All Title Author
Keywords Abstract

Publish in OALib Journal
ISSN: 2333-9721
APC: Only $99
Paper Submission

ViewsDownloads

Relative Articles

Blood biochemical profile of the South American rattlesnake (Crotalus durissus terrificus) in captivity

Acute hepatotoxicity of Crotalus durissus terrificus (South American rattlesnake) venom in rats

The venom-gland transcriptome of the eastern diamondback rattlesnake (Crotalus adamanteus)

Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)

On the unsual hemorrhagic and necrotic activities caused by the rattlesnake (Crotalus durissus cumanensis) in a Venezuelan patient

ISOLATION OF AN OPHIDIAN PARAMYXOVIRUS (OPMV) IN A CAPTIVE RATTLESNAKE (Crotalus durissus terrificus) FROM BOTUCATU, S？O PAULO STATE, BRAZIL

Shallow phylogeographic structure in the declining Mexican Lance-headed Rattlesnake, Crotalus polystictus (Serpentes: Viperidae)

The Evolutionary Implications of Hemipenial Morphology of Rattlesnake Crotalus durissus terrificus (Laurent, 1768) (Serpentes: Viperidae: Crotalinae)

On the unsual hemorrhagic and necrotic activities caused by the rattlesnake (Crotalus durissus cumanensis) in a Venezuelan patient

American rattlesnake (Crotalus durissus terrificus) bite accidents in dogs in Argentina

More...
Toxins  2011 

Isolation and Biochemical Characterization of Rubelase, a Non-Hemorrhagic Elastase from Crotalus ruber ruber (Red Rattlesnake) Venom

DOI: 10.3390/toxins3070900

Keywords: Crotalus ruber ruber toxin, elastase, amino acid sequence, cytotoxicity

Full-Text   Cite this paper   Add to My Lib

Abstract:

A novel non-hemorrhagic basic metalloprotease, rubelase, was isolated from the venom of Crotalus ruber ruber. Rubelase hydrolyzes succinyl-L-alanyl-L-alanyl-L-alanyl p-nitroanilide (STANA), a specific substrate for elastase, and the hydrolytic activity was inhibited by chelating agents. It also hydrolyzes collagen and fibrinogen. However, hemorrhagic activity was not observed. By ESI/Q-TOF and MALDI/TOF mass spectrometry combined with Edman sequencing procedure, the molecular mass of rubelase was determined to be 23,266 Da. Although its primary structure was similar to rubelysin (HT-2), a hemorrhagic metalloprotease isolated from the same snake venom, the circumstances surrounding putative zinc binding domain HEXXHXXGXXH were found to be different when the three-dimensional computer models of both metalloproteases were compared. The cytotoxic effects of rubelase and rubelysin on cultured endothelial and smooth muscle cells were also different, indicating that the substitution of several amino acid residues causes the changes of active-site conformation and cell preference.

