Resolution of isoforms of mutalysin II, the metalloproteinase from bushmaster snake venom

Toxicon

Volumn 41, Issue 8, 2003, Pages 1021-1031

  Sanchez, Eladio F ^a   Souza, Christiane T ^a   Bello, Cynthia A ^a   Richardson, Michael ^a   Oliveira, Eduardo B ^b   Magalhaes, Arinos ^a  

^a FUNDAÇÃO EZEQUIEL DIAS   (Brazil)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Bushmaster snake; Isoforms; Metalloproteinases; Mutalysin; Snake venom

Indexed keywords

DODECYL SULFATE SODIUM; EDETIC ACID; FIBRIN; FIBRINOGEN; HYPERIMMUNE GLOBULIN; IMMUNOGLOBULIN G; ISOPROTEIN; METALLOPROTEINASE; MUTALYSIN IIA; MUTALYSIN IIB; PROTEIN ANTIBODY; PROTEINASE; SEPHADEX; SEPHAROSE; SNAKE VENOM; UNCLASSIFIED DRUG; ZINC; CASEIN; GLYCOPROTEIN; HEMORRHAGIC FACTOR LHFII; ISOENZYME; MUT IIA PROTEIN, LACHESIS MUTA MUTA; MUT IIB PROTEIN, LACHESIS MUTA MUTA; N,N DIMETHYLCASEIN; N,N-DIMETHYLCASEIN; PEPTIDE HYDROLASE;

ANALYTIC METHOD; ANIMAL EXPERIMENT; ARTICLE; CHROMATOGRAPHY; CONTROLLED STUDY; CROSS REACTION; ENZYME GLYCOSYLATION; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME STRUCTURE; FIBRINOLYSIS; HYDROLYSIS; IC 50; IMMUNODIFFUSION; IMMUNOHISTOCHEMISTRY; MICROSCOPE; MOLECULAR WEIGHT; NONHUMAN; PEPTIDE MAPPING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN ISOLATION; PROTEIN STABILITY; PROTEIN STRUCTURE; RABBIT; WESTERN BLOTTING; ANIMAL; CHEMISTRY; DRUG EFFECT; ENZYMOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOLATION AND PURIFICATION; METABOLISM; SNAKE; SPECTROSCOPY;

LACHESIS MUTA; LACHESIS MUTA MUTA; ORYCTOLAGUS CUNICULUS; SERPENTES;

ANIMALS; CASEINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; FIBRIN; FIBRINOGEN; GLYCOPROTEINS; IMMUNOHISTOCHEMISTRY; ISOENZYMES; METALLOENDOPEPTIDASES; PEPTIDE HYDROLASES; PEPTIDE MAPPING; RABBITS; SNAKE VENOMS; SPECTRUM ANALYSIS; VIPERIDAE; ZINC;

EID: 0142087816     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(03)00076-X     Document Type: Article

References (33)

