Isolation and characterization of cotiaractivase, a novel low molecular weight prothrombin activator from the venom of Bothrops cotiara

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 5, 2006, Pages 863-871

  Senis, Yotis A ^a   Kim, Paul Y ^b   Fuller, Gemma L J ^a   García, Ángel ^c   Prabhakar, Sripadi ^c   Wilkinson, Mark C ^d   Brittan, Helen ^e   Zitzmann, Nicole ^c   Wait, Robin ^f   Warrell, David A ^e,g   Watson, Steve P ^a   Kamiguti, Aura S ^d,e   Theakston, R David G ^e   Nesheim, Michael E ^b   Laing, Gavin D ^e  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b QUEEN S UNIVERSITY   (Canada)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF LIVERPOOL   (United Kingdom)

^e LIVERPOOL SCHOOL OF TROPICAL MEDICINE   (United Kingdom)

^f UNIVERSITY OF OXFORD   (United Kingdom)

^g JOHN RADCLIFFE HOSPITAL   (United Kingdom)

Author keywords

Bothrops cotiara; Cotiaractivase; Prothrombin activator; Snake venom toxin

Indexed keywords

ARGININE; BENZENE DERIVATIVE; BLOOD CLOTTING FACTOR 10A; CALCIUM; CHELATING AGENT; CHROMOGENIC SUBSTRATE; COTIARACTIVASE; CYSTEINE; DEXTRO PHENYLALANYLPIPECOLYLARGININE 4 NITROANILIDE; DISINTEGRIN; EDETIC ACID; ENZYME; METALLOPROTEINASE; PEPTIDE; POLYPEPTIDE; PROTHROMBIN; SERINE PROTEINASE INHIBITOR; THREONINE; THROMBIN; UNCLASSIFIED DRUG; VIPER VENOM;

AMINO TERMINAL SEQUENCE; ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; ASSAY; BINDING AFFINITY; BRAZIL; CHEMICAL INTERACTION; COLUMN CHROMATOGRAPHY; COMPARATIVE STUDY; COMPETITIVE INHIBITION; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; HUMAN; HYDROPHOBICITY; MASS SPECTROMETER; MEASUREMENT; MOLECULAR WEIGHT; NORMAL HUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE; PURIFICATION; SEPARATION TECHNIQUE; SNAKE; TANDEM MASS SPECTROMETRY;

AMINO ACID SEQUENCE; ANIMALS; BOTHROPS; CROTALID VENOMS; METALLOPROTEASES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTHROMBIN;

BOTHROPS COTIARA; BOTHROPS JARARACA; CROTALINAE; VIPERINAE;

EID: 33646530932     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.03.004     Document Type: Article

References (25)

