Carbonylated Proteins and Their Implication in Physiology and Pathology

Levine, Rodney L.; Stadtman, Earl R.

doi:10.1002/0471973122.ch5

Cited by 16 publications

(17 citation statements)

References 430 publications

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“…MsrA activity was not affected by I/R (Fig. 7), indicating that this enzyme is relatively resistant to oxidative inactivation, perhaps in part because it is not metal dependent and thus lacks binding sites for metal-catalyzed oxidation (18).…”

Section: Resultsmentioning

confidence: 98%

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Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury

Zhao

Sun

Deschamps

et al. 2011

American Journal of Physiology-Heart and Circulatory Physiology

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Section: Resultsmentioning

confidence: 98%

“…ROS formed during I/R, can be measured in the perfusate effluent (28,48), and can damage macromolecules, usually with loss of function (18). MsrA activity was not affected by I/R (Fig.…”

Section: Resultsmentioning

confidence: 99%

Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury

Zhao

Sun

Deschamps

et al. 2011

American Journal of Physiology-Heart and Circulatory Physiology

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“…39 As a result, we can postulate that the increased levels of MDA in the body cause specific damage to macromolecules, leading to structural and functional changes to cell components, further promoting oxidative stress and inflammation and accelerating the generation of MDA, a cyclical process that underlies the progressive decline in physiologic function and the development of diseases. In fact, some studies have illustrated a direct risk role of MDA in a series of pathophysiologic processes, 28,30,40,41 and some potential antioxidant agents, including pyridoxamine and melatonin, perform their roles in the body by acting as MDA …”

Section: Discussionmentioning

confidence: 99%

Association Between Age-Related Decline of Kidney Function and Plasma Malondialdehyde

Chen²,

Hu³

et al. 2012

Rejuvenation Research

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Oxidative stress is a key factor linked renal function decline with age. However, there is still no large cohort study exploring the potential role of oxidative stress in mild insufficiency of kidney function (MIKF) and chronic kidney disease (CKD) after adjusting for confounding factors. This study tested the hypothesis that oxidative stress, indicated by plasma malondialdehyde (MDA), is associated with the prevalence of MIKF and CKD after controlling the effects of confounding factors. Plasma levels of MDA and serum levels of fasting glucose, cholesterol, triglycerides, creatinine, alanine aminotransferase, and aspartate aminotransferase were analyzed from 2,169 Chinese Han adults. A questionnaire and physical examination were performed to identify and suspect risk factors of renal function decline with age. Kidney function, as indicated by estimated glomerular filtration rate, showed a significant decline with age in both male and female. Although the association between age and plasma MDA levels was nonlinear, MDA was negatively related to kidney function. The multivariate-adjusted odds ratios showed that plasma MDA had a significantly graded relation to the prevalence of MIKF and CKD with or without adjustment for covariates. By comparison with the lowest quartile, individuals with the highest quartile of MDA level had a 99% and 223% increased risk of developing MIKF and CKD, respectively. Further results from multiinteraction analysis demonstrated that plasma MDA may be the mediator linking different covariates with renal function decline. The most striking finding of this study was that oxidative stress, as indicated by plasma MDA levels, is associated with the prevalence of MIKF and/or CKD. Although imposing an increasing burden on the kidney and/or promoting a cyclical process of oxidative stress in the body, high levels of MDA in plasma may link the decline of kidney function with age.

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“…Basically, the answer to this question requires identification of a specific carbonylated protein and a positive correlation between altered function of this protein and development of diseases. Increased levels of protein car-bonyls have been detected in a large variety of pathological states occurring in humans, thus suggesting their potential causative role in disease pathogenesis [7,18,19,89,[103][104][105].…”

Section: Is Protein Carbonylation An Early Event Of Cellular Dysfunctmentioning

confidence: 99%

“…Protein carbonylation is the most widely used biomarker for oxidative damage to proteins, and reflects cellular damage induced by multiple forms of ROS [7,10,[16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Protein carbonylation, cellular dysfunction, and disease progression

Dalle‐Donne

Aldini

Colombo

et al. 2006

Journal of Cellular and Molecular Medicine

728

545

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Carbonylation of proteins is an irreversible oxidative damage, often leading to a loss of protein function, which is considered a widespread indicator of severe oxidative damage and disease-derived protein dysfunction. Whereas moderately carbonylated proteins are degraded by the proteasomal system, heavily carbonylated proteins tend to form high-molecular-weight aggregates that are resistant to degradation and accumulate as damaged or unfolded proteins. Such aggregates of carbonylated proteins can inhibit proteasome activity. A large number of neurodegenerative diseases are directly associated with the accumulation of proteolysis-resistant aggregates of carbonylated proteins in tissues. Identification of specific carbonylated protein(s) functionally impaired and development of selective carbonyl blockers should lead to the definitive assessment of the causative, correlative or consequential role of protein carbonylation in disease onset and/or progression, possibly providing new therapeutic aproaches.

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Carbonylated Proteins and Their Implication in Physiology and Pathology

Cited by 16 publications

References 430 publications

Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury

Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury

Association Between Age-Related Decline of Kidney Function and Plasma Malondialdehyde

Protein carbonylation, cellular dysfunction, and disease progression

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