Ferricytochrome c Directly Oxidizes Aminoacetone to Methylglyoxal, a Catabolite Accumulated in Carbonyl Stress

Ferricytochrome c Directly Oxidizes Aminoacetone to Methylglyoxal, a Catabolite Accumulated in Carbonyl Stress

Autor Sartori, Adriano Autor UNIFESP Google Scholar
Mano, Camila M. Google Scholar
Mantovani, Mariana C. Autor UNIFESP Google Scholar
Dyszy, Fabio H. Google Scholar
Massari, Julio Google Scholar
Tokikawa, Rita Google Scholar
Nascimento, Otaciro R. Google Scholar
Nantes, Iseli L. Google Scholar
Bechara, Etelvino José Henriques Autor UNIFESP Google Scholar
Instituição Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Universidade Federal do ABC (UFABC)
Resumo Age-related diseases are associated with increased production of reactive oxygen and carbonyl species such as methylglyoxal. Aminoacetone, a putative threonine catabolite, is reportedly known to undergo metal-catalyzed oxidation to methylglyoxal, NH4+ ion, and H2O2 coupled with (i) permeabilization of rat liver mitochondria, and (ii) apoptosis of insulin-producing cells. Oxidation of aminoacetone to methylglyoxal is now shown to be accelerated by ferricytochrome c, a reaction initiated by one-electron reduction of ferricytochrome c by aminoacetone without amino acid modifications. the participation of O-2(center dot-) and HO center dot radical intermediates is demonstrated by the inhibitory effect of added superoxide dismutase and Electron Paramagnetic Resonance spin-trapping experiments with 5,5'-dimethyl-1-pyrroline-N-oxide. We hypothesize that two consecutive one-electron transfers from aminoacetone (E-0 values = -0.51 and -1.0 V) to ferricytochrome c (E-0 = 0.26 V) may lead to aminoacetone enoyl radical and, subsequently, imine aminoacetone, whose hydrolysis yields methylglyoxal and NH4+ ion. in the presence of oxygen, aminoacetone enoyl and O-2(center dot-) radicals propagate aminoacetone oxidation to methylglyoxal and H2O2. These data endorse the hypothesis that aminoacetone, putatively accumulated in diabetes, may directly reduce ferricyt c yielding methylglyoxal and free radicals, thereby triggering redox imbalance and adverse mitochondrial responses.
Idioma Inglês
Financiador Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
INCT Processos Redox em Biomedicina (Brazil)
Data 2013-03-06
Publicado em Plos One. San Francisco: Public Library Science, v. 8, n. 3, 13 p., 2013.
ISSN 1932-6203 (Sherpa/Romeo, fator de impacto)
Editor Public Library Science
Extensão 13
Fonte http://dx.doi.org/10.1371/journal.pone.0057790
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000316936100046
URI http://repositorio.unifesp.br/handle/11600/36080

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