Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator.

  title={Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator.},
  author={Anthony E. Pegg},
  journal={American journal of physiology. Endocrinology and metabolism},
  volume={294 6},
  • A. Pegg
  • Published 1 June 2008
  • Biology
  • American journal of physiology. Endocrinology and metabolism
Spermidine/spermine-N(1)-acetyltransferase (SSAT) regulates cellular polyamine content. Its acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. Since polyamines play critical roles in normal and neoplastic growth and in ion channel regulation, SSAT is a key enzyme in these processes. SSAT is very highly regulated. Its content is adjusted in response to alterations in polyamine content to maintain polyamine homeostasis. Certain polyamine analogs can… 

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Spermidine/spermine N1‐acetyltransferase — the turning point in polyamine metabolism

  • R. CaseroA. Pegg
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1993
An understanding of how a cell may, in a tightly controlled manner, facilitate the breakdown, excretion, cycling, and/or intracellular shuttling of the polyamines is led to.

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Proteasomal Degradation of Spermidine/Spermine N 1-Acetyltransferase Requires the Carboxyl-terminal Glutamic Acid Residues*

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Regulation of spermidine/spermine N1‐acetyltransferase expression by cytokines and polyamines in human hepatocarcinoma cells (HepG2)

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Polyamine-dependent Regulation of Spermidine-Spermine N1-Acetyltransferase mRNA Translation*

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