INVOLVEMENT OF ANTIZYME IN STABILIZATION OF ORNITHINE DECARBOXYLASE CAUSED BY INHIBITORS OF POLYAMINE SYNTHESIS
INVOLVEMENT OF ANTIZYME IN STABILIZATION OF ORNITHINE DECARBOXYLASE CAUSED BY INHIBITORS OF POLYAMINE SYNTHESIS
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DOI：
10.1111/j.1432-1033.1989.tb14630.x
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发表时间：
1989-03-01
期刊：
影响因子：
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通讯作者：
HAYASHI, S
中科院分区：
文献类型：
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作者：
MURAKAMI, Y;NISHIYAMA, M;HAYASHI, S
与以前的发现相反，通过用DL-α-鸟氨酸脱羧酶（ODC）处理细胞使其稳定。二氟甲基鸟氨酸，ODC的酶激活不可逆抑制剂。这两种抑制剂和环己胺，亚精胺合酶抑制剂，已知稳定ODC，引起抗酶/ODC的比例下降，增加ODC含量，反之降低抗酶含量。细胞内多胺水平与抗酶含量的关系表明，亚精胺是诱导抗酶的最重要的多胺。这些结果表明，抗酶参与了多胺合成抑制剂稳定ODC的机制，并支持细胞多胺通过抗酶调节ODC降解的假设。
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 antienzyme 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 polyamine regulate ODC degradation via antienzyme.