Q000187:drug effects* / Q000502:physiology; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology
D019774:Blood Coagulation Factor Inhibitors; D010980:Platelet Membrane Glycoproteins; D015956:Factor XIIa