TY - JOUR
T1 - Differential action of proteases from Trimeresurus malabaricus, Naja naja and Daboia russellii venoms on hemostasis
AU - Gowda, Raghavendra
AU - Nataraju, A.
AU - Rajesh, R.
AU - Dhananjaya, B. L.
AU - Sharath, B. K.
AU - Vishwanath, B. S.
N1 - Funding Information:
We acknowledge the support of Mr. R.M. Ray, Chief Wildlife Warden, Karnataka State Forest Department, Government of Karnataka, for his support and permission to carry out this work. We thank Dr. Madanlal, Director, Karnataka cardio diagnostic center, Mysore-570 001. A. Nataraju and R. Rajesh acknowledge the Council of Scientific and Industrial Research (CSIR), New Delhi, India for financial assistance. Authors also thank the Department of Studies in Applied Botany and Biotechnology, University of Mysore, Mysore for Electrophoresis gel documentation.
PY - 2006/7
Y1 - 2006/7
N2 - The action of venom proteases and their role in hemostasis has been compared in the venoms of Trimeresurus malabaricus, Daboia russellii and Naja naja from the Southern region of Western Ghats, India. These venoms exhibit varying amounts of proteolytic activity and also influence hemostasis differently. Casein hydrolyzing activity of T. malabaricus venoms was 16 and 24 fold higher than those of N. naja and D. russellii venoms, respectively. With the synthetic substrate TAME, the highest activity was observed in T. malabaricus venom. N. naja venom did not hydrolyze TAME even at higher concentrations. These variations in proteolytic activity also influenced the coagulation process. T. malabaricus and D. russellii venoms are strongly procoagulant and reduce the re-calcification time from 148 to 14 and 12 s, respectively. Similarly, both T. malabaricus and D. russellii venoms reduce the prothrombin time from 12.5 to 6.0 s. On the other hand, N. naja venom is anticoagulant and prolongs re-calcification time to 600 s and prothrombin time to 42 s. In spite of varied effects on hemostasis, all the venoms hydrolyze fibrinogen. T. malabaricus venom hydrolyses both Aα and Bβ subunits. While D. russellii and N. naja venoms hydrolyse only Aα. None of these venoms hydrolyze the γ subunit of fibrinogen. Inhibition studies with specific protease inhibitors revealed that both N. naja and T. malabaricus venoms contain only metalloproteases. D. russellii venom contained both serine and metalloproteases. Only, T. malabaricus venom exhibited thrombin-like activity and induces fibrin clot formation with purified fibrinogen within 58 s. Even though D. russellii venom exhibits procoagulant activity, it did not show thrombin-like activity and may act on other coagulation factors.
AB - The action of venom proteases and their role in hemostasis has been compared in the venoms of Trimeresurus malabaricus, Daboia russellii and Naja naja from the Southern region of Western Ghats, India. These venoms exhibit varying amounts of proteolytic activity and also influence hemostasis differently. Casein hydrolyzing activity of T. malabaricus venoms was 16 and 24 fold higher than those of N. naja and D. russellii venoms, respectively. With the synthetic substrate TAME, the highest activity was observed in T. malabaricus venom. N. naja venom did not hydrolyze TAME even at higher concentrations. These variations in proteolytic activity also influenced the coagulation process. T. malabaricus and D. russellii venoms are strongly procoagulant and reduce the re-calcification time from 148 to 14 and 12 s, respectively. Similarly, both T. malabaricus and D. russellii venoms reduce the prothrombin time from 12.5 to 6.0 s. On the other hand, N. naja venom is anticoagulant and prolongs re-calcification time to 600 s and prothrombin time to 42 s. In spite of varied effects on hemostasis, all the venoms hydrolyze fibrinogen. T. malabaricus venom hydrolyses both Aα and Bβ subunits. While D. russellii and N. naja venoms hydrolyse only Aα. None of these venoms hydrolyze the γ subunit of fibrinogen. Inhibition studies with specific protease inhibitors revealed that both N. naja and T. malabaricus venoms contain only metalloproteases. D. russellii venom contained both serine and metalloproteases. Only, T. malabaricus venom exhibited thrombin-like activity and induces fibrin clot formation with purified fibrinogen within 58 s. Even though D. russellii venom exhibits procoagulant activity, it did not show thrombin-like activity and may act on other coagulation factors.
UR - http://www.scopus.com/inward/record.url?scp=33744914362&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33744914362&partnerID=8YFLogxK
U2 - 10.1016/j.cbpc.2006.03.001
DO - 10.1016/j.cbpc.2006.03.001
M3 - Article
C2 - 16627005
AN - SCOPUS:33744914362
SN - 1532-0456
VL - 143
SP - 295
EP - 302
JO - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
JF - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
IS - 3
ER -