Strong myotoxic activity of Trimeresurus malabaricus venom: Role of metalloproteases.

Raghavendra Gowda, C. D. and Rajesh, R. and Nataraju, A. and Dhananjaya, B. L. and Raghupathi, A. R. and Veerabasappa Gowda, T. and Sharath, B. K. and Vishwanath, B. S. (2006) Strong myotoxic activity of Trimeresurus malabaricus venom: Role of metalloproteases. Molecular and Cellular Biochemistry, 282 (1-2, C). pp. 147-155. ISSN 0300-8177

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Official URL: http://dx.doi.org/10.1007/s11010-006-1738-3

Abstract

Trimeresurus malabaricus is an endemic snake found in the Southern region of Western Ghats section of India along with the more widely distributed species like Naja naja and Daboia russelii. T. malabaricus venom is not lethal when injected (i.p.) up to 20 mg/kg body wt. in mice, but causes extensive local tissue degeneration. N. naja and D. russelii are highly toxic (i.p.) with min. local tissue damage in exptl. mice. In this study a comparative anal. of local tissue damage of T. malabaricus venom is made with N. naja and D. russelii snake venoms of the Southern regions of Western Ghats. T. malabaricus venom exhibits caseinolytic activity 16 and 24 times more than N. naja and D. russelii venom. Inhibition studies with specific protease inhibitors reveal that the major proteases belong to metalloproteases. T. malabaricus venom hydrolyzes gelatin and induces strong hemorrhagic activity in mice. Both N. naja and D. russelii fail to hydrolyze gelatin even at very high concn. and did not induce any hemorrhagic activity. With D. russelii venom small hemorrhagic spot was obsd. at the site of injection. The hemorrhagic activity of T. malabaricus venom is completely neutralized by metalloprotease inhibitors and not by serine protease inhibitor. The i.m. injection of T. malabaricus venom causes extensive degrdn. of muscle tissue within 24 h. The light microscopic observation of muscle tissue showed congestion of blood vessels and hemorrhage at the early stage followed by extensive necrosis of muscle fibers. The elevated levels of serum CK and LDH activity further supported the muscle degeneration. Such pathol. symptoms were not seen with N. naja and D. russelii snake venom. The hemorrhagic and the muscle necrosis was completely neutralized by metalloprotease inhibitors and not by serine protease inhibitor strongly suggests that the major toxin component in the T. malabaricus venom is metalloprotease and its activity can be easily neutralized using chelating agents and its use in the first aid as chelation therapy is beneficial. [on SciFinder(R)]

Item Type: Article
Additional Information: Unmapped bibliographic data: PY - 2006/// [EPrints field already has value set] M3 - 10.1007/s11010-006-1738-3 [Field not mapped to EPrints] JA - Mol. Cell. Biochem. [Field not mapped to EPrints]
Uncontrolled Keywords: g1metalloprotease myotoxicity Trimeresurus venom chelator
Subjects: Agriculture Biological Sciences > Biochemistry
University of Mysore > PG Campuses > Manasagangotri, Mysore > Agriculture Biological Sciences > Biochemistry
Divisions: PG Campuses > Manasagangotri, Mysore > Biochemistry
Depositing User: Dhruvakumar
Date Deposited: 12 Jun 2013 10:12
Last Modified: 15 Oct 2015 10:21
URI: http://eprints.uni-mysore.ac.in/id/eprint/12496

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