Analysis of where and which types of proteinases participate in lysosomal proteinase processing using Bafilomycin A1 and Helicobacter pylori Vac A toxin

Journal of Biochemistry

Volumn 125, Issue 4, 1999, Pages 770-779

  Ishidoh, Kazumi ^a   Takeda Ezaki, Mitsue ^a   Watanabe, Sumio ^a   Sato, Nobuhiro ^a   Aihara, Miki ^b   Imagawa, Kenichi ^b   Kikuchi, Mikio ^b   Kominami, Eiki ^a  

^a JUNTENDO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b OTSUKA PHARMACEUTICAL CO LTD   (Japan)

Author keywords

Bafilomycin A1; Cathepsins; Processing; Proteinase inhibitors; Vac A toxin

Indexed keywords

ADENOSINE TRIPHOSPHATASE INHIBITOR; BACTERIAL TOXIN; BAFILOMYCIN A1; CATHEPSIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN L; ENZYME PRECURSOR; LYSOSOME ENZYME; PEPSTATIN; PROTEINASE; PROTEINASE INHIBITOR;

ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CONTROLLED STUDY; ENZYME DEGRADATION; HELICOBACTER PYLORI; MOUSE; NONHUMAN; PH; PROTEIN PROCESSING;

ANIMALIA; BACTERIA (MICROORGANISMS); HELICOBACTER PYLORI;

EID: 0032906630     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022348     Document Type: Article

References (53)

