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   <subfield code="a">Identification of an Interleukin-1β Converting Enzyme-Like Activity That Increases upon Treatment of P19 Cells with Retinoic Acid as the Proteasome</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Tatsuyiki Kobayashi, Ayako Shinozaki, Takashi Momoi, Kiichi Arahata, Toshifumi Tsukahara]</subfield>
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   <subfield code="a">We examined changes in proteinase activities in Pl9 embryonal carcinoma cells during retinoic acid-induced differentiation. The interleukin-1β 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 proteinam in P19 cells and may be involved in the neural differentiation and the apoptotic pathway.</subfield>
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   <subfield code="a">© 1996 BY THE JOURNAL OF BIOCHEMISTRY</subfield>
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   <subfield code="a">apoptosis</subfield>
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   <subfield code="a">Shinozaki</subfield>
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   <subfield code="t">The Journal of Biochemistry</subfield>
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