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Transverse acoustic modes of biogenic and alpha,omega-polyamines: a study by inelastic neutron scattering and Raman spectroscopies coupled to DFT calculations.

A complete analysis of the transverse acoustic modes (TAMs) for the homologous series of alpha,omega-diamines (H2N(CH2)nNH2) (n = 2-10, n = 12) as well as for the biogenic polyamines spermidine and spermine was undertaken, by Raman and inelastic neutron scattering (INS) spectroscopies combined with density functional theory (DFT) calculations. A complete assignment of the whole set of TAMs was carried out, for both the undeuterated and N-deuterated species. 1,2-Diaminoethane was found to display exceptional behavior, probably due to the formation of dimers in the solid state. An n-even/n-odd dependence of the low frequency INS pattern was observed for these polyamines. The very good accordance between their INS experimental TAMs and the ones previously reported for the corresponding n-alkanes suggest a close conformational similarity between these systems.

Algorithms↗

[Regulation of polyamine and cancer].

This review describes my work in the field of polyamine research for the last 35 years. My research started with developing the improved synthesis of decarboxylated S-adenosylmethionine and then moved to the purification of spermidine synthase from rat prostate. I also took considerable efforts to find the synthetic procedure for various polyamines with high yield in order to prepare (15)N-labeled polyamines. On the basis of these methodological work, I searched for the inhibitor of spermidine synthase and found trans-4-methylcyclohexylamine (MCHA), the most effective one at the present time. I also developed a new analytical method for polyamines using stable isotope and ionspray ionization mass spectrometry (IS-MS). Based on these studies I examined the role of polyamines in liver regeneration and found that oral administration of MCHA effectively changed the concentration of polyamines and inhibited the hepatic growth. I also found the close relationship between the concentration ratio of spermidine to spermine and the extent of liver regeneration. These results may shed new light on the control of cell growth by polyamine in vivo.

Animals↗

[Alteration of biogenic amines, serotonin, histamine and polyamines, in cases of diarrhea induced by various cathartics (author's transl)].

Effects of various cathartics on charcoal transport, permeability of blood vessels and biogenic amines (serotonin (5-HT), histamine (His), polyamines) in the small intestine of mice were investigated. Diarrhea was induced in mice by oral administration of magnesium sulfate, mannitol, dioctyl sodium sulfosuccinate (DSS), castor oil and pilocarpine. In diarrhea following ingestion of magnesium sulfate and mannitol, vascular permeability in the intestinal membrane accompanied release of His from the small intestine, but such was not so when diarrhea was induced by DSS and castor oil. In diarrhea induced by various cathartics, 5-HT and His were apparently not related to intestinal motility. Thus, alteration in polyamine metabolism in the small intestine may exert an influence on transport of substances in cases of diarrhea in mice.

Animals↗

Polyamines. An overview.

The polyamines spermine, spermidine, and putrescine are small organic molecules one or more of which are present in all living organisms. Many natural products contain polyamine residues. Polyamines are synthesized by a highly regulated pathway from arginine or ornithine and also can be transported in and out of cells. Polyamines are degraded to a variety of compounds the functions of which are largely unknown. Polyamines influence the transcriptional and translational stages of protein synthesis, stabilize membranes, and, in mammalian systems, modulate neurophysiological functions and may act as intracellular messengers. However, at the molecular level the mode of action of the polyamines is largely unknown.

Animals↗

Excretion of acetylated and free polyamines by polyamine depleted Chinese hamster ovary cells.

1. Cultured Chinese hamster ovary cells (CHO) and their ornithine decarboxylase deficient mutant cells (C55.7) were found to excrete small amounts of N8-acetylspermidine and free polyamines, putrescine and spermidine into the culture medium. 2. The concentration of N8-acetylspermidine in the control cells was 2-3% of that of spermidine. In the medium, however, the amount of N8-acetylspermidine was about 2-fold that of spermidine and 2- to 3-fold higher than the intracellular amount. N1-acetylspermidine or acetylated spermine were never detected in the cells or in the media. 3. Confluent CHO cells treated with 2 mM difluoromethylornithine stopped the excretion when the intracellular spermidine concentration had decreased to 20% of control while there was no decrease in spermine concentration. At low cell density, neither polyamine depleted CHO cells nor the C55.7 cells excreted any polyamines into the culture media.

Animals↗

[Polyamine transport in Escherichia coli and eukaryotic cells].

The polyamine content in cells is regulated by both polyamine biosynthesis and its transport. We recently obtained and characterized three clones of polyamine transport genes (pPT104, pPT79 and pPT71) in Escherichia coli. The system encoded by pPT104 was the spermidine-preferential uptake system and that encoded by pPT79 the putrescine-specific uptake system. Furthermore, these two systems were ABC (ATP binding cassette) transporters consisting of four kinds of proteins: pPT104 clone encoded PotA, -B, -C, and -D proteins and pPT79 clone encoded PotF, -G, -H, and I proteins. PotD and -F proteins were periplasmic substrate binding proteins and PotA and -G proteins membrane associated proteins having the nucleotide binding site. PotB and -C proteins, and PotH and -I proteins were transmembrane proteins probably forming channels for spermidine and putrescine, respectively. Their amino acid sequences in the corresponding proteins were similar to each other. The functions of PotA and -D proteins in the spermidine-preferential uptake system encoded by pPT104 clone were studied in detail through a combined biochemical and genetic approach. In contrast, the putrescine transport system encoded by pPT71 consisted of one membrane protein (PotE protein) having twelve transmembrane segments, and was active in both the uptake and excretion of putrescine. The uptake was dependent on the membrane potential, and the excretion was due to the exchange reaction between putrescine and ornithine. In mouse mammary carcinoma FM3A cells, it was shown that the antizyme, which negatively regulates the amount of ornithine decarboxylase, also negatively regulates the activity of polyamine transport.

Amino Acid Sequence↗