Identification of an interleukin-1β converting enzyme-like activity that increases upon treatment of P19 cells with retinoic acid as the proteasome

Journal of Biochemistry

Volumn 120, Issue 4, 1996, Pages 699-704

  Kobayashi, Tatsuyuki ^a,b   Shinozaki, Ayako ^a   Momoi, Takashi ^a,b   Arahata, Kiichi ^a   Tsukahara, Toshifumi ^a  

^a NATIONAL INSTITUTE OF NEUROSCIENCE   (Japan)

^b TOKYO MEDICAL UNIVERSITY   (Japan)

Author keywords

Apoptosis; ICE like activity; Neural differentiation; P19 cells; Proteasome

Indexed keywords

INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEASOME; RETINOIC ACID;

ANIMAL CELL; APOPTOSIS; ARTICLE; CELL DIFFERENTIATION; CONTROLLED STUDY; EMBRYONAL CARCINOMA; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; GENE; IMMUNOADSORPTION; IMMUNOBLOTTING; MOLECULAR WEIGHT; MOUSE; NONHUMAN;

ANIMALIA;

EID: 0029853157     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021467     Document Type: Article

References (28)

1. 1. Yuan, J., Shaham, S., Ledoux, S., Ellis, H.M., and Horvitz, H.R. (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-lβ-converting enzyme. Cell 75, 641-652
2. Miura, M., Zhu, H., Rotello, R., Hartwieg, E.A., and Yuan, J. (1993) Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C, elegans cell death gene ced-3. Cell 75, 653-660
3. Enari, M., Hug, H., and Nagata, S. (1995) Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375, 78-81
4. Los, M., Vande Crean, M., Penning, L.C., Schenk, H., Westendrop, M., Baeuerle, P.A., Droge, W., Krammer, P.H., Flers, W., and Schulze-Osthoff, K. (1995) Requirement of an ICE/CED-3 protease for Fas/APO-1 -mediated apoptosis. Nature 375, 81-83
5. Kumar, S. (1995) Inhibition of apoptosis by the expression of antisense Nedd-2. FEBS Lett. 368, 69-72
6. Oaborne, B.A. and Schwartz, L.M. (1994) Essential genes that regulate apoptosis. Trends Cell Biol. 4, 394-399
7. Steller, H. (1995) Mechanisms and genes of cellular suicide. Science 287, 1445-1462
8. Martin, S.J, and Green, D.R. (1995) Protease activation during apoptosis: Death by a thousand cuts? Cell 82, 349-352
9. Ayala, J.M., Yamin, T.-T., Egger, L.A., Chin, J., Kostura, M.J., and Miller, D.K. (1994) IL-1β-converting enzyme is present in monocytic cells as an inactive 45-κDa precursor. J. Immunol. 183, 2592-2599
10. McBurney, M.W., Jones-Villeneuve, E.M., Edwards, M.K., and Anderson, P.J. (1982) Control of muscle and neuronal differentiation in a cultured embryonal carcinoma cell line. Nature 299, 165-167
11. Campione-Piccardo, J., Sun, J.J., Craig, J., and McBurney, M.W. (1985) Cell-cell interaction can influence drug-induced differentiation of murine embryonal carcinoma cells. Dev. Biol. 109, 25-31
12. Tsukahara, T., Kunika, N., Momoi, T., and Arahata, K. (1995) Regulation of alternative splicing in the amyloid precursor protein (APP) mRNA during neuronal and glial differentiation of P19 embryonal carcinoma cells. Brain Res. 679, 178-183
13. Tsukahara, T., Ishiura, S., and Sugita, H. (1990) Changes in proteinase activities during the differentiation of murine erythroleukemia cells. Exp. Cell Res. 188, 111-116
14. Thornberry, N.A. (1994) Interleukin-1β converting enzyme in Methods in Enzymology (Barrett, A.J., ed.) Vol. 244, pp. 615-631, Academic Press, New York
15. Tsukahara, T., Ishiura, S., and Sugita, H. (1990) Regulation of prolyl endopeptidase activity by the intracellular redox state. J. Biol. Chem. 286, 21448-21453
16. Tsukahara, T., Ishiura, S., and Sugita, H. (1988) An ATP-dependent protease and- ingensin, the multicatalytic proteinase, in K562 cells. Eur, J. Biochem. 177, 261-266
17. Tanaka, K., Ii, K., Ichihara, A., Waxman, L., and Goldberg, A.L. (1986) A high molecular weight protease in the cytosol of rat liver. J. Biol. Chem. 281, 15197-15203
18. Yamamoto, T., Nojima, M., Ishiura, S., and Sugita, H. (1986) Purification of the two forms of the high-molecular-weight neutral proteinase ingensin from rat liver. Biochim. Biophys, Acta 882, 297-304
19. Sionov, R.V. and Gallily, R. (1992) The unique killing of embryo-derived teratocarcinoma cells by nonactivated murine macrophages is not due to a lack of H-2 antigen expression. Cell. Immunol. 142, 416-425
20. Peters, J.M. (1994) Proteasomes: Protein degradation machines of the cell. Trends Biochem. Sci. 19, 377-382
21. Hochstrasser, M. (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223
22. Irmler, M., Hertig, S., MacDonald, H.R., Sadoul, R., Becherer, J.D., Proudfoot, A., Solari, R., and Tschopp, J. (1995) Granzyme A is an interleukin Iβ-converting enzyme. J. Exp. Med. 181, 1917-1922
23. Akiyama, K., Yokota, K., Kagawa, S., Shimbara, N., Tamura, T., Akioka, H., Nothwang, H.G., Noda, C., Tanaka, K., and Ichihara, A. (1994) cDNA cloning and interferon gamma downregulation of proteasomal subunits X and Y. Science 285, 1231- 1234
24. Haas, A.L., Baboshina, O., Williams, B., and Schwartz, L.M. (1995) Coordinated'induction of the ubiquitin conjugation pathway accompanies the developmentally programmed death of insect skeletal muscle. J. Biol. Chem. 270, 9407-9412
25. Kaufmann, S.H., Desnoyers, S., Ottaviano, Y., Davidson, N.E., and Poirier, G.G. (1993) Specific proteolytic cleavage of poly(ADP-ribose)polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53, 3976-3985
26. Lazebnik, Y.A., Kaufmann, S.H., Desnoyers, S., Poirier, G.G., and Earnshaw, W.C. (1994) Cleavage of poly(ADP-ribose)polymerase by a proteinase with properties like ICE. Nature 371, 346-347
27. Casciola-Rosen, L.A., Miller, D.K., Anhalt, G.J., and Rosen, A. (1994) Specific cleavage of the 70-κDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J. BM, Chem. 269, 30757-30760
28. Lazebnik, Y.A., Takahashi, A., Moir, R.D., Goldman, R.D., Poirier, G.G., Kaufmann, S.H., and Earnshaw, W.C. (1995) Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution. Proc. Natl. Acad. Sci. USA 92, 9042-9046