Polyamines participate in the processes of cell growth and development. The degradation branch of their metabolism involves amine oxidases. The oxidation of spermine, spermidine and putrescine releases hydrogen peroxide and the corresponding aminoaldehyde. Polyamine-derived aminoaldehydes have been found to be cytotoxic, and they represent the subject of this review. 3-aminopropanal disrupts the lysosomal membrane and triggers apoptosis or necrosis in the damaged cells. It is implicated in the pathogenesis of cerebral ischemia. Furthermore, 3-aminopropanal yields acrolein through the elimination of ammonia. This reactive aldehyde is also generated by the decomposition of aminoaldehydes produced in the reaction of serum amine oxidase with spermidine or spermine. In addition, acrolein is a common environmental pollutant. It causes covalent modifications of proteins, including carbonylation, the production of Michael-type adducts and cross-linking, and it has been associated with inflammation-related diseases. APAL and acrolein are detoxified by aldehyde dehydrogenases and other mechanisms. High-performance liquid chromatography, immunochemistry and mass spectrometry have been largely used to analyze the presence of polyamine-derived aminoaldehydes and protein modifications elicited by their effect. However, the main and still open challenge is to find clues for discovering clear linkages between aldehyde-induced modifications of specific proteins and the development of various diseases.

• Keywords
• 3-aminopropanal, Michael adduct, Schiff base, acrolein, aldehyde dehydrogenase, amine oxidase, aminoaldehyde, cytotoxicity, glutathione, protein modification,
• MeSH
• Acrolein * pharmacology   MeSH
• Aldehydes pharmacology   MeSH
• Polyamines * MeSH
• Spermidine pharmacology   MeSH
• Spermine pharmacology   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH
• Names of Substances
• 3-aminopropionaldehyde MeSH Browser
• Acrolein * MeSH
• Aldehydes MeSH
• Polyamines * MeSH
• Spermidine MeSH
• Spermine MeSH

Soil arbuscular mycorrhizal fungi (AMF) enhance the tolerance of plants against soil moisture deficit stress (SMDS), but the underlying mechanisms are still not fully understood. Polyamines (PAs) as low-molecular-weight, aliphatic polycations have strong roles in abiotic stress tolerance of plants. We aimed to investigate the effect of AMF (Funneliformis mosseae) inoculation on PAs, PA precursors, activities of PA synthases and degrading enzymes, and concentration of reactive oxygen species in the roots of trifoliate orange (Poncirus trifoliata) subjected to 15 days of SMDS. Leaf water potential and total chlorophyll levels were comparatively higher in AMF-inoculated than in non-AMF-treated plants exposed to SMDS. Mycorrhizal plants recorded a significantly higher concentration of precursors of PA synthesis such as L-ornithine, agmatine, and S-adenosyl methionine, besides higher putrescine and cadaverine and lower spermidine during the 15 days of SMDS. AMF colonization raised the PA synthase (arginine decarboxylase, ornithine decarboxylase, spermidine synthase, and spermine synthase) activities and PA-degrading enzymes (copper-containing diamine oxidase and FAD-containing polyamine oxidase) in response to SMDS. However, mycorrhizal plants showed a relatively lower degree of membrane lipid peroxidation, superoxide anion free radical, and hydrogen peroxide than non-mycorrhizal plants, whereas the difference between them increased linearly up to 15 days of SMDS. Our study concluded that AMF regulated PA homeostasis in roots of trifoliate orange to tolerate SMDS.

• Keywords
• Poncirus trifoliata, citrus, mycorrhiza, polyamine, water deficit,
• Publication type
• Journal Article MeSH

This review reports on inhibitors of copper-containing amine oxidases and flavoprotein polyamine oxidases, which are structurally based on diamines. In the introduction, basic characteristics and classification of amine oxidases are described together with the significance of their synthetic inhibitors. The following text is divided into several chapters, which deal with diaminoketones, aza-diamines, unsaturated diamine analogs and diamines with heterocyclic substituents. Then it continues with diamine- and agmatine-based inhibitors of polyamine oxidases. Each chapter gives detailed information on the inhibition mode, potency and structural relationships. The conclusion points out possible roles of mechanism-based inhibitors of amine oxidases in physiological and medicinal research.

• MeSH
• Agmatine chemistry   pharmacology   MeSH
• Enzyme Activation drug effects   physiology   MeSH
• Diamines chemistry   pharmacology   MeSH
• Amine Oxidase (Copper-Containing) antagonists & inhibitors   metabolism   MeSH
• Enzyme Inhibitors chemistry   pharmacology   MeSH
• Ketones chemistry   pharmacology   MeSH
• Humans MeSH
• Molecular Structure MeSH
• Oxidoreductases Acting on CH-NH Group Donors antagonists & inhibitors   metabolism   MeSH
• Polyamine Oxidase MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH
• Names of Substances
• Agmatine MeSH
• Diamines MeSH
• Amine Oxidase (Copper-Containing) MeSH
• Enzyme Inhibitors MeSH
• Ketones MeSH
• Oxidoreductases Acting on CH-NH Group Donors MeSH