Disease relevance of N-Acetylspermine

• The addition of N1-acetylspermine did not stimulate cell growth of a polyamine-requiring mutant of Escherichia coli MA261, although acetylspermine was accumulated in the cells [1].

High impact information on N-Acetylspermine

• It was demonstrated definitively that PAO oxidizes N1-acetylspermine to spermidine and 3-acetamidopropanal and that it also oxidizes N1-acetylspermidine to putrescine and 3-acetamidopropanal [2].
• The debenzylation reaction was optimal between pH 9 and 10, identical to the pH optimum for polyamine oxidase activity when N1-acetylspermine was used as the substrate [3].
• The recombinant protein was purified by affinity chromatography on guazatine-Sepharose 4B and was shown to be a flavoprotein able to oxidize Spm, norspermine, and N1-acetylspermine with a pH optimum at 8 [4].
• This ranking is identical to that reported for purified PAO and distinctly different from the recently identified spermine oxidase (SMO), which prefers spermine over N1-acetylspermine [5].
• These results show that N1-acetylspermine is not able to substitute for the unmodified polyamines in supporting growth and suggest that acetylation is a physiological response to convert excess polyamines to a physiologically inert form which is readily excreted [6].

Biological context of N-Acetylspermine

• Cell death in the presence of N1-acetylspermine, dialysate and peak II appears unrelated to the apoptotic process [7].
• In vitro manipulation of L1210 cell cycle kinetics with 4-amidinoindan-1-one 2'-amidinohydrazone, alpha-difluoromethylornithine and N1-acetylspermine [8].

Anatomical context of N-Acetylspermine

• In the absence of factors washable from ribosomes (FWR fraction), mono-acylated or di-acylated analogues of spermine stimulate the binding of AcPhe-tRNA to a lesser degree than spermine, in the order: N1-acetylspermine > N1,N12-diacetylspermine approximately = N1,N12-dipivaloylspermine [9].
• RESULTS: Our data show that dialysate, chromatographic peak II, and 2 x 10(-8)M N1-acetylspermine cause inhibition of chick embryo skin culture development [7].
• The Syrian hamster epididymis contains rather high levels of sym-homospermidine, N1-acetylspermidine and N1-acetylspermine in addition to the common polyamines putrescine, spermidine, and spermine [10].

Associations of N-Acetylspermine with other chemical compounds

• The enzyme catalysed the acetylation of spermidine, spermine, sym-norspermidine, sym-norspermine, N-(3-aminopropyl)-cadaverine, N1-acetylspermine, 3,3'-diamino-N-methyldipropylamine and 1,3-diaminopropane, but was inactive with putrescine, cadaverine, sym-homospermidine and N1-acetylspermidine [11].
• A second enzyme of polyamine back-conversion, murine polyamine oxidase (PAO), was found to be competitively inhibited by pentamidine, with a Ki of 7.6 microM when N-acetylspermine was the substrate [12].
• Biochemical characterization of Fms1 shows that it can oxidize spermine, N(1)-acetylspermine, N(1)-acetylspermidine, and N(8)-acetylspermidine, but not spermidine [13].
• The trichomonad polyamine oxidase required FAD as a cofactor and had an apparent K:(m) of 6.0 microM for N(1)-acetylspermine [14].
• Detectable levels of at least two of the monoacetylated polyamines were found in all breast cancers: N1-acetylspermidine was present in 51 (13.1 +/- 6.3), N8-acetylspermidine in 32 (0.6 +/- 0.1) and N1-acetylspermine in 28 tumours (1.2 +/- 0.3) [15].

Gene context of N-Acetylspermine

• Lysates of human PAO cDNA-transfected HEK-293 cells, but not vector-transfected cells, rapidly oxidized N1-acetylspermine to spermidine [5].

Analytical, diagnostic and therapeutic context of N-Acetylspermine

• A competitive ELISA system, intended for measuring DiAcSpm in solution, was constructed using this antibody preparation, with N-acetylspermine coupled to a synthetic peptide via N-(8-maleimidocapryloxy)-succinimide as a solid phase antigen [16].
• The following methods were used for the identification of N1-acetylspermine: (a) High-pressure liquid-chromatography of the non-derivatized amines on a reversed-phase column, using octane sulfonate for ion-pairing [17].

References