Cathepsin B

International Journal of Biochemistry and Cell Biology

Volumn 29, Issue 5, 1997, Pages 715-720

  Mort, John S ^a   Buttle, David J ^b  

^a SHRINERS HOSPITAL FOR CHILDREN   (Canada)

^b UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

Cathepsin B; Cysteine protease; Enzyme mechanism; Role in pathology

Indexed keywords

ANTIGEN; CATHEPSIN B; COLLAGEN TYPE 1; CYSTEINE PROTEINASE; THYROGLOBULIN;

BONE TURNOVER; CANCER; CYTOCHEMISTRY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SYNTHESIS; HUMAN; INFLAMMATORY DISEASE; LYSOSOME; NONHUMAN; PANCREATITIS; PROTEIN DEGRADATION; PROTEIN PROCESSING; SHORT SURVEY;

EID: 0030810557     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(96)00152-5     Document Type: Article

References (10)

1. Berquin I. M., Cao L., Fong D. and Sloane B. F. (1995) Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene. Gene 159, 143-149.
2. Bohley P. and Seglen P. O. (1992) Proteases and proteolysis in the lysosome. Experientia 48, 151-157.
3. Burnett D., Abrahamson M., Devalia J. L., Sapsford R. J., Davies R. J. and Buttle D. J. (1995) Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by neutrophil elastase. Arch. Biochem. Biophys. 317, 305-310.
4. Buttle D. J. (1994) Lysosomal cysteine endopeptidases in the degradation of cartilage and bone. In Textbook of Immunopharmacology, Immunopharmacology of Joints and Connective Tissue (Edited by Dingle J.T. and Davies M.E.), pp. 224-243. Academic Press, London.
5. Cygler M., Sivaraman J., Grochulski P., Coulombe R., Storer A. C. and Mort J. S. (1996) Structure of rat procathepsin B. Model for inhibition of cysteine protease activity by the proregion. Structure 4, 405-416.
6. Hasnain S., Hirama T., Huber C. P., Mason P. and Mort J. S. (1993) Characterization of cathepsin B specificity by site-directed mutagenesis. Importance of Glu245 in the S2-P2 specificity for arginine and its role in transition state stabilization. J. Biol. Chem. 268, 235-240.
7. Kirschke H., Barrett A. J. and Rawlings N. D. (1995) Proteinases 1: lysosomal cysteine proteinases. Protein Profile 2, 1587-1643.
8. 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.
9. Reyes V. E., Lu S. and Humphreys R. E. (1991) Cathepsin B cleavage of Ii from class II MHC α- and β-chains. J. Immunol. 146, 3877-3880.
10. Rowan A. D., Mason P., Mach L. and Mort J. S. (1992) Rat procathepsin B. Proteolytic processing to the mature form in vitro. J. Biol. Chem. 267, 15993-15999.