cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

Hashii, Minako; Minabe, Yoshio; Higashida, Haruhiro

doi:10.1042/bj3450207

Cited by 44 publications

(52 citation statements)

References 35 publications

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“…Importantly, cADPR/ryanodine-sensitive stores are also responsible for the Ca 2ϩ -induced Ca 2ϩ release triggered by action potentials (36, for review see ref 50). Hence, the elevations in [Ca 2ϩ ] i reported here may be expected to boost the action-potential evoked Ca 2ϩ transients and transmitter release, as found in the nodose ganglion cells (58) or neuroblastoma cell lines (59,60). Whether the NO-cGMP-cADPR-Ca 2ϩ pathway is sufficiently powerful to lead to action potential-independent GABA release is at present unclear, although some data suggest that this might be the case, at least in the hypothalamus (17).…”

Section: Ca 2؉ Release From Cadpr-ryanodine Sensitive Stores Is a Keymentioning

confidence: 92%

Mechanism of nitric oxide action on inhibitory GABAergic signaling within the nucleus tractus solitarii

Wang

Teschemacher²,

Paton³

et al. 2006

FASEB j.

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The cellular mechanisms mediating nitric oxide (NO) modulation of the inhibitory transmission in the nucleus tractus solitarii (NTS) remain unclear, even though this could be extremely important for various physiological and pathological processes. Specifically, in the NTS NO-evoked glutamate and gamma-aminobutyric acid (GABA) release might contribute to pathological hypertension. In cultured rat brainstem slices, NTS GABAergic neurons were targeted using an adenoviral vector to express enhanced green fluorescent protein and studied with a combination of patch clamp and confocal microscopy. Low nanomolar concentrations of NO increased intracellular Ca2+ concentration ([Ca2+]i) in somata, dendrites, and putative axons of GABAergic neurons, with axons being the most sensitive compartment. This effect was cGMP mediated and not related to depolarization or indirect presynaptic effects on glutamatergic transmission. Blockade of the cyclic adenosine diphosphate ribose (cADPR)/ryanodine-sensitive stores but not the inositol triphosphate-sensitive stores, inhibited NO effect. Since cADPR/ryanodine-sensitive stores are implicated in the Ca2+-induced Ca2+ release, NO can be expected to potentiate GABA release. In support of this notion, a cADPR antagonist abolished the NO-induced potentiation of GABAergic inhibitory postsynaptic potentials in the NTS. Thus, the NO-cGMP-cADPR-Ca2+ pathway, previously described in sea urchin eggs, also operates in mammalian GABAergic neurons. Potentiation of GABA release by NO may have implications for numerous brain functions.

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Section: Ca 2؉ Release From Cadpr-ryanodine Sensitive Stores Is a Keymentioning

confidence: 92%

Mechanism of nitric oxide action on inhibitory GABAergic signaling within the nucleus tractus solitarii

Wang

Teschemacher²,

Paton³

et al. 2006

FASEB j.

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“…4 and 8). Although it is not known how cADPR regulates extracellular calcium influx in any cell type, it has been suggested that cADPR regulates the activation of L-type calcium channels and store-operated I crac channels (6,56). Interestingly, human neutrophils have been reported to express L-type channels as well as I crac channels (57,58).…”

Section: Discussionmentioning

confidence: 99%

Chemotaxis and Calcium Responses of Phagocytes to Formyl Peptide Receptor Ligands Is Differentially Regulated by Cyclic ADP Ribose

