Spermidine is one of the simple polyamines found in cells of virtually all living organisms. It undergoes a metabolic conversion to N8-acetylspermidine catalyzed by an enzyme in cell nuclei and is converted back to spermidine by a deacetylase in the
Similarity of effects of N8-acetylspermidine and its deacetylase inhibitor on stimulating the growth of L1210 cells.
Z Wang et al.
Proceedings of the Western Pharmacology Society, 38, 41-43 (1995-01-01)
Biochemical and biophysical research communications, 180(2), 591-596 (1991-10-31)
The activity of two naturally occurring monoacetylated polyamines, N8-acetylspermidine and N1-acetylspermidine, as inducers of differentiation of HL60 human leukemia cells was assessed. Differentiation was quantified by morphological changes and the ability to reduce nitroblue tetrazolium. N8-Acetylspermidine produced 25-35 percent differentiation
Journal of neuroscience research, 55(3), 341-351 (1999-05-29)
The endogenous polyamines have been extensively studied with respect to their role in cellular death mechanisms, although the results are contradictory. In contrast, their primary metabolites, the N-acetyl polyamines, have not been much studied. It has been hypothesized that the
Molecular and biochemical parasitology, 51(1), 91-98 (1992-03-01)
Polyamine oxidase plays a key role in the catabolism of polyamines and regeneration of spermidine and putrescine. The mammalian enzyme utilises N1-acetylspermidine, and N8-acetylspermidine, although formed in the mammals, is not catabolised further. We have characterised an enzyme from Acanthamoeba
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