Carbonic Anhydrase III. Oxidative modification in vivo and loss of phosphatase activity during aging
MetadataShow full item record
Oxidative modification of DNA, lipids, and proteins occurs as a consequence of reaction with free radicals and activated oxygen. Oxidative modification of total cellular proteins has been described under many pathologic and experimental conditions, but no specific proteins have been identified as in
vivo targets for oxidative modification. Utilizing an immunochemical method for detection of oxidatively modified proteins, we identified a protein in rat liver that was highly oxidized. It was purified to homogeneity and identified as carbonic anhydrase, isozyme III. Its characteristics match those previously described for a protein that was lost during aging of the rat, senescence marker protein-1. Carbonic anhydrase III was purified from rats aged 2, 10, and 18 months, and the proteins were characterized. All three preparations were highly oxidatively modified as assessed by their carbonyl content. The enzyme has three known catalytic activities, and the specific activities for carbon dioxide hydration and for ester hydrolysis decreased during aging by Graphic30%. However, the third activity, that of a phosphatase, was virtually lost during aging. While the physiologic role of carbonic anhydrase III is unknown, we suggest that it functions in an oxidizing environment, which leads to its own oxidative modification.
Is part ofJournal of Biological Chemistry, 1995, Vol. 270, núm. 24, p. 14742-14747
Showing items related by title, author, creator and subject.
Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage Irazusta, Verónica Patricia; Obis Monné, Èlia; Moreno Cermeño, Armando J.; Cabiscol Català, Elisa; Ros Salvador, Joaquim; Tamarit Sumalla, Jordi (Elsevier, 2010)Iron overload is involved in several pathological conditions, including Friedreich ataxia, a disease caused by decreased expression of the mitochondrial protein frataxin. In a previous study, we identified 14 proteins ...
Sir2 is induced by oxidative stress in a yeast model of Huntington disease and its activation reduces protein aggregation Sorolla Bardají, Maria Alba; Nierga, Clara; Rodríguez Colman, Maria José; Reverter Branchat, Gemma; Arenas, Alicia; Tamarit Sumalla, Jordi; Ros Salvador, Joaquim; Cabiscol Català, Elisa (Elsevier, 2011)Huntington disease (HD) is a neurodegenerative disorder caused by expansion of CAG trinucleotide repeats, leading to an elongated polyglutamine sequence (polyQ) in the huntingtin protein. Misfolding of mutant polyQ ...
Frataxin depletion in yeast triggers up-regulation of iron transport systems before affecting iron-sulfur enzyme activities Moreno Cermeño, Armando J.; Obis Monné, Èlia; Bellí i Martínez, Gemma; Cabiscol Català, Elisa; Ros Salvador, Joaquim; Tamarit Sumalla, Jordi (The American Society for Biochemistry and Molecular Biology, 2010)The primary function of frataxin, a mitochondrial protein involved in iron homeostasis, remains controversial. Using a yeast model of conditional expression of the frataxin homologue YFH1, we analyzed the primary effects ...