 References

[1]  Tu, A.T. Venoms. Chemistry and Molecular Biology; John Wiley & Sons: New York, NY, USA, 1977; pp. 372–399.
[2]  Tu, A.T. Rattlesnake Venom: Their Actions and Treatment; Marcel Dekker, Inc.: New York, NY, USA, 1982.
[3]  Omori-Satoh, T.; Sadahiro, S. Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts. Biochim. Biophys. Acta 1979, 580, 392–404. 518906
[4]  Sugihara, H.; Moriura, M.; Nikai, T. Purification and properties of a lethal, hemorrhagic protein “Mucrotoxin A” from the venom of the Chinese habu snake (Trimeresurus mucrosquamatus). Toxicon 1983, 21, 247–255, doi:10.1016/0041-0101(83)90009-0. 6857709
[5]  Nikai, T.; Sugihara, H.; Tanaka, T. Enzymochemical studies on snake venoms. II. Purification of lethal protein Ac1-Proteinase in the venom of Agkistrodon acutus. 1977, 97, 507–514.
[6]  Bjarnason, J.B.; Tu, A.T. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venoms: Isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry 1978, 17, 3395–3404, doi:10.1021/bi00609a033. 210790
[7]  Nikai, T.; Mori, N.; Kishida, M.; Sugihara, H.; Tu, A.T. Isolation and biochemical characterization of hemorrhagic toxin f from the venom of Crotalus atrox (western diamondback rattlesnake). Arch. Biochem. Biophys. 1984, 231, 309–319, doi:10.1016/0003-9861(84)90393-X. 6375570
[8]  Mori, N.; Nikai, T.; Sugihara, H.; Tum, A.T. Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom. Arch. Biochem. Biophys. 1987, 253, 108–121, doi:10.1016/0003-9861(87)90643-6. 2949699
[9]  Imai, K.; Nikai, T.; Sugihara, H.; Ownby, C.L. Hemorrhagic toxin from the venom of Agkistrodon bilineatus (common cantil). Int. J. Biochem. 1989, 21, 667–673, doi:10.1016/0020-711X(89)90388-1. 2676645
[10]  Miyata, T.; Takeya, H.; Ozeki, Y.; Arakawa, M.; Tokunaga, F.; Iwanaga, S.; Omori-Satoh, T. Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis. J. Biochem. 1989, 105, 847–853. 2753880
[11]  Shannon, J.D.; Baramova, E.N.; Bjarnason, J.B.; Fox, J.W. Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin. J. Biol. Chem. 1989, 264, 11575–11583. 2745407
[12]  Takeya, H.; Oda, K.; Miyata, T.; Omori-Satoh, T.; Iwanaga, S. The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis. J. Biol. Chem. 1990, 265, 16068–16073. 2398046
[13]  Takeya, H.; Onikura, A.; Nikai, T.; Sugihara, H.; Iwanaga, S. Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber. J. Biochem. 1990, 108, 711–719. 2081731
[14]  Takeya, H.; Nishida, S.; Nishino, N.; Makinose, Y.; Omori-Sato, T.; Nikai, T.; Sugihara, H.; Iwanaga, S. Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes. J. Biochem. 1993, 113, 473–483. 8514736
[15]  Hite, L.A.; Jia, L.G.; Bjarnason, J.B.; Fox, J.W. cDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys. 1994, 308, 182–191, doi:10.1006/abbi.1994.1026. 8311451
[16]  Nikai, T.; Kato, C.; Komori, Y.; Nodani, H.; Homma, M.; Sugihara, H. Primary structure of Ac1-Proteinase from the venom of Deinagkistrodon acutus (hundred-pace snake) from Taiwan. Biol. Pharm. Bull. 1995, 18, 631–633, doi:10.1248/bpb.18.631. 7655443
[17]  Nikai, T.; Taniguchi, K.; Komori, Y.; Masuda, K.; Fox, J.W.; Sugihara, H. Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch. Biochem. Biophys. 2000, 378, 6–15, doi:10.1006/abbi.2000.1795. 10871038
[18]  Watanabe, L.; Shannon, J.D.; Valente, R.H.; Rucavado, A.; Alape-Giron, A.; Kamiguti, A.S.; Theakston, R.D.; Fox, J.W.; Gutierrez, J.M.; Arni, R.K. Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities. Protein Sci. 2003, 12, 2273–2281. 14500885
[19]  Gong, W.; Zhu, X.; Liu, S.; Teng, M.; Niu, L. Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus. J. Mol. Biol. 1998, 283, 657–668, doi:10.1006/jmbi.1998.2110. 9784374
[20]  Gomis-Ruth, F.X.; Kress, L.F.; Kellermann, J.; Mayer, L.; Lee, X.; Huber, R.; Bode, W. Refined 2.0 ？ X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin. J. Mol. Biol. 1994, 239, 513–544, doi:10.1006/jmbi.1994.1392. 8006965
