Reductive activation markedly increases the stability of cathepsins B and L to extracellular ionic conditions

Biological Chemistry Hoppe-Seyler

Volumn 377, Issue 6, 1996, Pages 391-394

  Dehrmann, Frieda M ^a   Elliott, Edith ^a   Dennison, Clive ^a  

^a UNIVERSITY OF KWAZULU NATAL   (South Africa)

Author keywords

Activation; Cathepsins; Extracellular; Reduction; Stability

Indexed keywords

CATHEPSIN B; CATHEPSIN L;

ARTICLE; ENZYME ACTIVITY; ENZYME STABILITY; EXTRACELLULAR SPACE; HALF LIFE TIME; HUMAN; IONIC STRENGTH; LIVER; PRIORITY JOURNAL; PROTEIN METABOLISM;

BUFFERS; CATHEPSIN B; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; ENDOPEPTIDASES; ENZYME ACTIVATION; EXTRACELLULAR SPACE; HALF-LIFE; HUMANS; HYDROGEN-ION CONCENTRATION; LIVER; PROTEIN CONFORMATION;

EID: 0029838730     PISSN: 01773593     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Assfalg-Machleidt, I., Rothe, G., Klingel, S., Banati, R., Mangel, W.F., Valet, G., and Machleidt, W. (1992). Membrane permeable fluorogenic Rhodamine substrates for selective determination of cathepsin L Biol. Chem. Hoppe-SeyIer373,433-440.
2. Baici, A., Lang, A., Hörler, D., and Knopfel, M. (1988). Cathepsin B as a marker of the dedifferentiated chondrocyte phenotype. Ann. Rheum. Dis. 47,684 - 691.
3. Barrett, A.J., and Kirschke, H. (1981). Cathepsin B, cathepsin H, cathepsin L. In: Methods in Enzymology, Vol. 80, L. Lorand, ed. (San Diego, Ca., USA: Academic Press Inc.), pp. 535-561.
4. Brocklehurst, K., and Kierstan, M.P.J. (1973). Propapain and its conversion to papain: a new type of zymogen activation mechanism involving intramolecular thiol-disulphide interchange. Nature New Biol. 242,167 -170.
5. Buck, M.R., Karustis, D.G., Day, NA, Honn, K.V., and Sloane, B.F. (1992). Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem. J. 282, 273-278.
6. Chu, C.T., Oury, T.D., Enghild, J.J., and Pizzo, S.V. (1994). Adjuvant-free in vivo targeting. Antigen delivery by a2-macroglobulin enhances antibody formation. J. Immunol. 752,15381545.
7. Dehrmann, P.M., Coetzer, T.H.T., Pike, R.N., and Dennison, C. (1995). Mature cathepsin L is substantially active in the ionic milieu of the extracellular medium. Arch. Biochem. Biophys. 324,93-98.
8. Dennison, C., Pike, R.N., Coetzer, T.H.T., and Kirk, K.C. (1992). Characterisation of the activity and stability of single-chain cathepsin L and of proteolytically active cathepsin L/cystatin complexes. Biol. Chem. Hoppe-Seyler373,419 - 425.
9. Freshney, R.I. (1983). In: Culture of Animal Cells: A Manual of Basic Technique (New York, NY: Alan R. Liss Inc.), p. 69.
10. Gullino, P.M., Grantham, F.H., Smith, S.H., and Haggerty, A.C. (1965). Modification of the acid base status of the internal milieu of tumors. J. Natl. Cancer Inst. 34,857 - 869.
11. Hasnain, S., Hirama, T., Tam, A., and Mort, U.S. (1992). Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast. J. Biol. Chem. 267, 4713-4721.
12. Khan, M.Y., and Ahmad, S. (1987). Anomalous behaviour of cathepsin B: dependence of activity and stability on salt concentration. Biochem. Int. 75,111-115.
13. Khouri, H.E., Plouffe, C., Hasnain, S., Hirama, T., Storer, A.C., and Ménard, R. (1991). A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses. Biochem. J. 275, 751-757.
14. Kirschke, H., Wiederanders, B., Brömme, D., and Rinne, A. (1989). The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B. Biochem. J. 264,467 473.
15. Machleidt, W., Ritonja, A., Popovic, T., Kotnic, M., Brzin, J., Turk, V., Machleidt, I., and Müller-Esterl, W. (1986). Human cathepsins B, H and L: Characterization by amino acid sequences and some kinetics of inhibition by the kininogens. In: Cysteine Proteinases and their Inhibitors, V. Turk, ed. (Berlin, Germany: Walter de Gruyter), pp. 3 -18.
16. Mason, R.W. (1986). Species variants of cathepsin L and their immunological identification. Biochem. J. 240,285 - 288.
17. Mason, R.W., Wilcox, D., Wikstrom, P., and Shaw, E. (1989). The identification of active forms of cysteine proteinases in Kirstenvirus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitor. Biochem. J. 257,125 -129.
18. 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. 285,427 - 434.
19. Mort, J.S., and Recklies, A.D. (1986). Immunological studies on the secreted forms of cathepsin B. In: Cysteine Proteinases and their Inhibitors, V. Turk, ed. (Berlin, Germany: Walter de Gruyter), pp. 63-71.
20. Mort, J.S., Recklies, A.D., and Poole, A.R. (1984). Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH. Arthritis Rheum. 27, 509-515.
21. Pike, R.N., Coetzer, T.H.T., and Dennison, C. (1992). Proteolytically active complexes of cathepsin L and a cysteine protease inhibitor; purification and demonstration of their formation in vitro. Arch. Biochem. Biophys. 294,623 - 629.
22. Rich, D.H., Brown, M.A., and Barrett, A.J. (1986). Purification of cathepsin B by a new form of affinity chromatography. Biochem.J.235,731-734.
23. Turk, B., Dolenc, I., Turk, V., and Bieth, J.G. (1993). Kinetics of the pH-induced inactivation of human cathepsin L. Biochemistry 32,375-380.
24. Turk, B., Dolenc, I., Zerovnik, E., Turk, D., Gubensek, F., and Turk, V. (1994). Human cathepsin B is a metastable enzyme stabilized by specific ionic interactions associated with the active site. Biochemistry 33,14800 -14806.
25. Willenbrock, F., and Brocklehurst, K. (1985). A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Biochem. J. 227, 521-528.