Analysis for sites of anticoagulant action of plancinin, a new anticoagulant peptide isolated from the starfish Acanthaster planci, in the blood coagulation cascade.
1. Effects of plancinin, a new anticoagulant peptide, on the human blood coagulation cascade were investigated. 2. Plancinin prolonged both activated partial thromboplastin time and prothrombin time, and it significantly inhibited factor X activation by both intrinsic (factor IXa-factor VIIIa-phospholipids-Ca2+) and extrinsic (factor VIIa-tissue factor-phospholipids-Ca2+) tenase complexes and prothrombin activation by prothrombinase complex (factor Xa-factor Va-phospholipids-Ca2+) to 13.8%, 4.8% and 10.5% of control value, respectively. 3. Results indicate that sites of anticoagulant action of plancinin may be located in activation steps of prothrombin and factor X.
Department of Pharmacology, School of Medicine, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.
T
T
Koyama
K
K
Noguchi
Y
Y
Aniya
M
M
Sakanashi
D000818:Animals; D017302:Annexins / Q000378:metabolism; D000925:Anticoagulants / Q000302:isolation & purification / Q000494:pharmacology*; D001777:Blood Coagulation / Q000187:drug effects*; D002118:Calcium / Q000494:pharmacology; D010450:Endopeptidases / Q000187:drug effects; D005170:Factor X / Q000187:drug effects; D006801:Humans; D010455:Peptides / Q000494:pharmacology*; D010718:Phosphatidylserines / Q000378:metabolism; D011485:Protein Binding; D011516:Prothrombin / Q000187:drug effects; D013215:Starfish / Q000737:chemistry*
D017302:Annexins; D000925:Anticoagulants; D010455:Peptides; D010718:Phosphatidylserines; D011516:Prothrombin; D005170:Factor X; D010450:Endopeptidases; D002118:Calcium