[21]  Huang, K.F.; Chiou, S.H.; Ko, T.P.; Yuann, J.M.; Wang, A.H. The 1.35 ？ structure of cadmium-substituted TM-3, a snake-venom metalloproteinase from Taiwan habu: Elucidation of a TNFa-converting enzyme-like active-site structure with a distorted octahedral geometry of cadmium. Acta Crystallogr. Sect. D: Biol. Crystallogr. 2002, 58, 1118–1128, doi:10.1107/S090744490200656X.
[22]  Kumasaka, T.; Yamamoto, M.; Moriyama, H.; Tanaka, N.; Sato, M.; Katsube, Y.; Yamakawa, Y.; Omori-Satoh, T.; Iwanaga, S.; Ueki, T. Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis. J. Biochem. 1996, 119, 49–57. 8907175
[23]  Zhang, D.; Botos, I.; Gomis-Rüth, F.X.; Doll, R.; Blood, C.; Njoroge, F.G.; Fox, J.W.; Bode, W.; Meyer, E.F. Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d). Proc. Natl. Acad. Sci. USA 1994, 91, 8447–8451, doi:10.1073/pnas.91.18.8447. 8078901
[24]  Fox, J.W.; Serrano, S.M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45, 969–985, doi:10.1016/j.toxicon.2005.02.012. 15922769
[25]  Fox, J.W.; Serrano, S.M. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 2008, 275, 3016–3030, doi:10.1111/j.1742-4658.2008.06466.x. 18479462
[26]  Mackessy, S.P. Fractionation of red diamond rattlesnake (Crotalus ruber ruber) venom: Protease, phospho- diesterase, L-amino acid oxidase activities and effects of metal ions and inhibitors on protease activity. Toxicon 1985, 23, 337–340, doi:10.1016/0041-0101(85)90157-6. 2992122
[27]  Hasegawa, Y.; Nikai, T.; Okumura, Y.; Ogawa, K.; Sugihara, H. Characterization of elastolytic proteinase from Aspergillus flavus: Comparison of the elastolytic proteinase from Aspergillus fumigatus. Jpn. J. Med. Mycol. 1997, 38, 53–59, doi:10.3314/jjmm.38.53.
[28]  Murata, Y.; Satake, M.; Suzuki, T. Studies on snake venom: XII. Distribution of proteinase activities among Japanese and Formosan snake venoms. J. Biochem. 1963, 53, 431–437.
[29]  Ouyang, C.; Teng, C.M. Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom. Biochim. Biophys. Acta 1976, 420, 298–308. 1252459
[30]  Roberts, P.S. Measurement of the rate of plasmin action on synthetic substrates. J. Biol. Chem. 1958, 232, 285–291. 13549417
[31]  Rinderknecht, H.; Geokas, M.C.; Silverman, P.; Haverback, B.J. A new ultrasensitive method for the determination of proteolytic activity. Clin. Chim. Acta 1968, 21, 197–203, doi:10.1016/0009-8981(68)90127-7. 4299134
[32]  Charney, J.; Tomarelli, R.M. A colorimetric method for the determination of the proteolytic activity of duodenal juice. J. Biol. Chem. 1947, 171, 501–505. 20272088
[33]  Moore, G.L. Use of azo-dye-bound collagen to measure reaction velocities of proteolytic enzymes. Anal. Biochem. 1969, 23, 122–127.
[34]  Tanzer, M.L.; Gilvarg, C. Creatine and creatine kinase measurement. J. Biol. Chem. 1959, 234, 3201–3204. 13836864
[35]  Ishiyama, M.; Shiga, M.; Sasamoto, K.; Mizogucgi, M.; He, P. A new sulfonated tetrazolium salt that produces a highly water-soluble formazan dye. Chem. Pharm. Bull. 1993, 41, 1118–1122, doi:10.1248/cpb.41.1118.
[36]  Kurecki, T.; Laskowski, M., Sr.; Kress, L.F. Purification and some properties of two proteinases from Crotalus adamanteus venom that inactivate human a1-proteinase inhibitor. J. Biol. Chem. 1978, 253, 8340–8345. 309470
[37]  Nikai, T.; Kato, C.; Komori, Y.; Nodani, H.; Homma, M.; Sugihara, H. Primary structure of Ac1-proteinase from the venom of Deinagkistrodon acutus (hundred-pace snake) from Taiwan. Biol. Pharm. Bull. 1995, 18, 631–633, doi:10.1248/bpb.18.631. 7655443
[38]  Takeya, H.; Arakawa, M.; Miyata, T.; Iwanaga, S.; Omori-Satoh, T. Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis. J. Biochem. 1989, 106, 151–157. 2777746

Full-Text

comments powered by Disqus