caa a22 4500 445376422 CHVBK 20180317143004.0 cr unu---uuuuu 170323e20110701xx s 000 0 eng 10.1007/s00702-011-0611-z doi (NATIONALLICENCE)springer-10.1007/s00702-011-0611-z From caffeine to fish waste: amine compounds present in food and drugs and their interactions with primary amine oxidase [Elektronische Daten] [Aldo Olivieri, Daniel Rico, Zhied Khiari, Gary Henehan, Jeff O'Sullivan, Keith Tipton] Tissue bound primary amine oxidase (PrAO) and its circulating plasma-soluble form are involved, through their catalytic activity, in important cellular roles, including the adhesion of lymphocytes to endothelial cells during various inflammatory conditions, the regulation of cell growth and maturation, extracellular matrix deposition and maturation and glucose transport. PrAO catalyses the oxidative deamination of several xenobiotics and has been linked to vascular toxicity, due to the generation of cytotoxic aldehydes. In this study, a series of amines and aldehydes contained in food and drugs were tested via a high-throughput assay as potential substrates or inhibitors of bovine plasma PrAO. Although none of the compounds analyzed were found to be substrates for the enzyme, a series of molecules, including caffeine, the antidiabetics phenformin and tolbutamide and the antimicrobial pentamidine, were identified as PrAO inhibitors. Although the inhibition observed was in the millimolar and micromolar range, these data show that further work will be necessary to elucidate whether the interaction of ingested biogenic or xenobiotic amines with PrAO might adversely affect its biological roles. Springer-Verlag, 2011 Primary amine oxidase nationallicence Semicarbazide-sensitive amine oxidase nationallicence Xenobiotic(s) nationallicence Enzyme inhibition nationallicence PrAO : Primary amine oxidase nationallicence SSAO : Semicarbazide-sensitive amine oxidase nationallicence TPQ : 3,4,5-Trihydroxyphenylalanine quinone nationallicence DAO : Diamine oxidase nationallicence Olivieri Aldo School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland aut Rico Daniel Dublin Institute of Technology, School of Food Science and Environmental Health, Cathal Brugha Street, Dublin 1, Ireland aut Khiari Zhied Dublin Institute of Technology, School of Food Science and Environmental Health, Cathal Brugha Street, Dublin 1, Ireland aut Henehan Gary Dublin Institute of Technology, School of Food Science and Environmental Health, Cathal Brugha Street, Dublin 1, Ireland aut O'Sullivan Jeff Dublin Dental School and Hospital, Trinity College, Dublin 2, Ireland aut Tipton Keith School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland aut Journal of Neural Transmission Springer Vienna 118/7(2011-07-01), 1079-1089 0300-9564 118:7<1079 2011 118 702 https://doi.org/10.1007/s00702-011-0611-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00702-011-0611-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Olivieri Aldo School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland aut NATIONALLICENCE 700 1- Rico Daniel Dublin Institute of Technology, School of Food Science and Environmental Health, Cathal Brugha Street, Dublin 1, Ireland aut NATIONALLICENCE 700 1- Khiari Zhied Dublin Institute of Technology, School of Food Science and Environmental Health, Cathal Brugha Street, Dublin 1, Ireland aut NATIONALLICENCE 700 1- Henehan Gary Dublin Institute of Technology, School of Food Science and Environmental Health, Cathal Brugha Street, Dublin 1, Ireland aut NATIONALLICENCE 700 1- O'Sullivan Jeff Dublin Dental School and Hospital, Trinity College, Dublin 2, Ireland aut NATIONALLICENCE 700 1- Tipton Keith School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland aut NATIONALLICENCE 773 0- Journal of Neural Transmission Springer Vienna 118/7(2011-07-01), 1079-1089 0300-9564 118:7<1079 2011 118 702 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer