caa a22 4500 463186702 CHVBK 20180406164855.0 cr unu---uuuuu 170326e20070801xx s 000 0 eng 10.1007/s00726-007-0510-7 doi (NATIONALLICENCE)springer-10.1007/s00726-007-0510-7 The physiological role of biogenic amines redox reactions in mitochondria. New perspectives in cancer therapy [Elektronische Daten] [E. Agostinelli, G. Tempera, A. Molinari, M. Salvi, V. Battaglia, A. Toninello, G. Arancia] Summary.: In tumours, polyamines and amine oxidases increase as compared to normal tissues. Cytotoxicity induced by bovine serum amine oxidase (BSAO) and spermine is attributed to H2O2 and aldehydes produced by the reaction. Increasing the incubation temperature from 37 to 42 °C enhances cytotoxicity in cells exposed to spermine metabolites. The combination BSAO/spermine prevents tumour growth, particularly well if the enzyme has been conjugated with a biocompatible hydrogel polymer. Since the tumour cells release endogenous substrates of BSAO, the administration of spermine is not required. Combination with hyperthermia improves the cytocidal effect of polyamines oxidation products. Our findings show that multidrug resistant (MDR) cells are more sensitive to spermine metabolites than their wild-type counterparts, due to an increased mitochondrial activity which induces the generation of intracellular ROS prior to the onset of mitochondrial permeability transition (MPT). It makes this new approach attractive, since the development of MDR is one of the major problems of conventional cancer therapy. Springer-Verlag, 2007 Keywords: Polyamines - Amine oxidase - Reactive oxygen species - Multidrug resistance - Mitochondria - Cancer nationallicence AdNT : adenine nucleotide translocase nationallicence ADR : adriamycin resistant nationallicence ALDH : aldehyde dehydrogenase nationallicence AOs : amine oxidases nationallicence BSAO : bovine serum amine oxidase nationallicence CHO : Chinese hamster ovary nationallicence Cu-AOs : copper containing amine oxidases nationallicence DX : doxorubicin nationallicence ΔΨ : membrane potential nationallicence FAD-AO : flavin-adenin-dinucleotide dependent AO nationallicence MAO : monoamine oxidase nationallicence MDR : multidrug-resistant nationallicence METC : mitochondrial electron transport chain nationallicence MPT : mitochondrial permeability transition nationallicence Nγ : guanidine group of agmatine nationallicence ODC : ornithine decarboxylase nationallicence PAOs : FAD polyamine oxidase (not a CuAO) nationallicence PEG : polyethylene glycol nationallicence P-gp : P-glycoprotein nationallicence Pi : inorganic phosphate nationallicence RLM : rat liver mitochondria nationallicence ROS : reactive oxygen species nationallicence SEM : scanning electron microscopy nationallicence SH : thiol groups nationallicence SMO : spermine oxidase nationallicence SOD : superoxide dismutase nationallicence SSAOs : semicarbazide-sensitive amine oxidases nationallicence TEM : transmission electron microscopy nationallicence TPQ : 2,4,5-trihydroxyphenylalanine quinone nationallicence VDAC : voltage-dependent anion channel nationallicence WR-1065 : aminothiol N-(2-mercaptoethyl)-1,3-propanediamine nationallicence WT : wild-type nationallicence Agostinelli E. Department of Biochemical Sciences "A. Rossi Fanelli”, Institute of Molecular Biology and Pathology, University of Rome "La Sapienza” and CNR, Rome, Italy aut Tempera G. Department of Biochemical Sciences "A. Rossi Fanelli”, Institute of Molecular Biology and Pathology, University of Rome "La Sapienza” and CNR, Rome, Italy aut Molinari A. Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy aut Salvi M. Department of Biological Chemistry, University of Padua, Institute of Neurosciences of the C.N.R., Padua, Italy aut Battaglia V. Department of Biological Chemistry, University of Padua, Institute of Neurosciences of the C.N.R., Padua, Italy aut Toninello A. Department of Biological Chemistry, University of Padua, Institute of Neurosciences of the C.N.R., Padua, Italy aut Arancia G. Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy aut Amino Acids Springer-Verlag 33/2(2007-08-01), 175-187 0939-4451 33:2<175 2007 33 726 https://doi.org/10.1007/s00726-007-0510-7 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-007-0510-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Agostinelli E. Department of Biochemical Sciences "A. Rossi Fanelli”, Institute of Molecular Biology and Pathology, University of Rome "La Sapienza” and CNR, Rome, Italy aut NATIONALLICENCE 700 1- Tempera G. Department of Biochemical Sciences "A. Rossi Fanelli”, Institute of Molecular Biology and Pathology, University of Rome "La Sapienza” and CNR, Rome, Italy aut NATIONALLICENCE 700 1- Molinari A. Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy aut NATIONALLICENCE 700 1- Salvi M. Department of Biological Chemistry, University of Padua, Institute of Neurosciences of the C.N.R., Padua, Italy aut NATIONALLICENCE 700 1- Battaglia V. Department of Biological Chemistry, University of Padua, Institute of Neurosciences of the C.N.R., Padua, Italy aut NATIONALLICENCE 700 1- Toninello A. Department of Biological Chemistry, University of Padua, Institute of Neurosciences of the C.N.R., Padua, Italy aut NATIONALLICENCE 700 1- Arancia G. Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 33/2(2007-08-01), 175-187 0939-4451 33:2<175 2007 33 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer