| Co-Investigator(Kenkyū-buntansha) |
KOIKE Hisashi MEIJI PHARMACEUTICAL UNIVERSITY, FACULTY OF PHARMACY, Instructor, 薬学部, 助手 (50328978)
TORIBE Michihisa The Japan Snake Institute, Director, 所長 (40109856)
ATODA Hideko MEIJI PHARMACEUTICAL UNIVERSITY, FACULTY OF PHARMACY, Associate Professor, 薬学部, 助教授 (20221046)
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| Research Abstract |
Snake venom contains a diverse range of interesting proteins, including procoagulants, anticoagulants, fibrinolytic components, platelet agonists, platelet antagonists, and hemorrhagic components. One of the functional components of snake venom is a member of the C-type lectin-like protein (CLP) family that includes factor IX/X-binding protein (IX-X-bp), carinactivase-1 (calcium-dependent prothrombin activator), RVV-X (factor X activator of Russell's viper venom), alboaggregin-B (platelet agonist), and flavocetin-A (platelet antagonist). These CLPs perform a variety of activities, and various CLPs have been sequenced. CLPs have proved to be useful tools in elucidating the complex mechanisms involved in clotting and platelet formation and the structure-function relationship of human clotting factors and glycoproteins of platelets.
We isolated, characterized, and cloned genes for three novel CRISP family proteins (piscivorin, ophanin, and catrin) from the venom of eastern cottonmouth (Agkislrodon piscivorus piscivorus), king cobra (Ophiophagus hannah), and western diamondback rattlesnake (Crotalus atrox). Our results show the wide distribution of snake venom CRISP family proteins among Viperidae and Elapidae from different continents, indicating that CRISP family proteins compose a new group of snake venom proteins.
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