Structural and functional characterization of a P-III metalloproteinase, leucurolysin-B, from Bothrops leucurus venom

Archives of Biochemistry and Biophysics

Volumn 468, Issue 2, 2007, Pages 193-204

  Sanchez, Eladio F ^a,d   Gabriel, Lucilene M ^a   Gontijo, Sileia ^a   Gremski, Luiza H ^b,e   Veiga, Silvio S ^b   Evangelista, Karla S ^c   Eble, Johannes A ^c   Richardson, Michael ^a  

^a Ezequiel Dias Foundation   (Brazil)

^b FEDERAL UNIVERSITY OF PARANÁ   (Brazil)

^c UNIVERSITY OF MÜNSTER   (Germany)

^d Hospital Santa Casa de Belo Horizonte   (Brazil)

^e FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Bothrops leucurus; Disintegrin like protein; Leucurolysin B; Metalloproteinase; Snake venom

Indexed keywords

ALANINE; ARGINYLGLYCYLASPARTIC ACID; CALCIUM ION; CHELATING AGENT; COPPER; CYSTEINE; DISINTEGRIN; FIBRIN; FIBRINOGEN; FIBRONECTIN; INSULIN; LEUCINE; LEUCUROLYSIN B; MAGNESIUM ION; METALLOPROTEINASE; METALLOPROTEINASE P III; UNCLASSIFIED DRUG; VENOM; VITRONECTIN; ZINC ION;

ALKYLATION; AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; BLEEDING; BOTHROPS LEUCURUS; CARBOXY TERMINAL SEQUENCE; CATION TRANSPORT; ENZYME ANALYSIS; EXTRACELLULAR MATRIX; GEL FILTRATION; HYDROLYSIS; ION EXCHANGE; LIQUID CHROMATOGRAPHY; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN MOTIF; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RABBIT; REDUCTION KINETICS; SNAKE;

AMINO ACID SEQUENCE; ANIMALS; BOTHROPS; CROTALID VENOMS; ENZYME ACTIVATION; ENZYME STABILITY; METALLOPROTEASES; MOLECULAR SEQUENCE DATA;

BOTHROPS JARARACA; BOTHROPS LEUCURUS; ORYCTOLAGUS CUNICULUS;

EID: 36148929821     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2007.10.002     Document Type: Article

References (57)