Partida-Sánchez

Iribarren

Moreno‐García

et al. 2004

The Journal of Immunology

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Cyclic ADP ribose (cADPR) is a calcium-mobilizing metabolite that regulates intracellular calcium release and extracellular calcium influx. Although the role of cADPR in modulating calcium mobilization has been extensively examined, its potential role in regulating immunologic responses is less well understood. We previously reported that cADPR, produced by the ADP-ribosyl cyclase, CD38, controls calcium influx and chemotaxis of murine neutrophils responding to fMLF, a peptide agonist for two chemoattractant receptor subtypes, formyl peptide receptor and formyl peptide receptor-like 1. In this study, we examine whether cADPR is required for chemotaxis of human monocytes and neutrophils to a diverse array of chemoattractants. We found that a cADPR antagonist and a CD38 substrate analogue inhibited the chemotaxis of human phagocytic cells to a number of formyl peptide receptor-like 1-specific ligands but had no effect on the chemotactic response of these cells to ligands selective for formyl peptide receptor. In addition, we show that the cADPR antagonist blocks the chemotaxis of human monocytes to CXCR4, CCR1, and CCR5 ligands. In all cases, we found that cADPR modulates intracellular free calcium levels in cells activated by chemokines that induce extracellular calcium influx in the apparent absence of significant intracellular calcium release. Thus, cADPR regulates calcium signaling of a discrete subset of chemoattractant receptors expressed by human leukocytes. Since many of the chemoattractant receptors regulated by cADPR bind to ligands that are associated with clinical pathology, cADPR and CD38 represent novel drug targets with potential application in chronic inflammatory and neurodegenerative disease.

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“…2ϩ -dependent ERK Activation in NG108 Neuroblastoma Cells-To investigate the potential role of CaMKs in modulat-ing Ca 2ϩ -dependent ERK activation, we selected the NG108 neuroblastoma cell line that can be stimulated by depolarization to raise intracellular calcium levels (41,42). Depolarization of neuronal cells is known to produce activation of CaMKII (43) and CaMKK (35) as well as ERK (5,44).…”

Section: Camentioning

confidence: 99%

Calcium Activation of ERK Mediated by Calmodulin Kinase I

Schmitt

Wayman

Nozaki

et al. 2004

Journal of Biological Chemistry

144

133

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Elevated intracellular Ca2؉ triggers numerous signaling pathways including protein kinases such as the calmodulin-dependent kinases (CaMKs) and the extracellular signal-regulated kinases (ERKs). In the present study we examined Ca 2؉ -dependent "cross-talk" between these two protein kinase families. Using a combination of pharmacological inhibitors and dominant-negative kinases (dnKinase), we identified a requirement for CaMKK acting through CaMKI in the stimulation of ERKs upon depolarization of the neuroblastoma cell line, NG108. Depolarization stimulated prolonged ERK and JNK activation that was blocked by the CaMKK inhibitor, STO-609; this inhibition of ERK activation by STO-609 was rescued by expression of a STO-609-insensitive mutant of CaMKK. However, activation of ERK by epidermal growth factor or carbachol were not suppressed by inhibition of CaMKK, indicating specificity for this "cross-talk." To identify the downstream target of CaMKK that mediated ERK activation upon depolarization, dnKinases were expressed. The dnCaMKI completely suppressed ERK2 activation whereas dnAKT/PKB or nuclear-targeted dnCaMKIV, other substrates for CaMKK, were not inhibitory. ERK activation upon depolarization or transfection with constitutively active (ca) CaMKI was blocked by dnRas. Additionally, depolarization of NG108 cells promoted neurite outgrowth, and this effect was blocked by inhibition of either CaMKK (STO-609) or ERK (UO126). Co-transfection with caCaMKK plus caCaMKI also stimulated neurite outgrowth that was blocked by inhibition of ERK (UO126). These data are the first to suggest that ERK activation and neurite outgrowth in response to depolarization are mediated by CaMKK activation of CaMKI.

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cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

Cited by 44 publications

References 35 publications

Mechanism of nitric oxide action on inhibitory GABAergic signaling within the nucleus tractus solitarii

Mechanism of nitric oxide action on inhibitory GABAergic signaling within the nucleus tractus solitarii

Chemotaxis and Calcium Responses of Phagocytes to Formyl Peptide Receptor Ligands Is Differentially Regulated by Cyclic ADP Ribose

Calcium Activation of ERK Mediated by Calmodulin Kinase I

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