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Title: Physiological importance of polyamines
Authors: Lenis, Yasser Y.
Elmetwally, Mohammed A.
Maldonado-Estrada, Juan G.
Bazer, Fuller W.
Issue Date: 2017
Citation: Lenis, Y. Y., Elmetwally, M. A., Maldonado-Estrada, J. G., & Bazer, F. W. (2017). Physiological importance of polyamines. Zygote, 25(3), 244-255. doi:10.1017/S0967199417000120
Series/Report no.: Zygote;Vol., 25, No. 3, Jun. 1 2017, páginas 244-255
Abstract: Polyamines are polycationic molecules that contain two or more amino groups (-NH3 +) and are present in all eukaryotic and prokaryotic cells. Polyamines are synthesized from arginine, ornithine, and proline, and from methionine as the methyl-group donor. In the traditional pathway for polyamine synthesis, arginase converts arginine into ornithine, which is decarboxylated by ornithine decarboxylase (ODC1) to generate putrescine. The latter is converted to spermidine and spermine. Recent studies have indicated the existence of 'non-classical pathways' for the generation of putrescine from arginine and proline in animal cells. Specifically, arginine decarboxylase (ADC) catalyzes the conversion of arginine into agmatine, which is hydrolyzed by agmatinase (AGMAT) to form putrescine. Additionally, proline is oxidized by proline oxidase to yield pyrroline-5-carboxylate, which undergoes transamination with glutamate to produce ornithine for decarboxylation by ODC1. Intracellular production of polyamines is controlled by antizymes binding to and inactivating ODC1. Polyamines exert effects that include stimulation of cell division and proliferation, gene expression for the survival of cells, DNA and protein synthesis, regulation of apoptosis, oxidative stress, angiogenesis, and cell-cell communication activity. Accordingly, polyamines are essential for early embryonic development and successful pregnancy outcome in mammals. In this paper the main concepts on the history, structure and molecular pathways of polyamines as well as their physiological role on angiogenesis, and reproductive physiology are reviewed. © Copyright Cambridge University Press 2017.
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