1. Pfeifer, U. (1987) Functional morphology of the lysosomal apparatus in Lysosomes: Their Role in Protein Breakdown (Glaumann, H. and Ballard, F.J., eds.) pp. 3-59, Academic Press, London
2. Erickson, A.M., Ginns, E.I., and Barranger, J.A. (1985) Biosynthesis of the lysosomal enzyme glucocerebrosidase. J. Biol. Chem. 260, 14319-14324
3. Kirschke, H. and Barrett, A.J. (1987) Chemistry of lysosomal proteases in Lysosomes: Their Role in Protein Breakdown (Glaumann, H. and Ballard, F.J., eds.) pp. 193-238, Academic Press, London
4. Ishidoh, K. and Kominami, E. (1995) Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro. Biochem. Biophys. Res. Commun. 217, 624-631
5. Rowan, A.D., Mason, P., Mach, L., and Mort, J.S. (1992) Rat cathepsin B-proteolytic processing to the mature from in vitro-. J. Biol. Chem. 267, 15993-15999
6. Menard, R., Carmona, E., Takebe, S., Defour, E., Plouffe, C., Mason, P., and Mort, J.S. (1998) Autocatalytic processing of recombinant human procathepsin L-contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem. 273, 4478-4484
7. Larsen, L.B., Boisen, A., and Petersen, T. (1993) Procathepsin D cannot autoactivate to cathepsin D at acid pH. FEBS Lett. 319, 54-58
8. Nishimura, Y., Kawabata, T., Furuno, K., and Kato, K. (1989) Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosomes. Arch. Biochem. Biophys. 271, 400-406
9. Hara, K., Kominami, E., and Katunuma, N. (1988) Effect of proteinase inhibitors on intracellular processing of cathepsin B, H, and H in rat macrophages. FEBS Lett. 231, 229-231
10. Ammerer, G., Hunter, C.P., Rothman, J.H., Saari, G.C., Valls, L.A., and Stevens, T.H. (1986) PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell. Biol. 6, 2490-2499
11. Woolford, C.A., Daniels, L.B., Park, F.J., Jones, E.W., Van Arsdell, J.N., and Innis, M.A. (1986) The PEP4 gene encodes an aspartic protease implicated in the post translational regulation of Saccharomyces cerevisiae vacuolar hydrolyses. Mol. Cell. Biol. 6, 2500-2510
12. Authier, F., Mort, J.S., Bell, A.W., Posner, B.I., and Bergeron, J.J. (1995) Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D. J. Biol. Chem. 270, 15798-15807
13. Pierre, P. and Mellman, I. (1998) Exploring the mechanisms of antigen processing by cell fractionation. Curr. Opin. Immunol. 10, 145-153
14. Chapman, H.A. (1998) Endosomal proteolysis and MHC class II function. Curr. Opin. Immunol. 10, 93-102
15. Nakagawa, T., Roth, W., Wong, P., Nelson, A., Farr, A., Deussing, J., Villadangos, J.A., Ploegh, H., Peters, C., and Rudensky, A. Y. (1998) Cathepsin L: critical role in Ii degradation and CD4 T cells selection in the thymous. Science 280, 450-453
16. Bowman, E.J., Siebers, A., and Altendorf, K. (1988) Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. USA 85, 7972-7976
17. Oda, K., Nishimura, Y., Ikehara, Y., and Kato, K. (1991) Bafilomycin A1 inhibits the targeting of lysosomal acid hydrolyses in cultured hepatocytes. Biochem. Biophys. Res. Commun. 178, 369-377
18. van Weert, A.W., Dumm, K.W., Gueze, H.J., Maxfield, F.R., and Stoorvogel, W. (1995) Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump. J. Cell Biol. 130, 821-834
19. Yoshimori, T., Yamamoto, A., Moriyama, Y., Futai, M., and Tashiro, Y. (1991) Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells. J. Biol. Chem. 266, 17707-17712
20. Cover, T.L. and Blaser, M.J. (1992) Purification and characterization of the vacuolating toxin from Helicobacter pylori. J. Biol. Chem. 267, 10570-10575
21. Cover, T.L., Tummuru, M.K., Cao, P., Thompson, S.A., and Blaser, M.J. (1994) Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains. J. Biol. Chem. 269, 10566-10573
22. Phadnis, S.H., Ilver, D., Janzon, L., Normark, S., and Westblom, T.U. (1994) Pathological significance and molecular characterization of the vacuolar toxin gene of Helicobacter pylori. Infect. Immun. 62, 1557-1565
23. Papini, E., Bugnoli, M., de Bernard, M., Figura, N., Rappuoli, R., and Montecucco, C. (1993) Bafilomycin A1 inhibits Helicobacter pylori-induced vocalization of HeLa cells. Mol. Microbiol. 7, 323-327
24. Cover, T.L., Reddy, L.Y., and Blaser, M.J. (1993) Effects of ATPase inhibitors on the response of HeLa cells to Helicobacter pylori vacuolating toxin. Infect. Immun. 61, 1427-1431
25. Papini, E., de Bernard, M., Milia, E., Bognoli, M., Zerial, M., Rappuoli, R., and Montecucco, C. (1994) Cellular vacuoles induced by Helicobacter pylori originate from late endosomal compartments. Proc. Natl. Acad. Sci. USA 91, 9720-9724
26. Papini, E., Satin, B., Bucci, C., de Bernard, M., Telford, J.L., Manetti, R., Rappuoli, R., Zerial, M., and Montecucco, C. (1997) The small GTP binding protein Rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin. EMBO J. 16, 15-24
