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

Journal of Biochemistry
T KobayashiT Tsukahara

Abstract

We examined changes in proteinase activities in P19 embryonal carcinoma cells during retinoic acid-induced differentiation. The interleukin-1 beta converting enzyme (ICE)-like Ac-YVAD-MCA hydrolytic activity was increased about 6-fold by treatment with retinoic acid. This activity was inhibited by N-ethylmaleimide and Ac-YVAD-H but not by E-64, EDTA, PMSF, or amastatin. The ICE-like activity in P19 cells eluted as a single peak just after the void volume on gel filtration. No ICE-like activity was observed at a molecular mass of 30-50 kDa. Enzymatic purification, Western blot analysis, and an immunoabsorption study demonstrated that the ICE-like activity in P19 cells is caused by the proteasome, and is stimulated during retinoic acid-induced differentiation. The proteasome purified from mouse liver also cleaved Ac-YVAD-MCA. These results strongly suggest that the proteasome is a major ICE-like proteinase in P19 cells and may be involved in the neural differentiation and the apoptotic pathway.

Citations

Aug 19, 2005·Molecular and Cellular Biology·Stephen E KendallJoseph M Verdi
Mar 4, 2008·Methods : a Companion to Methods in Enzymology·Scott H KaufmannWilliam C Earnshaw
Oct 22, 2005·FEMS Microbiology Letters·Michele BastianiFabiana Horn
Jan 30, 2008·Current Protocols in Cell Biology·S H KaufmannW C Earnshaw
Apr 16, 1998·The Journal of Biological Chemistry·L MonneyC Borner

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