Purification of bovine cathepsin B: Proteomic characterization of the different forms and production of specific antibodies

Biochemistry and Cell Biology

Volumn 81, Issue 4, 2003, Pages 317-326

  Sentandreu, M A ^a   Aubry, L ^a   Ouali, A ^a  

^a CEMAGREF   (France)

Author keywords

Antibodies; Bovine kidney; Cathepsin B; Cathepsin B isoforms; MALDI TOF

Indexed keywords

AMMONIUM COMPOUNDS; ANTIBIOTICS; ELECTROPHORESIS; GELS; ION EXCHANGE; PURIFICATION; SIZE EXCLUSION CHROMATOGRAPHY;

MOLECULAR MASSES;

BIOCHEMISTRY;

CATHEPSIN B;

ANIMAL CELL; ANIMAL TISSUE; ANTIBODY PRODUCTION; ARTICLE; CATTLE; CONTROLLED STUDY; HYDROLYSIS; ION EXCHANGE CHROMATOGRAPHY; KIDNEY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEOMICS; SEPARATION TECHNIQUE;

ANIMALS; ANTIBODIES; CATHEPSIN B; CATTLE; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; KIDNEY; LYSOSOMES; PROTEIN ISOFORMS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0345258029     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o03-060     Document Type: Article

References (39)