27. Sato, N., Watanabe, S., Wang, X-E., Hirose, M., Oide, H., Kitamura, T., Ohkura, R., Otaka, K., Miwa, H., Miyazaki, A., Aihara, M., Azuma, A., Imagawa, K., and Kikuchi, M. (1996) Inhibition of rabbit gastric epithelial restoration be a water extract of Helicobacter pylori: evidence using a cultured cell model. Inflammopharmacology 4, 341-349
28. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
29. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
30. Okazaki, I., Himeno, M., Ezaki, J., Ishikawa, T., and Kato, K. (1992) Purification and characterization of an 85 kDa sialoglycoprotein in rat liver lysosomal membrane. J. Biochem. 111, 763-769
31. Muno, D., Ishidoh, K., Ueno, T., and Kominami, E. (1993) Processing and transport of the precursor of cathepsin C during its transfer into lysosomes. Arch. Biochem. Biophys. 306, 103-110
32. Muno, D., Sutoh, N., Watanabe, T., Uchiyama, Y., and Kominami, E. (1990) Effect of metabolic alternations on the density and the contents of cathepsins B, H, and L of lysosomes in rat macrophages. Eur. J. Biochem. 191, 91-98
33. Ishidoh, K., Saido, T.C., Kawashima, S., Hirose, M., Watanabe, S., Sato, N., and Kominami, E. (1998) Multiple processing of procathepsin L to cathepsin L in vivo. Biochem. Biophys. Res. Commun. 252, 202-207
34. Ishidoh, K. and Kominami, E. (1994) Multi-step processing of procathepsin L in vitro. FEBS Lett. 352, 281-284
35. Kominami, E., Ueno, T., Muno, D., and Katunuma, N. (1991) The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins. FEBS Lett. 287, 189-192
36. Rosenfeld, M.G., Kreibich, G., Sabatini, D.D., and Kato, K. (1983) Biosynthesis of lysosomal enzymes in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) Vol. 96, pp. 764-777, Academic Press, San Diego
37. 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
38. Strous, G.J., van Kerkhof, P., Dekker, J., and Schwartz, A.L. (1988) Metalloendopeptidase inhibitors block protein synthesis, intracellular transport, and endocytosis in hepatoma cells. J. Biol. Chem. 263, 18197-18204
39. Claus, V., Jahraus, A., Tjelle, T., Berg, T., Kirschke, H., Faulstich, H., and Griffith, G. (1998) Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages-enrichment of cathepsin H in early endosomes. J. Biol. Chem. 273, 9842-9851
40. Shi, G-P., Webb, A.C., Foster, K.E., Knoll, J.H., Lemere, C.A., Munger, J.S., and Chapman, H.A. (1994) Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. J. Biol. Chem. 269, 11530-11536
41. Riese, R.J., Wolf, P.R., Bromme, D., Natkin, L.R., Villadangos, J.A., Ploegh, H.L., and Chapman, H.A. (1996) Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4, 357-366
42. Ishidoh, K., Muno, D., Sato, N., and Kominami, E. (1991) Molecular cloning of cDNA for rat cathepsin C-cathepsin C, a cysteine proteinase with an extremely long propeptide. J. Biol. Chem. 266, 16312-16317
43. Nikawa, T., Towatari, T., and Katunuma, N. (1992) Purification and characterization of cathepsin J from rat liver. Eur. J. Biochem. 204, 381-393
44. Fukuda, M. (1991) Lysosomal membrane glycoproteins-structure, biosynthesis, and intracellular trafficking. J. Biol. Chem. 266, 21327-21330
45. + T-lymphocytes. FEBS Lett. 405, 253-259
46. Saftig, P., Hetman, M., Schmahl, W., Weber, K., Heine, L., Mossmann, H., Koster, A., Hess, B., Evert, M., von Figura, K., and Peters, C. (1995) Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 14, 3599 3608
47. Deussing, J., Roth, W., Saftig, P., Peters, C., Ploegh, H.L., and Villadangos, J.A. (1998) Cathepsins B and D are dispensable for major histocompatibility complex class-II mediated antigen presentation. Proc. Natl. Acad. Sci. USA 95, 4516-4521
48. Simons, K. and Zerial, M. (1993) Rab proteins and the road maps for intracellular transport. Neuron 11, 789-799
49. Vitelli, R., Santillo, M., Lattero, D., Chiariello, M., Bifulco, M., Bruni, C.B., and Bucci, C. (1997) Role of the small GTPase RAB7 in the late endocytic pathway. J. Biol. Chem. 272, 4391-4397
50. Mukhopadhyay, A., Funato, K., and Stahl, P.D. (1997) Rab 7 regulates transport from early to late endocytic compartment in Xenopus oocytes. J. Biol. Chem. 272, 13055-13059
51. Kornfeld, S. (1990) Lysosomal enzyme targeting. Biochem. Soc. Trans. 18, 367-374
52. Griffith, G., Hoflack, B., Simons, K., Mellman, I., and Kornfeld, S. (1988) The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell 52, 329-341
53. Guagliardi, L.E., Koppelman, B., Blum, J.S., Marks, M.S., Cresswell, P., and Brodsky, F.M. (1990) Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature 343, 133-139