Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.

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) permeabilizatio...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Adriano Sartori, Camila M Mano, Mariana C Mantovani, Fábio H Dyszy, Júlio Massari, Rita Tokikawa, Otaciro R Nascimento, Iseli L Nantes, Etelvino J H Bechara
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b6839cca912d41ed8682441244502df5
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:b6839cca912d41ed8682441244502df5
record_format	dspace
spelling	oai:doaj.org-article:b6839cca912d41ed8682441244502df52021-11-18T07:54:40ZFerricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.1932-620310.1371/journal.pone.0057790https://doaj.org/article/b6839cca912d41ed8682441244502df52013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23483930/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Age-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 O2(•-) and HO (•) 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 (E0 values = -0.51 and -1.0 V) to ferricytochrome c (E0 = 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 O2(•-) 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.Adriano SartoriCamila M ManoMariana C MantovaniFábio H DyszyJúlio MassariRita TokikawaOtaciro R NascimentoIseli L NantesEtelvino J H BecharaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e57790 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Adriano Sartori Camila M Mano Mariana C Mantovani Fábio H Dyszy Júlio Massari Rita Tokikawa Otaciro R Nascimento Iseli L Nantes Etelvino J H Bechara Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
description	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 O2(•-) and HO (•) 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 (E0 values = -0.51 and -1.0 V) to ferricytochrome c (E0 = 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 O2(•-) 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.
format	article
author	Adriano Sartori Camila M Mano Mariana C Mantovani Fábio H Dyszy Júlio Massari Rita Tokikawa Otaciro R Nascimento Iseli L Nantes Etelvino J H Bechara
author_facet	Adriano Sartori Camila M Mano Mariana C Mantovani Fábio H Dyszy Júlio Massari Rita Tokikawa Otaciro R Nascimento Iseli L Nantes Etelvino J H Bechara
author_sort	Adriano Sartori
title	Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
title_short	Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
title_full	Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
title_fullStr	Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
title_full_unstemmed	Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
title_sort	ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/b6839cca912d41ed8682441244502df5
work_keys_str_mv	AT adrianosartori ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT camilammano ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT marianacmantovani ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT fabiohdyszy ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT juliomassari ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT ritatokikawa ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT otacirornascimento ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT iselilnantes ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress AT etelvinojhbechara ferricytochromecdirectlyoxidizesaminoacetonetomethylglyoxalacataboliteaccumulatedincarbonylstress
_version_	1718422794632429568

Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.

Ejemplares similares