1. Lewis R.L., and Gutmann L. Snake venoms and the neuromuscular junction. Semin. Neurol. 24 (2004) 175-179
2. Lu Q., Clemetson J.M., and Clemetson K.J. Snake venoms and hemostasis. J. Thromb. Haemost. 3 (2005) 1791-1799
3. Teixeira Cde F., Fernandes C.M., Zuliani J.P., and Zamuner S.F. Inflammatory effects of snake venom metalloproteinases. Mem. Inst. Oswaldo Cruz 100 Suppl. 1 (2005) 181-184
4. Wijeyewickrema L.C., Berndt M.C., and Andrews R.K. Snake venom probes of platelet adhesion receptors and their ligands. Toxicon 45 (2005) 1051-1061
5. Kalafatis M. Coagulation factor V: a plethora of anticoagulant molecules. Curr. Opin. Hematol. 12 (2005) 141-148
6. Walsh P.N. Platelet coagulation-protein interactions. Semin. Thromb. Hemost. 30 (2004) 461-471
7. Jenny N.S., and Mann K.G. In: Colman R.W., Hirsch J., Marder V.J., Clowes A.W., and George J.N. (Eds). Hemostasis and thrombosis: basic principles and clinical practice (2001), Lippincott Williams & Wilkins, Philadelphia 171-189
8. Nahas L., Kamiguti A.S., and Barros M.A. Thrombin-like and factor X-activator components of Bothrops snake venoms. Thromb. Haemost. 41 (1979) 314-328
9. Castro H.C., Fernandes M., and Zingali R.B. Identification of bothrojaracin-like proteins in snake venoms from Bothrops species and Lachesis muta. Toxicon 37 (1999) 1403-1416
10. Francischetti I.M., Castro H.C., Zingali R.B., Carlini C.R., and Guimaraes J.A. Bothrops sp. snake venoms: comparison of some biochemical and physicochemical properties and interference in platelet functions. Comp. Biochem. Physiol. C, Pharmacol. Toxicol. Endocrinol. 119 (1998) 21-29
11. Brufatto N., and Nesheim M.E. Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process. J. Biol. Chem. 278 (2003) 6755-6764
12. Senis Y.A., Atkinson B.T., Pearce A.C., Wonerow P., Auger J.M., Okkenhaug K., Pearce W., Vigorito E., Vanhaesebroeck B., Turner M., and Watson S.P. Role of the p110delta PI 3-kinase in integrin and ITAM receptor signalling in platelets. Platelets 16 (2005) 191-202
13. Krishnaswamy S., and Betz A. Exosites determine macromolecular substrate recognition by prothrombinase. Biochemistry 36 (1997) 12080-12086
14. Bajzar L., Fredenburgh J.C., and Nesheim M. The activated protein C-mediated enhancement of tissue-type plasminogen activator-induced fibrinolysis in a cell-free system. J. Biol. Chem. 265 (1990) 16948-16954
15. Licklider L.J., Thoreen C.C., Peng J., and Gygi S.P. Automation of nanoscale microcapillary liquid chromatography-tandem mass spectrometry with a vented column. Anal. Chem. 74 (2002) 3076-3083
16. Garcia A., Prabhakar S., Hughan S., Anderson T.W., Brock C.J., Pearce A.C., Dwek R.A., Watson S.P., Hebestreit H.F., and Zitzmann N. Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins. Blood 103 (2004) 2088-2095
17. Mann K.G., Elion J., Butkowski R.J., Downing M., and Nesheim M.E. Prothrombin. Methods Enzymol. 80 Pt C (1981) 286-302
18. Silva M.B., Schattner M., Ramos C.R., Junqueira-de-Azevedo I.L., Guarnieri M.C., Lazzari M.A., Sampaio C.A., Pozner R.G., Ventura J.S., Ho P.L., and Chudzinski-Tavassi A.M. A prothrombin activator from Bothrops erythromelas (jararaca-da-seca) snake venom: characterization and molecular cloning. Biochem. J. 369 (2003) 129-139
19. Paine M.J., Desmond H.P., Theakston R.D., and Crampton J.M. Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family. J. Biol. Chem. 267 (1992) 22869-22876
20. Zhou Q., Smith J.B., and Grossman M.H. Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen. Biochem. J. 307 Pt 2 (1995) 411-417
21. Nishida S., Fujita T., Kohno N., Atoda H., Morita T., Takeya H., Kido I., Paine M.J., Kawabata S., and Iwanaga S. cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom. Biochemistry 34 (1995) 1771-1778
22. Fox J.W., and Serrano S.M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 45 (2005) 969-985
23. Gutierrez J.M., and Rucavado A. Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 82 (2000) 841-850
24. Andrews R.K., Kamiguti A.S., Berlanga O., Leduc M., Theakston R.D., and Watson S.P. The use of snake venom toxins as tools to study platelet receptors for collagen and von Willebrand factor. Haemostasis 31 (2001) 155-172
25. Mann K.G., Brummel K., and Butenas S. What is all that thrombin for?. J. Thromb. Haemost. 1 (2003) 1504-1514