Regulation of voltage‐dependent K<sup>+</sup> channels by methionine oxidation: effect of nitric oxide and vitamin C

Ciorba, Matthew A.; Heinemann, Stefan H.; Weissbach, Herbert; Brot, Nathan; Hoshi, Toshinori

doi:10.1016/s0014-5793(98)01616-0

Cited by 61 publications

(48 citation statements)

References 37 publications

(51 reference statements)

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“…Different forms of redox modulation of Kv channels have been reported, including methionine oxidation by methioninesulfoxide reductase or reactive oxygen species (35)(36)(37) and cysteine oxidation by reactive oxygen species (38). This study adds NADPH to the targets of oxidation, and in this case, because it is mediated by an aldoketoreductase, it has the potential of being highly selective for a specific substrate.…”

Section: Discussionmentioning

confidence: 94%

Functional Coupling between the Kv1.1 Channel and Aldoketoreductase Kvβ1

Pan

Weng

Cao

et al. 2008

Journal of Biological Chemistry

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The Shaker family voltage-dependent potassium channels (Kv1) assemble with cytosolic ␤-subunits (Kv␤) to form a stable complex. All Kv␤ subunits have a conserved core domain, which in one of them (Kv␤2) is an aldoketoreductase that utilizes NADPH as a cofactor. In addition to this core, Kv␤1 has an N terminus that closes the channel by the N-type inactivation mechanism. Point mutations in the putative catalytic site of Kv␤1 alter the on-rate of inactivation. Whether the core of Kv␤1 functions as an enzyme and whether its enzymatic activity affects N-type inactivation had not been explored. Here, we show that Kv␤1 is a functional aldoketoreductase and that oxidation of the Kv␤1-bound cofactor, either enzymatically by a substrate or non-enzymatically by hydrogen peroxide or NADP ؉ , induces a large increase in open channel current. The modulation is not affected by deletion of the distal C terminus of the channel, which has been suggested in structural studies to interact with Kv␤. The rate of increase in current, which reflects NADPH oxidation, is ϳ2-fold faster at 0-mV membrane potential than at ؊100 mV. Thus, cofactor oxidation by Kv␤1 is regulated by membrane potential, presumably via voltage-dependent structural changes in Kv1.1 channels.

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Section: Discussionmentioning

confidence: 94%

Functional Coupling between the Kv1.1 Channel and Aldoketoreductase Kvβ1

Pan

Weng

Cao

et al. 2008

Journal of Biological Chemistry

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“…This study does not directly address how these two mechanisms contribute to the Ca 2ϩ potentiation. Acting as a radical, NO may directly affect the properties of voltage-dependent K ϩ channels and thus alter cellular excitability and Ca 2ϩ signaling (42,43). NO also has been implicated in cellular plasticity including neuronal differentiation and neurite outgrowth and, as recently suggested, in cortex development (44)(45)(46).…”

Section: Discussionmentioning

confidence: 99%

Reactive oxygen species and nitric oxide mediate plasticity of neuronal calcium signaling

Yermolaieva

Brot

Weissbach

et al. 2000

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

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103

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Reactive oxygen species (ROS) and nitric oxide (NO) are important participants in signal transduction that could provide the cellular basis for activity-dependent regulation of neuronal excitability. In young rat cortical brain slices and undifferentiated PC12 cells, paired application of depolarization͞agonist stimulation and oxidation induces long-lasting potentiation of subsequent Ca 2؉ signaling that is reversed by hypoxia. This potentiation critically depends on NO production and involves cellular ROS utilization. The ability to develop the Ca 2؉ signal potentiation is regulated by the developmental stage of nerve tissue, decreasing markedly in adult rat cortical neurons and differentiated PC12 cells.

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“…With regard to GPxs, TRs, and MsrB1, the enzymes with known functions, it appears clear that redox regulation or protection from reactive oxygen species may be the main functions (54). It may well be that neuronal signaling or synaptic transmission are modulated by the (transient) redox potential around neurotransmitter receptors, and at least for one K ϩ channel regulation through reversible methionine oxidation has been demonstrated (62). Many selenoproteins with still unknown function have a common thioredoxin fold, suggesting catalysis of redox reactions.…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Selenocysteine Machinery and Selenoproteome Gene Expression in Mouse Brain Identifies Neurons as Key Functional Sites of Selenium in Mammals

Zhang

Zhou

Schweizer

et al. 2008

Journal of Biological Chemistry

161

123

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Although dietary selenium (Se) deficiency results in phenotypes associated with selenoprotein depletion in various organs, the brain is protected from Se loss. To address the basis for the critical role of Se in brain function, we carried out comparative gene expression analyses for the complete selenoproteome and associated biosynthetic factors. Using the Allen Brain Atlas, we evaluated 159 regions of adult mouse brain and provided experimental analyses of selected selenoproteins. All 24 selenoprotein mRNAs were expressed in the mouse brain. Most strikingly, neurons in olfactory bulb, hippocampus, cerebral cortex, and cerebellar cortex were exceptionally rich in selenoprotein gene expression, in particular in GPx4, SelK, SelM, SelW, and Sep15. Over half of the selenoprotein genes were also expressed in the choroid plexus. A unique expression pattern was observed for one of the highly expressed selenoprotein genes, SelP, which we suggest to provide neurons with Se. Cluster analysis of the expression data linked certain selenoproteins and selenocysteine machinery genes and suggested functional linkages among selenoproteins, such as that between SelM and Sep15. Overall, this study suggests that the main functions of selenium in mammals are confined to certain neurons in the brain.

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Regulation of voltage‐dependent K⁺ channels by methionine oxidation: effect of nitric oxide and vitamin C

Cited by 61 publications

References 37 publications

Functional Coupling between the Kv1.1 Channel and Aldoketoreductase Kvβ1

Functional Coupling between the Kv1.1 Channel and Aldoketoreductase Kvβ1

Reactive oxygen species and nitric oxide mediate plasticity of neuronal calcium signaling

Comparative Analysis of Selenocysteine Machinery and Selenoproteome Gene Expression in Mouse Brain Identifies Neurons as Key Functional Sites of Selenium in Mammals

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Regulation of voltage‐dependent K+ channels by methionine oxidation: effect of nitric oxide and vitamin C

Cited by 61 publications

References 37 publications

Functional Coupling between the Kv1.1 Channel and Aldoketoreductase Kvβ1

Functional Coupling between the Kv1.1 Channel and Aldoketoreductase Kvβ1

Reactive oxygen species and nitric oxide mediate plasticity of neuronal calcium signaling

Comparative Analysis of Selenocysteine Machinery and Selenoproteome Gene Expression in Mouse Brain Identifies Neurons as Key Functional Sites of Selenium in Mammals

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Regulation of voltage‐dependent K⁺ channels by methionine oxidation: effect of nitric oxide and vitamin C