Disease relevance of Sms

• It is suggested that although hepatic spermine synthase is sensitive to excess methionine feeding, methionine toxicity is not mediated by defective polyamine metabolism [1].
• The effects of a potent spermidine synthase inhibitor, trans-4-methylcyclohexylamine (4MCHA), and a spermine synthase inhibitor, N-(3-aminopropyl)cyclohexylamine (APCHA), on polyamine biosynthesis and cell growth have been studied in rat hepatoma cells (HTC cells) in culture [2].

High impact information on Sms

• Preliminary biological results demonstrate that AdoDATAD is a potent and specific inhibitor of mammalian spermine synthase in vitro, while being almost completely devoid of inhibitory activity toward the closely related aminopropyltransferase spermidine synthase [3].
• Synthesis and biological evaluation of S-adenosyl-1,12-diamino-3-thio-9-azadodecane, a multisubstrate adduct inhibitor of spermine synthase [3].
• It was found that none of the compounds were effective substrates for spermine synthase, and only one, namely 8,8-dimethylspermidine, was a substrate for spermidine/spermine N1-acetyltransferase [4].
• Hepatic accumulation of S-adenosylmethionine was accompanied by 40% stimulation of methionine adenosyltransferase and 40% repression of spermine synthase over a 2-week period [5].
• The specific inhibitors of spermidine and spermine synthase, bis-cyclohexylammonium sulphate and N-alkylated-1,3-diaminopropane respectively, inhibited the stimulation of Na+/K(+)-ATPase by AVP, this inhibition being reversed by spermine [6].

Biological context of Sms

• Seven different polyamine-linked Sepharose derivatives were prepared for the affinity chromatography of spermidine and spermine binding macromolecules: Spermine synthase from rat and hog brain was used as a model protein with a spermidine binding site [7].

Associations of Sms with chemical compounds

• The spermine content of the cells was increased by exposure to this drug presumably since spermine synthase was able to use a greater proportion of the available decarboxylated S-adenosylmethionine when spermidine synthase was inhibited [8].
• Two of them, trans-4-methylcyclohexylamine (4MCHA) and N-(3-aminopropyl)cyclohexylamine (APCHA), selectively and potently inhibited the activities of spermidine synthase and spermine synthase, respectively [9].
• Aminooxy analogues of spermidine as inhibitors of spermine synthase and substrates of hepatic polyamine acetylating activity [10].
• Inhibition by ATA of spermidine synthase was 'uncompetitive' with respect to putrescine and that of spermine synthase was 'non-competitive' with respect to spermidine [11].
• Activities of aminopropyltransferases (spermidine synthase and spermine synthase) were inhibited by aurintricarboxylic acid (ATA) [11].

Other interactions of Sms

• Both compounds were good competitive inhibitors and poor substrates of spermine synthase, good substrates of cytosolic polyamine acetyltransferase, inactivators of S-adenosylmethionine decarboxylase and inhibitors of ornithine decarboxylase [10].

References