Modulation of ion channels by reactive oxygen and nitrogen species: a pathophysiological role in brain aging?

Annunziato, Lucio; Pannaccione, Anna; Cataldi, Mauro; Secondo, Agnese; Castaldo, Pasqualina; Renzo, Gianfranco Di; Taglialatela, Maurizio

doi:10.1016/s0197-4580(02)00069-6

Cited by 105 publications

(82 citation statements)

References 133 publications

(132 reference statements)

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“…This finding is consistent with the report that ROS, especially superoxide, enhance Ca 2ϩ currents only at negative depolarizing voltages (Li et al, 1998;Annunziato et al, 2002); however, the mechanisms by which ROS alter Ca 2ϩ channel activities remain poorly understood (Kourie, 1998). One possibility is that ROS produce oxidation of sulfhydryl groups of cystine residues, resulting in the formation of disulfide bonds (S-S) that modify the structure-function relationship of Ca 2ϩ channel proteins (Chiamvimonvat et al, 1995;Kourie, 1998;Li et al, 1998).…”

Section: Mechanisms Of Ros Actions On Ca 2؉ Currentssupporting

confidence: 90%

NADPH Oxidase Contributes to Angiotensin II Signaling in the Nucleus Tractus Solitarius

Wang¹,

Anrather²,

Huang³

et al. 2004

J. Neurosci.

157

183

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Section: Mechanisms Of Ros Actions On Ca 2؉ Currentssupporting

confidence: 90%

NADPH Oxidase Contributes to Angiotensin II Signaling in the Nucleus Tractus Solitarius

Wang¹,

Anrather²,

Huang³

et al. 2004

J. Neurosci.

157

183

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“…Various studies demonstrate functional modulation of ionic channels by oxidation (Aizenmann et al 1989;Annunziato et al, 2002;Cai and Sesti, 2009). In the present study, treatment of the cerebellar slices with oxidizing agents did not induce significant changes in basic electrophysiological properties of PF-EPSC (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…However, it is still possible that protein oxidation indirectly inhibited these synaptic plasticities through impairment of synaptic function itself, because functional losses of ionic channels by oxidation had been reported in previous studies (Annunziato et al, 2002). To exclude these possibilities, we examined whether oxidation by the oxidizing agent (H2O2) affect basic electrophysiological properties of PF 14 synapses.…”

Section: Pf-synaptic Plasticitymentioning

confidence: 97%

“…We first incubated acute cerebellar slices from young mice with H2O2, typical oxidizing agent which is known to induce functional changes in ionic channels (Annunziato et al, 2002;Cai and Sesti, 2009). In the cerebellar slices preincubated with H2O2, PF-PTP and PF-LTP were impaired in a dose-dependent manner (Suppl Fig.…”

Section: Biotin-switch Assay For Protein S-nitrosylationmentioning

confidence: 99%

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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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“…The large surface to volume ratio of nerve endings, where transduction occurs, presumably further increases the vulnerability of membrane proteins therein to oxidative damages. Products of oxidation may accumulate analogous to the accrual of oxidized proteins in aging (47)(48)(49) or other neurological disorders, like Alzheimer's disease, Parkinson's disease, and chronic neuropathic pain (44,(50)(51)(52). Unless neurons repair or remove oxidized TRPV1, covalently modified receptors may reside in sensory nerves for an unduly long time and contribute to the development of chronic pain.…”

Section: Discussionmentioning

confidence: 99%

Oxidative challenges sensitize the capsaicin receptor by covalent cysteine modification

Chuang

Lin

2009

Proc. Natl. Acad. Sci. U.S.A.

165

119

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The capsaicin receptor TRPV1, one of the major transduction channels in the pain pathway, integrates information from extracellular milieu to control excitability of primary nociceptive neurons. Sensitization of TRPV1 heightens pain sensation to moderately noxious or even innocuous stimuli. We report here that oxidative stress markedly sensitizes TRPV1 in multiple species' orthologs. The sensitization can be recapitulated in excised insideout membrane patches, reversed by strong reducing agents, and blocked by pretreatment with maleimide that alkylates cysteines. We identify multiple cysteines required for full modulation of TRPV1 by oxidative challenges. Robust oxidative modulation recovers the agonist sensitivity of receptors desensitized by prolonged exposure to capsaicin. Moreover, oxidative modulation operates synergistically with kinase or proton modulations. Thus, oxidative modulation is a robust mechanism tuning TRPV1 activity via covalent modification of evolutionarily conserved cysteines and may play a role in pain sensing processes during inflammation, infection, or tissue injury.covalent modification ͉ pain

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Modulation of ion channels by reactive oxygen and nitrogen species: a pathophysiological role in brain aging?

Cited by 105 publications

References 133 publications

NADPH Oxidase Contributes to Angiotensin II Signaling in the Nucleus Tractus Solitarius

NADPH Oxidase Contributes to Angiotensin II Signaling in the Nucleus Tractus Solitarius

Protein oxidation inhibits NO-mediated signaling pathway for synaptic plasticity

Oxidative challenges sensitize the capsaicin receptor by covalent cysteine modification

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