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.
Koyama
T
T
Department of Pharmacology, School of Medicine, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.
Noguchi
K
K
Aniya
Y
Y
Sakanashi
M
M
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