Accumulation of <i>N</i>1-acetylspermidine in heart and spleen of isoprenaline-treated rats

Stefanelli, Claudio; Carati, Daniela; Rossoni, Carmen; Flamigni, Flavio; Caldarera, Claudio Marcello

doi:10.1042/bj2370931

Cited by 11 publications

(4 citation statements)

References 20 publications

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“…The acetylated polyamine is then oxidized by a flavin-dependent enzyme, polyamine oxidase (PAO), with the formation of the parent polyamine (putrescine or spermidine) and the oxidation products H202 and acetamidopropanal (Pegg, 1986). N1-SAT is a short-lived protein that is rapidly induced by a wide variety of stresses and trophic agents (Matsui et al, 1981;Danzin et al, 1982;Della Ragione & Pegg, 1983;Persson & Pegg, 1984;Stefanelli et al, 1986;Erwin & Pegg, 1986;Halline et al, 1989). This burst of oxidative polyamine catabolism may be part of a general cellular response to stressors, although there may be species-specific differences in the regulation and expression of PAO (Hirvonen et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Polyamine regulation of heat-shock-induced spermidine N1-acetyltransferase activity

Fuller

Carper

Clay

et al. 1990

Biochemical Journal

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The enzyme spermidine/spermine N1-acetyltransferase (N1-SAT) is rapidly induced by heat shock in CHO and A549 cells, with activity declining by 24 h. Depletion of intracellular polyamines by alpha-difluoromethylornithine, an inhibitor of ornithine decarboxylase, blocks this induction. Re-addition of putrescine to these cultures restores the response to heat shock, with a concomitant increase in intracellular N1-acetylspermidine. Diaminopropane is more than twice as effective as the naturally occurring diamine putrescine, suggesting that the propylamine moiety of spermidine is involved in the regulation of N1-SAT induction. Inhibitor studies indicate transcriptional activation and that the enzyme has an apparent half-life of 30-60 min. A second heat shock rapidly inhibits induced N1-SAT activity, which decays with a half-life of 2-3 min. Despite its induction by heat, N1-SAT is not a stable enzyme, suggesting that the activity observed is not due to a modification of an existing peptide, but is due to a transcriptional event, which may justify the inclusion of this enzyme in the family of heat-shock proteins.

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Section: Introductionmentioning

confidence: 99%

Polyamine regulation of heat-shock-induced spermidine N1-acetyltransferase activity

Fuller

Carper

Clay

et al. 1990

Biochemical Journal

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“…Previous studies have shown that SAT activity is increased by a number of factors, including hepatotoxins, hormones, lectins, growth factors and heat shock (Matsui & Pegg, 1980;Matsui et al, 1981;Danzin et al, 1982;Della Ragione & Pegg, 1984;Shinki et al, 1985;Steffanelli et al, 1986;Ekstrom et al, 1989;Harari et al, 1989a,b;Matsui-Yuasa et al, 1989). One possible unifying factor which might mediate stimulation by these agents is an increase in the free intracellular polyamine concentration, owing to the overproduction of polyamines or the release of intracellular polyamines from some Vol.…”

Section: Discussionmentioning

confidence: 99%

Induction of spermidine/spermine N1-acetyltransferase activity in Chinese-hamster ovary cells by N1N11-bis(ethyl)norspermine (corrected) and related compounds

Pegg

Pakala

Bergeron

1990

Biochemical Journal

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Treatment of Chinese-hamster ovary (CHO) cells with N1N11-bis(ethyl)norspermine (BENSM) led to a very large increase in the activity of spermidine/spermine N1-acetyltransferase (SAT), which rose by about 600-fold within 48 h. Smaller, but still very large increases, were also produced in decreasing order of potency by 3,7,11,15,19-penta-azaheneicosane, N1N12-bis(ethyl)spermine and by N1N14-bis(ethyl)homospermine. The rise in acetyltransferase activity was due to an increase in enzyme protein, as indicated by immunoblotting using antibodies directed against rat liver SAT. There was an increase in the content of mRNA for SAT, indicating that BENSM regulates the level of enzyme protein partly by means of a change in transcription or stability of the mRNA. There was also a decreased rate of degradation of the protein in CHO cells trated with the drug. This may be due to the binding of BENSM, which is a competitive inhibitor of the enzyme with a Ki of 120 microM. Exposure to BENSM led to an increased conversion of spermidine into N1-acetylspermidine and putrescine, a rapid fall in the content of intracellular polyamines and the excretion from the cell of putrescine, N1-acetylspermidine and spermidine. When polyamine oxidase activity in the treated cells was blocked, increases in N1-acetylspermidine and N1-acetylspermine were much greater, and the formation of putrescine was prevented. These results indicate that the induction of SAT facilities the degradation of spermine and spermidine to putrescine and the subsequent excretion of putrescine from the cell. When the degradation of the N1-acetyl derivatives by polyamine oxidase is blocked, the cells excrete N1-acetylspermidine instead of putrescine. CHO cells also contained and excreted N8-acetylspermidine, but its synthesis was not increased in cells treated with BENSM, confirming data obtained in vitro that SAT does not produce this derivative.

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“…Paraquat accepts electrons from cellular electron transfer systems and donates them to oxygen, forming superoxide anion in many tissues (23). Isoprenaline produces superoxide anion directly (22), and it also elevates the N1-acetyl-SPD levels in rat heart and spleen (25). In contrast, CC14, CHC13 and CH2C12 are changed into chloromethyl-free radicals through dehalogenation by cytochrome P-450 enzyme, especially in the liver (10, 17).…”

Section: Discussionmentioning

confidence: 99%

Elevation of acetylpolyamine levels in mouse tissues, serum and urine after treatment with radical-producing drugs and lipopolysaccharide

et al. 1988

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Polyamines and acetylpolyamines were analyzed in the liver, spleen, lung, kidney, serum and urine by high-performance liquid chromatography on a column of cation-exchange resin after administering various cytotoxic substances to male mice. All of the compounds tested more or less affected the tissue levels of polyamines, including putrescine, spermidine, spermine and acetylpolyamines (N1-acetylspermidine and N1-acetylspermine). It was found that they were classified into two groups of substances: one group (including radical-producing drugs and lipopolysaccharide) which elevated the tissue levels of N1-acetylspermidine, especially in the liver, while another group of drugs (such as D-galactosamine and DL-ethionine) had little effect on the acetylpolyamine levels. When the acetylpolyamine levels rose, the levels of spermidine and spermine declined, and then putrescine levels were elevated. N1-Acetylspermine was detected only when N1-acetylspermidine levels were very high after treatment with radical-producing drugs and lipopolysaccharide. Halogenated carbon, such as carbon tetrachloride and halothane, elevated the levels of acetylpolyamines especially in the liver, while paraquat elevated them in all tissues examined.

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Accumulation of N1-acetylspermidine in heart and spleen of isoprenaline-treated rats

Cited by 11 publications

References 20 publications

Polyamine regulation of heat-shock-induced spermidine N1-acetyltransferase activity

Polyamine regulation of heat-shock-induced spermidine N1-acetyltransferase activity

Induction of spermidine/spermine N1-acetyltransferase activity in Chinese-hamster ovary cells by N1N11-bis(ethyl)norspermine (corrected) and related compounds

Elevation of acetylpolyamine levels in mouse tissues, serum and urine after treatment with radical-producing drugs and lipopolysaccharide

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