1. Markland F.S. Toxicon 36 (1998) 1749-1800
2. Matsui T., Fujimura Y., and Titani K. Biochim. Biophys. Acta 1477 (2000) 146-156
3. Stocker W., Grams F., Baumann U., Reinemer P., Gomis-Rüth F.-X., McKay D., and Bode W. Protein Sci. 4 (1995) 823-840
4. Andrews R.K., Gardiner E.E., Asazuma N., Berlanga O., Tulasne D., Nieswandt B., Smith A.I., Berndt M.C., and Watson S.P. J. Biol. Chem. 276 (2001) 28092-28097
5. Kishimoto M., and Takahashi T. Toxicon 40 (2002) 1369-1375
6. You W.-K., Jang Y.-J., Chung K.-H., Jeon O.-H., and Kim D.S. Biochem. Biophys. Res. Commun. 339 (2006) 964-970
7. Wang W.-J., Shih C.-O., and Huang T.-F. Biochimie 87 (2005) 1065-1077
8. Bjarnason J.B., and Fox J.W. Meth. Enzymol. 248 (1995) 345-368
9. Duffy M.J., Lynn D.J., Lloyd AT., and O'Shea C.M. Thromb. Haemost. 89 (2003) 622-631
10. Wolfberg T.G., Strainght P.D., Gerena R.L., Huovila A.P., Primakoff P., Myles D.G., and White J.M. Dev. Biol. 169 (1995) 378-383
11. Blobel C.P., Wolfdberg T.G., Turck C.W., Myles D.G., Primakoff P., and White J.M. Nature 356 (1992) 248-252
12. Baramova E.N., Shannon J.D., Bjarnason J.B., and Fox J.W. Arch. Biochem. Biophys. 275 (1989) 63-71
13. Kamiguti A.S., Slupsky J.R., Zuzel M., and Hay C.R. Thromb. Haemostasis 72 (1994) 244-249
14. Jia L.G., Wang X.M., Shannon J.D., Bjarnason J.B., and Fox J.W. J. Biol. Chem. 272 (1997) 13094-13102
15. Kamiguti A.S., Hay C.R., Theakston R.D., and Zuzel M. Toxicon 34 (1996) 627-642
16. Gutierrez J.M., and Rucavado A. Biochimie 82 (2000) 841-850
17. Ministério da Saúde do Brasil-Fundação Nacional de Saúde, Manual de diagnóstico e tratamento de acidentes por animais peçonhentos, DF, Brasilia, 1999.
18. Da Silva L.R.M., and Nunes B.T. Toxicon 31 (1993) 143-144
19. Camey K.U., Velarde D.T., and Sanchez E.F. Toxicon 40 (2002) 501-509
20. Bello C.A., Hermogenes A.L., Magalhaes A., Veiga S.S., Gremski L.H., Richardson M., and Sanchez E.F. Biochimie 88 (2006) 189-200
21. Magalhaes A., Magalhaes H.B., Richardson M., Gontijo S., Ferreira R., Almeida A.P., and Sanchez E.F. Comp. Biochem. Physiol. Part A Mol. Integrative Physiol. 146 (2007) 565-575
22. Higuchi D.A., Chagas J.R., Bincoleto C.M.V., Magalhaes A., Richardson M., Sanchez E.F., Pesquero J.B., and Pesquero J.L. Biochimie 89 (2007) 319-328
23. Engvall E., and Ruoslathi E. Int. J. Cancer 20 (1977) 1-5
24. Yatohgo T., Izumi M., Kashiwagi H., and Hayashi M. Cell Struct. Funct. 13 (1988) 281-292
25. Timpl R., Rohde H., Robey P.G., Rennard S.I., Foidartc J.M., and Martin G.R. J. Biol. Chem. 254 (1979) 9933-9937
26. Paulsson M., Aumaillay M., Deutzmann R., Timpl R., and Beck K. Eur. J. Biochem. 166 (1987) 11-19
27. Guis M.B., Slootweg R., and Tonino J.G.M. Arch. Oral Biol. 18 (1973) 253-263
28. Wilson K.J., and Yuan P.M. In: Findlay J.B.C., and Geisow M.J. (Eds). Protein Sequencing a Practical Approach (1989), I.R.L. Press, Oxford, New York, Tokyo 3-41
29. Laemmli U.K. Nature 227 (1970) 680-685
30. Sanchez E.F., Cordeiro M.N., Oliveira E.B., Juliano E.B.L., Prado E.S., and Diniz C.R. Toxicon 33 (1995) 1061-1070
31. Sanchez E.F., Santos C.I., Magalhaes A., Diniz C.R., Figueiredo S., and Richardson M. Arch. Biochem. Biophys. 378 (2000) 131-141
32. Estevao-Costa M.I., Diniz C.R., Magalhaes A., Markland F.S., and Sanchez E.F. Thromb. Res. 99 (2000) 363-376
33. Eble A.J., Beermann B., Hinz H.-J., and Schmidt-Hederich A. J. Biol. Chem. 276 (2001) 12274-12284
34. Zigrino P., Kamiguti A.S., Eble J., Drescher C., and Nischt R. J. Biol. Chem. 277 (2002) 40526-40535
35. Eble A.J., Kassner A., Niland S., Mörgelin M., Grifka J., and Grässel S. J. Biol. Chem. 281 (2006) 25745-25756
36. Takeya H., Oda K., Miyata K., Omori-Satoh T., and Iwanaga S. J. Biol. Chem. 265 (1990) 16068-16073
37. Cerretti D.P., DuBose R.F., Black R.A., and Nelson N. Biochem. Biophys. Res. Commun. 263 (1999) 810-815
38. Fox J.W., and Serrano S.M.T. Toxicon 45 (2005) 969-985
39. Civello D.J., Duong H.L., and Geren C.R. Biochemistry 22 (1983) 749-755
40. Nikai T., Mori N., Kishida M., Kato Y., Takenata Ch., Murakami T., Shigezane S., and Sugihara H. Biochim. Biophys. Acta 838 (1985) 122-131
41. Swenson S., and Markland F.S. Toxicon 45 (2005) 1021-1039
42. Chain D., Korc-Grodzicki B., Kreisman T., and Shaltiel S. Biochem. J. 274 (1991) 387-394
43. Gremski L.H., Chaim O.M., Paludo K.S., Sade Y.B., Otuki M.F., Richardson M., Sanchez E.F., and Veiga S.S. Toxicon 50 (2007) 120-134
44. Sanchez E.F., and Swenson S. Curr. Pharm. Anal. 3 (2007) 147-157
45. Kini R.M., and Evans H.J. Toxicon 30 (1992) 265-293
46. Peichoto M.E., Teibler P., Mackessey S.P., Leiva L., Acosta O., Gonçalves L.R.C., Tanaka A.M., and Santoro M.L. Biochim. Biophys. Acta 1770 (2007) 810-819
47. Lovejoy B., Hassell A.M., Luther M.A., Weigl D., and Jordan S.R. Biochemistry 33 (1994) 8207-8217
48. Ala-aho R., and Kähäri V.-M. Biochimie 87 (2005) 273-286
49. Kamiguti A.S., Slupski J.R., Zuzel M., and Hay C.R.M. Thromb. Haemost. 72 (1994) 244-249
50. Jeon O.-H., and Kim D.-S. Eur. J. Biochem. 263 (1999) 526-533
51. Kamiguti A.S., Gallagher P., Marcionkiewitz C., Theakston R.D.G., Zuzel M., and Fox J.W. FEBS Lett. 549 (2003) 129-134
52. Nymalm Y., Puranen J.S., Nyholm T.K., Kapyla J., Kidron H., Pentikainen O.T., Airenne T.T., Heino J., Slotte J.P., Johonson M.S., and Salminem T.A. J. Biol. Chem. 103 (2004) 2150-5156
53. Liu C.Z., and Huang T.F. Arch. Biochem. Biophys. 337 (1997) 291-299
54. Wang W.-E. Biochimie 89 (2007) 105-115
55. Gomis-Ruth F.-X., Kress L.F., Kellermann J., Mayr I., Huber R., and Bode W. J. Mol. Biol. 239 (1994) 513-544
56. Rodriguez V.M., Soares A.M., Guerra-Sa R., Rodrigues V., Fontes M.R.M., and Giglio J.R. Arch. Biochem. Biophys. 381 (2000) 213-224
57. Kern A., Eble J., Golbik R., and Kühn K. Eur. J. Biochem. 225 (1993) 151-159