1. Aronson, N.N., Jr., and Barrett, A.J. 1978. The specificity of cathepsin B. Hydrolysis of glucagon at the C-terminus by a peptidyldipeptidase mechanism. Biochem. J. 171: 759-765.
2. Barrett, A.J., and Kirschke, H. 1981. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80(Pt. C): 535-561.
3. Baudys, M., Meloun, B., Gan-Erdene, T., Fusek, M., Mares, M., Kostka, V., Pohl, J., and Blake, C.C. 1991. S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo-and endopeptidase activities among cathepsins B, H and L. Biomed. Biochim. Acta, 50: 569-577.
4. Benyamin, Y., Roustan, C., and Boyer, M. 1986. Anti-actin antibodies. Chemical modification allows the selective production of antibodies to the N-terminal region. J. Immunol. Methods, 86: 21-29.
5. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
6. Bradley, J.D., and Whitaker, J.N. 1986. Isolation and characterization of cathepsin B from bovine brain. Neurochem. Res. 11: 851-867.
7. Chan, S.J., San Segundo, B., McCormick, M.B., and Steiner, D.F. 1986. Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc. Natl. Acad. Sci. U.S.A. 83: 7721-7725.
8. Chapman, H.A., Riese, R.J., and Shi, G.P. 1997. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59: 63-88.
9. Choudhury, S.D., Lamsal, M., Agarwal, S.K., Sharma, R., and Khan, M.Y. 1997. On the tissue/species dependence of cathepsin B isozymes. Mol. Cell. Biochem. 177: 89-95.
10. Deval, C., Bechet, D., Obled, A., and Ferrara, M. 1990. Purification and properties of different isoforms of bovine cathepsin B. Biochem. Cell Biol. 68: 822-826.
11. Ishisaka, R., Utsumi, T., Yabuki, M., Kanno, T., Furuno, T., Inoue, M., and Utsumi, K. 1998. Activation of caspase-3-like protease by digitonin-treated lysosomes. FEBS Lett. 435: 233-236.
12. Kirschke, H., Barrett, A.J., and Rawlings, N.D. 1995. Proteinases 1: lysosomal cysteine proteinases. Protein Profile, 2: 1581-1643.
13. Kominami, E., Tsukahara, T., Bando, Y., and Katunuma, N. 1985. Distribution of cathepsins B and H in rat tissues and peripheral blood cells. J. Biochem. (Tokyo), 98: 87-93.
14. Kos, J., and Lah, T.T. 1998. Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review). Oncol. Rep. 5: 1349-1361.
15. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-685.
16. Lamsal, M., Agarwal, S.K., Choudhury, S.D., and Khan, M.Y. 1997. Purification and tissue/species dependence of the specificity of buffalo kidney cathepsin B. Indian J. Biochem Biophys. 34: 461-469.
17. Lardeux, B., Gouhot, B., and Forestier, M. 1983. Improved recovery of rat liver fractions enriched in lysosomes by specific alteration of the sedimentation properties of mitochondria. Anal. Biochem. 131: 160-165.
18. Maciewicz, R.A., and Etherington, D.J. 1988. A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Biochem. J. 256: 433-440.
19. Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262: 10 035-10 038.
20. Moin, K., Day, N.A., Sameni, M., Hasnain, S., Hirama, T., and Sloane, B.F. 1992. Human tumour cathepsin B. Comparison with normal liver cathepsin B. Biochem. J. 285(Pt. 2): 427-434.
21. Mordier, S., Bechet, D., Roux, M.-P., Obled, A., and Ferrara, M. 1993. Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism in the protein coding region. Biochim. Biophys. Acta, 1174: 305-311.
22. Mort, J.S. 1998. Cathepsin B. In Handbook of proteolytic enzymes. Edited by A.J. Barrett, N.D. Rawlings, and J.F. Woessner. Academic Press, London, U.K. pp. 609-617.
23. Musil, D., Zucic, D., Turk, D., Engh, R.A., Mayr, I., Huber, R., Popovic, T., Turk, V., Towatari, T., Katunuma, N., and Bode, W. 1991. The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 10: 2321-2330.
24. Pennacchio, L.A., Bouley, D.M., Higgins, K.M., Scott, M.P., Noebels, J.L., and Myers, R.M. 1998. Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 20: 251-258.
25. Pontremoli, S., Melloni, E., Salamino, F., Sparatore, B., Michetti, M., and Horecker, B.L. 1983. Endogenous inhibitors of lysosomal proteinases. Proc. Natl. Acad. Sci. U.S.A. 80: 1261-1264.
26. Popovic, T., Puizdar, V., Ritonja, A., and Brzin, J. 1996. Simultaneous isolation of human kidney cathepsins B, H, L and C and their characterisation. J. Chromatogr. B. Biomed. Appl. 681: 251-262.
27. Portaro, F.C., Santos, A.B., Cezari, M.H., Juliano, M.A., Juliano, L., and Carmona, E. 2000. Probing the specificity of cysteine proteinases at subsites remote from the active site: analysis of P4, P3, P2′ and P3′ variations in extended substrates. Biochem. J. 347(Pt. 1): 123-129.
28. Rawlings, N.D., and Barrett, A.J. 1994. Families of cysteine peptidases. Methods Enzymol. 244: 461-486.
29. Reddy, V.Y., Zhang, Q.Y., and Weiss, S.J. 1995. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. U.S.A. 92: 3849-3853.
30. Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858.
31. Srisomsap, C., Subhasitanont, P., Otto, A., Mueller, E.C., Punyarit, P., Wittmann-Liebold, B., and Svasti, J. 2002. Detection of cathepsin B up-regulation in neoplastic thyroid tissues by proteomic analysis. Proteomics, 2: 706-712.
32. Takahashi, S., Murakami, K., and Miyake, Y. 1981. Purification and characterization or porcine kidney cathepsin B. J. Biochem. (Tokyo), 90: 1677-1684.
33. Takahashi, T., Dehdarani, A.H., Schmidt, P.G., and Tang, J. 1984a. Cathepsins B and H from porcine spleen. Purification, polypeptide chain arrangements, and carbohydrate content. J. Biol. Chem. 259: 9874-9882.
34. Takahashi, T., Schmidt, P.G., and Tang, J. 1984b. Novel carbohydrate structures of cathepsin B from porcine spleen. J. Biol. Chem. 259: 6059-6062.
35. Takahashi, T., Yonezawa, S., Dehdarani, A.H., and Tang, J. 1986. Comparative studies of two cathepsin B isozymes from porcine spleen. Isolation, polypeptide chain arrangements, and enzyme specificity. J. Biol. Chem. 261: 9368-9374.
36. Turk, B., Turk, D., and Turk, V. 2000. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta, 1477: 98-111.
37. Turk, V., Turk, B., and Turk, D. 2001. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20: 4629-4633.
38. Wada, K., and Tanabe, T. 1988. Purification and characterization of chicken liver cathepsin B. J. Biochem. (Tokyo), 104: 472-476.
39. Wang, P.H., Do, Y.S., Macaulay, L., Shinagawa, T., Anderson, P.W., Baxter, J.D., and Hsueh, W.A. 1991. Identification of renal cathepsin B as a human prorenin-processing enzyme. J. Biol. Chem. 266: 12 633-12 638.