Regulation of spermidine/spermine N 1‐acetyltransferase by intracellular polyamine pools

FEBS Letters

Fogel-Petrovic, M.F.¹  Shappell, N.W.¹  Porter, C.W.¹ 

[1] Grace Cancer Drug Center, Roswell Park Cancer Institute, Elm and Carlton Streets, Buffalo, NY 14263-0001, USA

关键词: Polyamine;    Polyamine homeostasis;    Spermidine;    Spermine;    Spermidine/spermine N 1-acetyltransferase;    AMA;    S-(5'-deoxy-5-adenosyl)-methylthioethylhydroxylamine;    DFMO;    α-difluoromethylornithine;    ODC;    ornithine decarboxylase;    PUT;    putrescine;    SAMDC;    S-adenosylmethionine decarboxylase;    SPD;    spermidine;    SPM;    spermine;    SSAT;    spermidine/ spermine-N 1-acetyltransferase;   

DOI  :  10.1016/0014-5793(93)80103-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Through its role in polyamine acetylation and the back-conversion pathway, spermidine/spermine N ¹-acetyltransferase (SSAT) has the potential to control intracellular polyamine pools by facilitating their catabolism and/or excretion. The possibility that the enzyme is subject to regulation by intracellular polyamine pools was investigated in MALME-3 human melanoma cells. Increases in intracellular polyamine pools by treatment with 3 μM exogenous spermidine or spermine for 48 h caused SSAT activity to increase 111% and 226%, respectively, and SSAT-specific mRNA to rise 19% and 66%, respectively. Decreases in polyamine pools by treatment with inhibitors of polyamine biosynthesis caused SSAT activity to decrease by 46% and mRNA to fall by 89%. Both SSAT activity and mRNA were more sensitive to changes in spermine than spermidine. The identification of a positive regulatory relationship between SSAT and intracellular polyamine pools further implicates this enzyme in a proposed model for polyamine pool homeostasis.

【 授权许可】

Unknown