Formation of S-(carboxymethyl)-cysteine in rat liver mitochondrial proteins: effects of caloric and methionine restriction
Issue date
2013Author
Cacabelos Barral, Daniel
Caro, Pilar
Gómez, José
Barja, Gustavo
Suggested citation
Naudí i Farré, Alba;
Jové Font, Mariona;
Cacabelos Barral, Daniel;
Ayala Jové, Ma. Victoria (Maria Victoria);
Cabré Cucó, Rosanna;
Caro, Pilar;
...
Pamplona Gras, Reinald.
(2013)
.
Formation of S-(carboxymethyl)-cysteine in rat liver mitochondrial proteins: effects of caloric and methionine restriction.
Amino Acids, 2013, vol. 44, núm. 2, p. 361-371.
https://doi.org/10.1007/s00726-012-1339-2.
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Show full item recordAbstract
Maillard reaction contributes to the chemical
modification and cross-linking of proteins. This process
plays a significant role in the aging process and determination
of animal longevity. Oxidative conditions promote
the Maillard reaction. Mitochondria are the primary site of
oxidants due to the reactive molecular species production.
Mitochondrial proteome cysteine residues are targets of
oxidative attack due to their specific chemistry and localization.
Their chemical, non-enzymatic modification leads
to dysfunctional proteins, which entail cellular senescence
and organismal aging. Previous studies have consistently
shown that caloric and methionine restrictions, nutritional
interventions that increase longevity, decrease the rate of
mitochondrial oxidant production and the physiological
steady-state levels of markers of oxidative damage to
macromolecules. In this scenario, we have detected
S-(carboxymethyl)-cysteine (CMC) as a new irreversible
chemical modification in mitochondrial proteins. CMC
content in mitochondrial proteins significantly correlated
with that of the lysine-derived analog Ne-(carboxymethyl)-
lysine. The concentration of CMC is, however, one order of
magnitude lower compared with CML likely due in part to
the lower content of cysteine with respect to lysine of the
mitochondrial proteome. CMC concentrations decreases in
liver mitochondrial proteins of rats subjected to 8.5 and 25 % caloric restriction, as well as in 40 and 80 %
methionine restriction. This is associated with a concomitant
and significant increase in the protein content of
sulfhydryl groups. Data presented here evidence that CMC,
a marker of Cys-AGE formation, could be candidate as a
biomarker of mitochondrial damage during aging.