tailieunhanh - Báo cáo khoa học: Glycation damage targets glutamate dehydrogenase in the rat liver mitochondrial matrix during aging

Aging is accompanied by gradual cellular dysfunction associated with an accumulation of damaged proteins, particularly via oxidative processes. This cellular dysfunction has been attributed, at least in part, to impair-ment of mitochondrial function as this organelle is both a major source of oxidants and a target for their damaging effects, which can result in a reduction of energy production, thereby compromising cell function. | ỊFEBS Journal Glycation damage targets glutamate dehydrogenase in the rat liver mitochondrial matrix during aging Maud Hamelin Jean Mary Michal Vostry Bertrand Friguet and Hilaire Bakala Laboratoire de Biologie et Biochimie Cellulaire du Vieillissement Universite Paris 7-Denis Diderot France Keywords aging glycation liver mitochondria proteomics urea cycle enzymes Correspondence H. Bakala Laboratoire de Biologie et Biochimie Cellulaire du Vieillissement EA3106 IFR117 Universite Paris 7-Denis Diderot 2 place Jussieu 75251 Paris Cedex 05 France Fax 33 1 44 27 39 25 Tel 33 1 44 27 82 27 E-mail bakala@ These authors contributed equally to this work Received 22 May 2007 revised 21 September 2007 accepted 25 September 2007 doi Aging is accompanied by gradual cellular dysfunction associated with an accumulation of damaged proteins particularly via oxidative processes. This cellular dysfunction has been attributed at least in part to impairment of mitochondrial function as this organelle is both a major source of oxidants and a target for their damaging effects which can result in a reduction of energy production thereby compromising cell function. In the present study we observed a significant decrease in the respiratory activity of rat liver mitochondria with aging and an increase in the advanced glycation endproduct-modified protein level in the mitochondrial matrix. Western blot analysis of the glycated protein pattern after 2D electrophoresis revealed that only a restricted set of proteins was modified. Within this set we identified by mass spectrometry proteins connected with the urea cycle and especially glutamate dehydrogenase which is markedly modified in older animals. Moreover mitochondrial matrix extracts exhibited a significant decrease in glutamate dehydrogenase activity and altered allosteric regulation with age. Therefore the effect of the glycating agent methylglyoxal on glutamate dehydrogenase activity and

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