Oxidized protein degradation and repair in ageing and oxidative stress

Friguet, Bertrand

doi:10.1016/j.febslet.2006.03.028

Cited by 190 publications

(149 citation statements)

References 73 publications

(111 reference statements)

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“…Female Wistar rats have a median lifespan of 900 days (Koolhaas 2010), taken this into account the old rats we used paralleled to humans at the brink of retirement, about 65 years of age. Due to an imbalance between free-radical generation and their elimination, ROS accumulates and causes buildup of oxidative-modified proteins and a decline in cellular antioxidant defense (Harman 1981;Friguet 2006;Squier 2001). ROS formation is closely coupled to redox-active iron availability through the Haber-Weiss reaction (Leibovitz and Siegel 1980).…”

Section: Discussionmentioning

confidence: 99%

“…Changes characteristic for aging closely correlate with oxidation of cellular components and the accumulation of oxidized metabolic products (Friguet 2006;Harman 1956;Kregel and Zhang 2007;Petropoulos and Friguet 2006;Squier 2001). However, a direct causal link between reactive oxygen-derived species (ROS) and aging has yet to be established.…”

Section: Introductionmentioning

confidence: 99%

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Aging is an organ-specific process: changes in homeostasis of iron and redox proteins in the rat

Bulvik

Berenshtein

Konijn

et al. 2011

AGE

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Organ-specific changes of iron-and redoxrelated proteins occur with age in the rat. Ferritin, the major iron storage and detoxifying protein, as well as the proteins of the methionine-centered redox cycle (MCRC) were examined in old and young animals, and showed organ-dependent changes. In spleens and livers of aged rats, ferritin (protein) levels were greater than in young ones, and their iron saturation increased, rendering higher ferritin-bound iron (FtBI). Iron saturation of the ferritin molecule in the tongues and sternohyoids of old rats was lower but ferritin level was higher than in young rats, resulting in increased FtBI with age. Ferritin level in the esophagus of older rats was lower than in young rats but its molecular iron content higher thus the total FtBI remained the same. In the larynx, both ferritin and its iron content were the same in young and old animals. MCRC proteins were measured in livers and spleens only. With aging, methionine sulfoxide reductase A and B (MsrA and MsrB) levels in livers and spleens decreased. Thioredoxin1 (Trx) and Trx-reductase1 were elevated in old spleens, but reduced in livers. Aged spleens showed reduced Msr isozyme activity; but in the liver, its activity increased. mRNA changes with age were monitored and found to be organ specific. These organ-specific changes could reflect the different challenges and the selective pathways of each organ and its resultant capacity to cope with aging.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Aging is an organ-specific process: changes in homeostasis of iron and redox proteins in the rat

Bulvik

Berenshtein

Konijn

et al. 2011

AGE

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“…Although strong oxidation may cause irreversible damage to cellular function, some oxidative changes in the redox-sensitive proteins could be reduced by endogenous reductant enzyme. For example, the oxidation of key sulfur-containing amino acid residues, such as methionine and cysteine, could be regulated by endogenous reductant enzyme (Stadtman & Levine, 2003;Friguet, 2006). Therefore, this reduction of sulfur-containing amino acid residues oxidation may be beneficial for treating the dysfunction induced by oxidative inactivation of key macromolecules.…”

Section: Discussionmentioning

confidence: 99%

Reversal of aging‐associated hippocampal synaptic plasticity deficits by reductants via regulation of thiol redox and NMDA receptor function

Yang

Long

et al. 2010

Aging Cell

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SummaryDeficits in learning and memory accompanied by agerelated neurodegenerative diseases are closely related to the impairment of synaptic plasticity. In this study, we investigated the role of thiol redox status in the modulation of the N-methyl-D-aspartate receptor (NMDAR)-dependent long-term potentiation (LTP) in CA1 areas of hippocampal slices. Our results demonstrated that the impaired LTP induced by aging could be reversed by acute administration of reductants that can regulate thiol redox status directly, such as dithiothreitol or b-mercaptoethanol, but not by classical anti-oxidants such as vitamin C or trolox. This repair was mediated by the recruitment of aging-related deficits in NMDAR function induced by these reductants and was mimicked by glutathione, which can restore the age-associated alterations in endogenous thiol redox status. Moreover, antioxidant prevented but failed to reverse H 2 O 2 -induced impairment of NMDARmediated synaptic plasticity. These results indicate that the restoring of thiol redox status may be a more effective strategy than the scavenging of oxidants in the treatment of pre-existing oxidative injury in learning and memory.

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“…of oxygen radicals, decreased defenses against reactive oxygen species, or reduced capacity to degrade such proteins (70). Several groups have reported an increased content of oxidatively damaged proteins in aged rodent muscle (48,49) as well as of the chaperones, Hsp70 (48) and Hsp90 (18).…”

Section: Discussionmentioning

confidence: 99%

Muscle Wasting in Aged, Sarcopenic Rats Is Associated with Enhanced Activity of the Ubiquitin Proteasome Pathway

Altun

Besche

Overkleeft

et al. 2010

Journal of Biological Chemistry

197

155

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Among the hallmarks of aged organisms are an accumulation of misfolded proteins and a reduction in skeletal muscle mass ("sarcopenia"). We have examined the effects of aging and dietary restriction (which retards many age-related changes) on components of the ubiquitin proteasome system (UPS) in muscle. The hindlimb muscles of aged (30 months old) rats showed a marked loss of muscle mass and contained 2-3-fold higher levels of 26S proteasomes than those of adult (4 months old) controls. 26S proteasomes purified from muscles of aged and adult rats showed a similar capacity to degrade peptides, proteins, and an ubiquitylated substrate, but differed in levels of proteasome-associated proteins (e.g. the ubiquitin ligase E6AP and deubiquitylating enzyme USP14). Also, the activities of many other deubiquitylating enzymes were greatly enhanced in the aged muscles. Nevertheless, their content of polyubiquitylated proteins was higher than in adult animals. The aged muscles contained higher levels of the ubiquitin ligase CHIP, involved in eliminating misfolded proteins, and MuRF1, which ubiquitylates myofibrillar proteins. These muscles differed from ones rapidly atrophying due to disease, fasting, or disuse in that Atrogin-1/MAFbx expression was low and not inducible by glucocorticoids. Thus, the muscles of aged rats showed many adaptations indicating enhanced proteolysis by the UPS, which may enhance their capacity to eliminate misfolded proteins and seems to contribute to the sarcopenia. Accordingly, dietary restriction decreased or prevented the aging-associated increases in proteasomes and other UPS components and reduced muscle wasting.

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Oxidized protein degradation and repair in ageing and oxidative stress

Cited by 190 publications

References 73 publications

Aging is an organ-specific process: changes in homeostasis of iron and redox proteins in the rat

Aging is an organ-specific process: changes in homeostasis of iron and redox proteins in the rat

Reversal of aging‐associated hippocampal synaptic plasticity deficits by reductants via regulation of thiol redox and NMDA receptor function

Muscle Wasting in Aged, Sarcopenic Rats Is Associated with Enhanced Activity of the Ubiquitin Proteasome Pathway

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