Protein Carbonylation

Suzuki, Yuichiro; Carini, Marina; Butterfield, D. Allan

doi:10.1089/ars.2009.2887

Cited by 342 publications

(211 citation statements)

References 28 publications

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“…The protein reservoir functions amid an environment which is constantly challenged by extrinsic stress factors (such as heat or oxidative stress insults) and intrinsic, potentially harmful agents. For instance, reactive oxygen species (ROS), which are natural by-products of mitochondrial oxidative phosphorylation, can carbonylate polypeptides, damaging them in an irreversible manner (Suzuki et al 2010). To fulfil the pivotal task of preserving the proteome integrity, evolution has invented elaborate mechanisms to remove polypeptides which have accumulated damage.…”

Section: Introductionmentioning

confidence: 99%

Small heat shock proteins in ageing and age-related diseases

Charmpilas

Kyriakakis

Tavernarakis

2017

Cell Stress and Chaperones

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Small heat shock proteins (sHSPs) are gatekeepers of cellular homeostasis across species, preserving proteome integrity under stressful conditions. Nonetheless, recent evidence suggests that sHSPs are more than molecular chaperones with merely auxiliary role. In contrast, sHSPs have emerged as central lifespan determinants, and their malfunction has been associated with the manifestation of neurological disorders, cardiovascular disease and cancer malignancies. In this review, we focus on the role of sHSPs in ageing and ageassociated diseases and highlight the most prominent paradigms, where impairment of sHSP function has been implicated in human pathology.

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Section: Introductionmentioning

confidence: 99%

Small heat shock proteins in ageing and age-related diseases

Charmpilas

Kyriakakis

Tavernarakis

2017

Cell Stress and Chaperones

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“…Oxidizing agents including endogenous ROS also modify cysteine residues and exert its action on proteins (Ansari et al, 2006;Forman et al, 2008;Mikkelsen and Wardman, 2003;Suzuki et al, 2010). Therefore, NO and oxidizing agents competitively share cysteine residues to exert their action, and it is highly possible that oxidizing agents affect S-nitrosylation mediated signaling pathways essential 6 for the potentiation of PF synapse and impair or occlude the potentiation.…”

Section: Introductionmentioning

confidence: 99%

Protein oxidation inhibits NO-mediated signaling pathway for synaptic plasticity

Kakizawa

Shibazaki

Mori

2012

Neurobiology of Aging

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Oxidative stress is a primary factor inducing brain dysfunction in aged animals.However, how oxidation affects brain function is not fully understood. Here we show that oxidation inhibits signaling pathways essential for synaptic plasticities in the cerebellum. We first revealed that nitric oxide (NO)-dependent plasticities at parallel fiber-Purkinje cell synapse (PF synapse) were impaired in the cerebellar slices from aged mice, suggesting possible inhibitory action of protein oxidation by endogenous reactive oxygen species. PF-synaptic plasticities were also blocked in the cerebellar slices from young mice preincubated with oxidizing agents or thiol blocker. Because the treatment of the slices with the oxidizing agent did not affect basic electrophysiological properties of PF-EPSC and did not occlude the synaptic plasticities, oxidation was revealed to specifically inhibit signaling pathways essential for the PF-synaptic plasticities. Finally, biochemical analysis confirmed the idea that inhibitory action of protein oxidation on the PF-synaptic plasticities was mediated by impairment of NO-induced protein S-nitrosylation. Therefore, oxidation was revealed to inhibit S-nitrosylation dependent signaling pathway essential for synaptic plasticity in a "competitive" manner.

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“…3). Other methods for PCO analysis include use of biotin hydrazide coupled to fluorescein isothiocyanate (FITC)-labeled streptavidin (374).…”

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confidence: 99%

Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

Butterfield

Perluigi

Reed

et al. 2012

Antioxidants & Redox Signaling

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Several studies demonstrated that oxidative damage is a characteristic feature of many neurodegenerative diseases. The accumulation of oxidatively modified proteins may disrupt cellular functions by affecting protein expression, protein turnover, cell signaling, and induction of apoptosis and necrosis, suggesting that protein oxidation could have both physiological and pathological significance. For nearly two decades, our laboratory focused particular attention on studying oxidative damage of proteins and how their chemical modifications induced by reactive oxygen species/reactive nitrogen species correlate with pathology, biochemical alterations, and clinical presentations of Alzheimer's disease. This comprehensive article outlines basic knowledge of oxidative modification of proteins and lipids, followed by the principles of redox proteomics analysis, which also involve recent advances of mass spectrometry technology, and its application to selected age-related neurodegenerative diseases. Redox proteomics results obtained in different diseases and animal models thereof may provide new insights into the main mechanisms involved in the pathogenesis and progression of oxidativestress-related neurodegenerative disorders. Redox proteomics can be considered a multifaceted approach that has the potential to provide insights into the molecular mechanisms of a disease, to find disease markers, as well as to identify potential targets for drug therapy. Considering the importance of a better understanding of the cause/effect of protein dysfunction in the pathogenesis and progression of neurodegenerative disorders, this article provides an overview of the intrinsic power of the redox proteomics approach together with the most significant results obtained by our laboratory and others during almost 10 years of research on neurodegenerative disorders since we initiated the field of redox proteomics. Antioxid. Redox Signal. 17, 1610-1655.

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Protein Carbonylation

Cited by 342 publications

References 28 publications

Small heat shock proteins in ageing and age-related diseases

Small heat shock proteins in ageing and age-related diseases

Protein oxidation inhibits NO-mediated signaling pathway for synaptic plasticity

Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

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