1. Barrett A.J., Rawlings N.D. MEROPS: the peptidase database. Nucl. Acids Res. 28:2000;323-325.
2. Bjarnason J.B., Fox J.W. Proteolytic specificity and cobalt exchange of hemorrhagic toxin e, a zinc protease isolated from the venom of the western diamondback rattlesnake. Biochemistry. 22:1983;3770-3778.
3. Bjarnason J.B., Fox J.W. Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom. Biochim. Biophys. Acta. 911:1987;356-363.
4. Bjarnason J.B., Fox J.W. Hemorrhagic metalloproteases from snake venoms. Pharmac.Theor. 62:1994;325-372.
5. Brattstrom B.J. Evolution of the pit vipers. Trans. San Diego Soc. Nat. His. 13:1964;185-268.
6. Camey K.U., Velarde D.T., Sanchez E.F. Pharmacological characterization and neutralization of the venoms used in the production of Bothropic antivenom in Brazil. Toxicon. 40:2002;501-509.
7. Chen H.M., Guan A.L., Markland F.S. Immunological properties of the fibrinolytic enzyme (fibrolase) from southern copperhead (Agkistrodon contortrix contortrix) venom and its purification by immunoaffinity chromatography. Toxicon. 29:1991;683-694.
8. Estevao-Costa M.I., Diniz C.R., Magalhaes A., Markland F.S., Sanchez E.F. Action of metalloproteinases mutalysin I and II on several components of the hemostatic and fibrinolytic systems. Thromb. Res. 99:2000;363-376.
9. Ey P.L., Powse S.J., Jenking C.R. Isolation of pure IgGa, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-Sepharose. Immunochemistry. 15:1978;429-436.
10. Gomis-Ruth F.-X., Kres L.F., Bode W. First structure of a snake venom metalloproteinase: a prototipe for matrix metalloproteinase/collagenase. EMBO J. 12:1993;4151-4157.
11. Kini R.M., Evans H.J. Structural domains in venom proteins: evidence that metalloproteinases and non-enzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived from a common precursor. Toxicon. 30:1992;265-293.
12. Kondo H., Kondo S., Ikesawa H., Murata R., Oshaka A. Studies on the quantitative method for determination of hemorrhagic activity of habu snake venom. Jpn. J. Med. Sci. Biol. 13:1960;43-51.
13. Kunitz M. Crystalline soybean trypsin inhibitor II, general properties. J. Gen. Physiol. 30:1946;291-310.
14. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
15. Lin Y., Means G.E., Feeney R.E. The action of proteolytic enzymes on N,N-dimethylproteins. J. Biol. Chem. 244:1969;789-793.
16. Loayza S.L., Thrika M., Markland F.S., Riquelme P., Kuo J. Resolution of isoforms of natural and recombinant fibrolase, the fibrinolytic enzyme from Agkistrodon contortrix contortrix snake venom, and comparison of their EDTA sensitives. J. Chromatogr. B662:1994;227-243.
17. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
18. Markland F.S. Snake venoms and the hemostatic system. Toxicon. 36:1998;149-180.
19. Markland F.S., Friederichs G.S., Pewitt S.R., Lucchesi B.R. Thrombolytic effects of recombinant fibrolase or APSAC in a canine model of carotid artery thrombosis. Circulation. 90:1994;2448-2456.
20. Miyata T., Takeya H., Ozeki Y., Arakawa M., Tokunga F., Iwanaga S., Omori-Satoh T. Primary structure of hemorrhagic toxin, HR2a, isolated from the venom of Trimeresurus flavoviridis. J. Biochem. 105:1989;847-853.
21. Sanchez E.F. Mutalysins. Barrett A.J., Rawlings N.D., Woessner J.F. Handbook of Proteolytic Enzymes. 2003;Academic Press, London. in press.
22. Sanchez E.F., Magalhaes A., Diniz C.R. Purification of a hemorrhagic factor (LHF-I) from the venom of the bushmaster snake (Lachesis muta muta). Toxicon. 25:1987;611-619.
23. Sanchez E.F., Magalhaes A., Mandelbaum F.R., Diniz C.R. Purification and characterization of the hemorrhagic factor II from the venom of the bushmaster snake (Lachesis muta muta). Biochim. Biophys. Acta. 1074:1991;347-356.
24. Sanchez E.F., Diniz C.R., Richardson M. The complete amino acid sequence of the hemorrhagic factor LHF II, a metalloproteinase isolated from the venom of the bushmaster snake (Lachesis muta muta). FEBS Lett. 282:1991;178-182.
25. Sanchez E.F., Cordeiro M.N., Oliveira E.B., Juliano L., Prado E.S., Diniz C.R. Proteolytic specificity of two hemorrhagic factors, LHF-I and LHF-II, isolated from the venom of the bushmaster snake (Lachesis muta muta). Toxicon. 33:1995;1061-1070.
26. 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. 264:1989;11575-11583.
27. Souza C.T., Moura M.B., Magalhaes A., Heneine L.G.D., Olortegui C.C., Diniz C.R., Sanchez E.F. Inhibition of mutalysin II, a metalloproteinase from bushmaster snake venom by human α2-macroglobulin and rabbit immunoglobulin. Comp. Biochem. Physiol. 130B:2001;155-168.
28. Stocker K.F. Snake venom proteins affecting haemostasis and fibrinolysis. Stocker K.F. Medical Use of Snake Venom Proteins. 1990;97-160 CRC Press Inc, Boca Raton.
29. Stocker W., Grams F., Baumann U., Reinemer P., Gomis-Ruth F.-X., McKay D.B., Bode W. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins and matrixins (collagenases) define a superfamily of zinc-endopeptidases. Protein Sci. 4:1995;823-840.
30. 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 habu snake, Trimeresurus flavoviridis. J. Biochem. 106:1989;151-157.
31. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA. 76:1979;4350-4354.
32. Willis T.W., Tu A.T., Miller C.W. Thrombolysis with snake venom protease in a rat model of venous thrombosis. Thromb. Res. 53:1989;19-29.
33. Zhang D., Botos I., Gomis-Ruth 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. 91:1994;8447-8451.