PMID: 2495941Mar 1, 1989Paper

Involvement of antizyme in stabilization of ornithine decarboxylase caused by inhibitors of polyamine synthesis

European Journal of Biochemistry
Y MurakamiS Hayashi

Abstract

Contrary to previous findings, ornithine decarboxylase (ODC) was stabilized by treatment of cells with DL-alpha-difluoromethylornithine, an enzyme-activated irreversible inhibitor of ODC. Both this inhibitor and cyclohexylamine, a spermidine synthase inhibitor known to stabilize ODC, caused decreases in the antizyme/ODC ratio by increasing ODC content and conversely decreasing antizyme content. The relationship between cellular polyamine levels and antizyme content indicated that spermidine is the most important polyamine for antizyme induction. These results suggest that antizyme is involved in the mechanism underlying the stabilization of ODC by inhibitors of polyamine synthesis and support the hypothesis that cellular polyamines regulate ODC degradation via antizyme.

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Citations

Apr 26, 2000·Proceedings of the National Academy of Sciences of the United States of America·I P IvanovJ F Atkins
Dec 17, 2008·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Hua TangKen-ichi Yamamura
Dec 1, 1992·Cell Biochemistry and Function·C StefanelliC M Caldarera
Feb 16, 2018·Scientific Reports·Noriyuki MuraiSenya Matsufuji
Jan 1, 1990·Life Sciences·J A López-BallesterR Peñafiel
Oct 1, 1991·Archives of Biochemistry and Biophysics·J L MitchellA Bareyal-Leyser
Sep 29, 1989·Biochemical and Biophysical Research Communications·F FlamigniC M Caldarera
Oct 30, 1990·Biochemical and Biophysical Research Communications·F FlamigniC M Caldarera

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