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Disease relevance of Trimeresurus


High impact information on Trimeresurus

  • Six Trimeresurus flavoviridis (Habu snake) venom gland phospholipase A2 (PLA2) isozyme genes were found to consist of four exons and three introns and to encode proteins of 138 amino acid residues, including the signal sequence of 16 amino acid residues [6].
  • The stereoselective synthesis makes use of the monolysocardiolipin 1-(3-sn-phosphatidyl)-3-[1-acyl-2-lyso-sn-glycero(3)phospho]-sn-glycerol, available from the stereospecific hydrolysis of cardiolipin by phospholipase A2 (phosphatide 2-acylhydrolase, EC of Trimeresurus flavoviridis [7].
  • The snake venom C-type lectin alboaggregin A (or 50-kd alboaggregin) from Trimeresurus albolabris was previously shown to be a platelet glycoprotein (GP) Ib agonist [8].
  • [Alignment; indels; intron analysis; length-variant heterozygotes; Trimeresurus.] [9].
  • The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity [10].

Chemical compound and disease context of Trimeresurus


Biological context of Trimeresurus


Anatomical context of Trimeresurus

  • Phospholipase A2 inhibitor (PLI), purified from the blood plasma of the Habu snake (Trimeresurus flavoviridis), was separated into two distinct subunits, PLI-A and PLI-B [19].
  • Using extracellular recording from IR-sensitive trigeminal ganglion (TG) neurons (primary neurons) and tectal (OT) neurons of the crotaline snake Trimeresurus flavoviridis, we examined the IR response to ethanol (EtOH) in vivo [20].
  • Capsaicin, the main pungent ingredient in hot peppers (genus Capsicum), caused degeneration of the infrared receptor terminals in infrared sensitive snakes, Trimeresurus flavoviridis, when it was applied perineurally to a branch of the trigeminal nerve [21].

Associations of Trimeresurus with chemical compounds


Gene context of Trimeresurus

  • The Habu snake has a venom-specific VEGF-like molecule, T. flavoviridis snake venom VEGF (TfsvVEGF), in addition to VEGF-A [27].
  • A novel plasminogen activator from Trimeresurus stejnegeri venom (TSV-PA) has been identified and purified to homogeneity [28].
  • Triflavin, a 7.5-kD cysteine-rich polypeptide purified from Trimeresurus favoviridis snake venom, belongs to a family of Arg-Gly-Asp-(RGD)-containing peptides, termed disintegrins [29].
  • As a step toward understanding the structure and function of phospholipases A2 (PLA2s), we isolated and sequenced several cDNAs encoding Trimeresurus flavoviridis venom PLA2 isozymes including two [Lys49]PLA2s called basic proteins I and II, [Thr37]PLA2, and PLX'-PLA2 [30].
  • Jerdostatin represents a novel RTS-containing short disintegrin cloned by reverse transcriptase-PCR from the venom gland mRNA of the Chinese Jerdons pit viper Trimeresurus jerdonii [23].

