Rapid turnover of tryptophan hydroxylase in serotonin producing cells: demonstration of ATP‐dependent proteolytic degradation

FEBS Letters

Oguro, Kazuya¹  Nakanishi, Nobuo²  Kojima, Masayo¹  Hasegawa, Hiroyuki¹ 

[1] Department of Bioscience, The Nishi-Tokyo University, Uenohara, Yamanashi 409-01, Japan;Department of Biochemistry, Meikai University School of Dentistry, Sakato, Saitama 350-02, Japan

关键词: Tryptophan hydroxylase;    Serotonin biosynthesis;    Mast cell;    Proteolysis;   

DOI  :  10.1016/0014-5793(95)00629-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A rapid and continuous proteolysis of tryptophan hydroxylase was demonstrated with two mast cell lines derived from rat basophilic leukemia cells (RBL2H3) and mouse mastocytoma (FMA3). Under conditions in which protein biosynthesis was arrested by administration of cycloheximide, the decay profile of tryptophan hydroxylase protein was traced by Western blot analysis. Incorporation of [³⁵S]methionine and the chase experiment performed without interfering with the metabolic stage also showed that tryptophan hydroxylase has been cleaved rapidly. The half life of the enzyme was 11–15 min in RBL2H3 cells and 40–60 min in FMA3 cells, and the process was demonstrated to be dependent on intracellular ATP.

【 授权许可】

Unknown