Nitric oxide induces a reversible inactivation of C-kinase activity and phorbol ester binding

Gopalakrishna, Rayudu; Chen, Zhen Hai; Gundimeda, Usha

doi:10.1016/0891-5849(93)90299-a

Cited by 71 publications

(86 citation statements)

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“…However, somewhat surprising, co-addition of DTT failed to reverse the inhibitory effect of SIN-1 on PKC-regulated insulin release (Sjo È holm, 1996d). This indicates either that SIN-1 acts unrelated to S-nitrosylation in this case, or, alternatively, that NO permanently inactivated PKC, as has been reported previously (Gopalakrishna et al, 1993).…”

Section: No Impacts Negatively On the B-cell Insulin Stimulus-secretisupporting

confidence: 50%

“…This is an attractive hypothesis since PKC has critical thiol residues that that influence its kinase activity and which can be oxidized by NO (Gopalakrishna et al, 1993). However, somewhat surprising, co-addition of DTT failed to reverse the inhibitory effect of SIN-1 on PKC-regulated insulin release (Sjo È holm, 1996d).…”

Section: No Impacts Negatively On the B-cell Insulin Stimulus-secretimentioning

confidence: 99%

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Aspects of the involvement of interleukin-1 and nitric oxide in the pathogenesis of insulin-dependent diabetes mellitus

Sjöholm

1998

Cell Death Differ

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The possible involvement of the cytokine interleukin-1 (IL-1) and nitric oxide (NO) in the pathogenesis of insulin-dependent diabetes mellitus (IDDM) is reviewed and current and potential therapies are discussed. IDDM is a common disorder in the Western world and it is rising in incidence. In IDDM, isletinfiltrating macrophages produce IL-1 which is cytotoxic specifically to b-cells in vitro. IL-1 increases b-cell formation of NO, ceramide, prostaglandins, heat-shock proteins, and activates a protease. Additionally, IL-1 depresses b-cell energy production, insulin gene expression and cyclic AMP synthesis, and impacts negatively on different parts of the insulin stimulus-secretion coupling, actions mimicked by NO. Conversely, blocking NO formation prevented many of these effects in most reports published. Also, changes in cyclic AMP and prostaglandins seem unlikely events in mediating the cytotoxicity of IL-1, while the role of ceramide remains less clear. Peptides capable of blocking b-cell IL-1 receptors, and agents blocking NO synthesis may prove valuable in preserving b-cell function in IDDM. Although IDDM causes immense morbidity and expense, uniformly effective preventive or b-cell protective therapy is not currently available. If IL-1 is causing b-cell dysfunction in human IDDM through NO production, several processes in the IL-1-NO connection are appropriate targets for agents protecting b-cells from destruction and functional inhibition in IDDM.

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Section: No Impacts Negatively On the B-cell Insulin Stimulus-secretisupporting

confidence: 50%

Section: No Impacts Negatively On the B-cell Insulin Stimulus-secretimentioning

confidence: 99%

Aspects of the involvement of interleukin-1 and nitric oxide in the pathogenesis of insulin-dependent diabetes mellitus

Sjöholm

1998

Cell Death Differ

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“…3E). Although the effect of nNOS and NO on GluA1-S831 phosphorylation might be the result of effects on PKC or CaMKII, this possibility is unlikely because S-nitrosylation of these two enzymes reduces their activity (19)(20)(21). Also, a role for guanylate cyclase in mediating the activating effects of NO on GluA1-S831 phosphorylation is unlikely because inhibition of cyclic guanylate kinase increases glycine-stimulated phosphorylation of GluA1-S831 (22).…”