Analytical, diagnostic and therapeutic context of Trimeresurus


  1. Sequential expression of cellular fibronectin by platelets, macrophages, and mesangial cells in proliferative glomerulonephritis. Barnes, J.L., Hastings, R.R., De la Garza, M.A. Am. J. Pathol. (1994) [Pubmed]
  2. Origin of interstitial fibroblasts in an accelerated model of angiotensin II-induced renal fibrosis. Faulkner, J.L., Szcykalski, L.M., Springer, F., Barnes, J.L. Am. J. Pathol. (2005) [Pubmed]
  3. Trigramin, an RGD-containing peptide from snake venom, inhibits cell-substratum adhesion of human melanoma cells. Knudsen, K.A., Tuszynski, G.P., Huang, T.F., Niewiarowski, S. Exp. Cell Res. (1988) [Pubmed]
  4. Effect of dimercaptosuccinic acid on toxicity of Habu snake (Trimeresurus flavoviridis, Hallowell) venom. Kurihara, N. Jpn. J. Pharmacol. (1978) [Pubmed]
  5. Properties and cDNA cloning of an antihemorrhagic factor (HSF) purified from the serum of Trimeresurus flavoviridis. Deshimaru, M., Tanaka, C., Fujino, K., Aoki, N., Terada, S., Hattori, S., Ohno, M. Toxicon (2005) [Pubmed]
  6. Accelerated evolution of Trimeresurus flavoviridis venom gland phospholipase A2 isozymes. Nakashima, K., Ogawa, T., Oda, N., Hattori, M., Sakaki, Y., Kihara, H., Ohno, M. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  7. Cardiolipin: a stereospecifically spin-labeled analogue and its specific enzymic hydrolysis. Cable, M.B., Jacobus, J., Powell, G.L. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  8. Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib. Dörmann, D., Clemetson, J.M., Navdaev, A., Kehrel, B.E., Clemetson, K.J. Blood (2001) [Pubmed]
  9. Optimal intron analyses in the trimeresurus radiation of Asian pitvipers. Creer, S., Pook, C.E., Malhotra, A., Thorpe, R.S. Syst. Biol. (2006) [Pubmed]
  10. Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases. Zhu, Z., Liang, Z., Zhang, T., Zhu, Z., Xu, W., Teng, M., Niu, L. J. Biol. Chem. (2005) [Pubmed]
  11. Amino acid sequence of a thrombin like enzyme, elegaxobin II, from the venom of Trimeresurus elegans (Sakishima-Habu). Oyama, E., Takahashi, H. Toxicon (2004) [Pubmed]
  12. Edema factor from the venom of Trimeresurus elegans (Sakishimahabu). Nikai, T., Suzuki, Y., Komori, Y., Sugihara, H. Journal of natural toxins. (2000) [Pubmed]
  13. Focal mesangial proliferative glomerulonephritis in the rat caused by Habu venom: the effect of antiplatelet agents. Cattell, V., Mehotra, A. British journal of experimental pathology. (1980) [Pubmed]
  14. Assessing the phylogenetic utility of four mitochondrial genes and a nuclear intron in the asian pit viper genus, Trimeresurus: separate, simultaneous, and conditional data combination analyses. Creer, S., Malhotra, A., Thorpe, R.S. Mol. Biol. Evol. (2003) [Pubmed]
  15. Frangulin B, an antagonist of collagen-induced platelet aggregation and adhesion, isolated from Rhamnus formosana. Teng, C.M., Lin, C.H., Lin, C.N., Chung, M.I., Huang, T.F. Thromb. Haemost. (1993) [Pubmed]
  16. Amino acid sequence and molecular modelling of glycoprotein IIb-IIIa and fibronectin receptor iso-antagonists from Trimeresurus elegans venom. Scaloni, A., Di Martino, E., Miraglia, N., Pelagalli, A., Della Morte, R., Staiano, N., Pucci, P. Biochem. J. (1996) [Pubmed]
  17. Cloning and sequence analysis of cDNA for Trimeresurus flavoviridis phospholipase A2, and consequent revision of the amino acid sequence. Oda, N., Ogawa, T., Ohno, M., Sasaki, H., Sakaki, Y., Kihara, H. J. Biochem. (1990) [Pubmed]
  18. Snake venom proteinases as tools in hemostasis studies: structure-function relationship of a plasminogen activator purified from Trimeresurus stejnegeri venom. Wisner, A., Braud, S., Bon, C. Haemostasis (2001) [Pubmed]
  19. Amino acid sequences of the two subunits of a phospholipase A2 inhibitor from the blood plasma of Trimeresurus flavoviridis. Sequence homologies with pulmonary surfactant apoprotein and animal lectins. Inoue, S., Kogaki, H., Ikeda, K., Samejima, Y., Omori-Satoh, T. J. Biol. Chem. (1991) [Pubmed]
  20. Response of the infrared receptors of a crotaline snake to ethanol. Moon, C., Terashima, S. Neurosci. Lett. (2002) [Pubmed]
  21. Degeneration of infrared receptor terminals of snakes caused by capsaicin. Terashima, S., Ogawa, K. Brain Res. (2002) [Pubmed]
  22. Trimeresurus stejnegeri snake venom plasminogen activator. Site-directed mutagenesis and molecular modeling. Zhang, Y., Wisner, A., Maroun, R.C., Choumet, V., Xiong, Y., Bon, C. J. Biol. Chem. (1997) [Pubmed]
  23. cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha1beta1 integrin. Sanz, L., Chen, R.Q., Pérez, A., Hilario, R., Juárez, P., Marcinkiewicz, C., Monleón, D., Celda, B., Xiong, Y.L., Pérez-Payá, E., Calvete, J.J. J. Biol. Chem. (2005) [Pubmed]
  24. Crystallization and preliminary X-ray study of blood coagulation factor IX/factor X-binding protein with anticoagulant activity from Habu snake venom. Mizuno, H., Atoda, H., Morita, T. J. Mol. Biol. (1991) [Pubmed]
  25. Molecular cloning and characterization of a neurotoxic phospholipase A2 from the venom of Taiwan habu (Trimeresurus mucrosquamatus). Tsai, I.H., Lu, P.J., Wang, Y.M., Ho, C.L., Liaw, L.L. Biochem. J. (1995) [Pubmed]
  26. Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri. Xu, Q., Wu, X.F., Xia, Q.C., Wang, K.Y. Biochem. J. (1999) [Pubmed]
  27. A novel snake venom vascular endothelial growth factor (VEGF) predominantly induces vascular permeability through preferential signaling via VEGF receptor-1. Takahashi, H., Hattori, S., Iwamatsu, A., Takizawa, H., Shibuya, M. J. Biol. Chem. (2004) [Pubmed]
  28. A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning. Zhang, Y., Wisner, A., Xiong, Y., Bon, C. J. Biol. Chem. (1995) [Pubmed]
  29. Triflavin inhibits platelet-induced vasoconstriction in de-endothelialized aorta. Sheu, J.R., Yen, M.H., Hung, W.C., Lee, Y.M., Su, C.H., Huang, T.F. Arterioscler. Thromb. Vasc. Biol. (1997) [Pubmed]
  30. Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes. Ogawa, T., Oda, N., Nakashima, K., Sasaki, H., Hattori, M., Sakaki, Y., Kihara, H., Ohno, M. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  31. Purification and some chemical properties of thrombin-like enzyme from Trimeresurus flavoviridis venom. Kosugi, T., Ariga, Y., Nakamura, M., Kinjo, K. Thromb. Haemost. (1986) [Pubmed]
  32. Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms. Tu, X., Wang, J., Guo, M., Zheng, D., Teng, M., Niu, L., Liu, Q., Huang, Q., Hao, Q. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  33. Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Atoda, H., Yoshida, N., Ishikawa, M., Morita, T. Eur. J. Biochem. (1994) [Pubmed]
  34. Isolation and fundamental properties of a phospholipase A2 inhibitor from the blood plasma of Trimeresurus flavoviridis. Kogaki, H., Inoue, S., Ikeda, K., Samejima, Y., Omori-Satoh, T., Hamaguchi, K. J. Biochem. (1989) [Pubmed]
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