Section: Resultsmentioning

confidence: 99%

S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis

Selvakumar

Jenkins

Hussain

et al. 2012

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

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NMDA receptor activation can elicit synaptic plasticity by augmenting conductance of the AMPA receptor GluA1 subsequent to phosphorylation at S831 by Ca 2+ -dependent kinases. NMDA receptor activation also regulates synaptic plasticity by causing endocytosis of AMPA receptor GluA1. We demonstrate a unique signaling cascade for these processes mediated by NMDA receptor-dependent NO formation and GluA1 S-nitrosylation. Thus, S-nitrosylation of GluA1 at C875 enhances S831 phosphorylation, facilitates the associated AMPA receptor conductance increase, and results in endocytosis by increasing receptor binding to the AP2 protein of the endocytotic machinery.A MPA receptors (AMPARs) are tetramers in their physiologic form, with GluA1 being one of the more important regulatory subunits (1). Synaptic plasticity frequently is mediated by activation of NMDA receptors (NMDARs), which can modulate surface expression and single-channel conductance of AMPARs during the early phase of long-term potentiation (LTP) (1, 2). Phosphorylation of S831 of GluA1 mediates such plasticity, as phosphorylation of this site increases during LTP (3, 4), and mutant mice overexpressing a phosphomimetic S831D mutation display enhanced AMPAR conductance and LTP (5, 6).Mechanisms whereby NMDAR transmission augments AMPAR conductance have been unclear. NMDAR activation leads to calcium entry, which stimulates catalytic activity of neuronal nitric oxide synthase (nNOS) (7,8). NO (nitric oxide) signals by activating guanylate cyclase, and by S-nitrosylating cysteines of many target proteins (9, 10). NO regulates AMPARs by targeting AMPARinteracting proteins that determine receptor surface expression. Thus, physiologic S-nitrosylation of NSF (N-ethylmaleimide sensitive factor) elicits enhanced surface expression of GluA2 (11). Transmembrane AMPAR regulatory proteins are prominent auxiliary proteins for AMPARs, with stargazin being the best characterized (12). NMDAR transmission triggers S-nitrosylation of stargazin, which increases surface expression of GluA1 (13).The surface expression of AMPARs that determines synaptic plasticity is regulated by endocytosis because inhibitors of endocytosis block AMPAR removal from the plasma membrane, resulting in increased surface expression of AMPARs and long term depression (LTD) (14). Although NO has been implicated in regulation of protein endocytosis (15), its role in regulating AMPAR endocytosis is unknown.In the present study, we show that GluA1 is physiologically S-nitrosylated under basal conditions, with increased nitrosylation upon NMDAR stimulation. Moreover, the NMDAR-dependent phosphorylation of GluA1-S831 is regulated by endogenous NO, which acts by S-nitrosylating GluA1-C875. These events regulate single-channel conductance of GluA1, as the increase of such conductance by phosphorylation is markedly slowed in GluA1-C875S mutants. Endocytosis of AMPAR also is regulated by nitrosylation of GluA1-C875, because the C875S mutant of GluA1 reduces AMPAR endocytosis in neuronal cells and decreases binding ...

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“…18,19 NO may inactivate NADPH oxidase by inhibiting its assembling process. 45 Alternatively, NO may reduce NADPH oxidase activity via the inhibition of protein kinase C. 46 The inhibitory effect of NO on MCP-1 induction is not mediated via cGMP because ECs treated with KT5823, a cGMPdependent protein kinase inhibitor, did not attenuate the inhibitory effect of NO on cyclic strain-induced MCP-1 expression (data not shown). This is consistent with a previous observation that cGMP is not involved in the suppressive effect of NO on shear-induced Egr-1 expression.…”

Section: Discussionmentioning

confidence: 99%

NO Modulates Monocyte Chemotactic Protein-1 Expression in Endothelial Cells Under Cyclic Strain

Wung

Cheng

Shyue

et al. 2001

ATVB

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Nitric oxide induces a reversible inactivation of C-kinase activity and phorbol ester binding

Cited by 71 publications

References 0 publications

Aspects of the involvement of interleukin-1 and nitric oxide in the pathogenesis of insulin-dependent diabetes mellitus

Aspects of the involvement of interleukin-1 and nitric oxide in the pathogenesis of insulin-dependent diabetes mellitus

S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis

NO Modulates Monocyte Chemotactic Protein-1 Expression in Endothelial Cells Under Cyclic Strain

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