Depleted internal store-activated Ca2+ entry can trigger neurotransmitter release in bovine chromaffin cells

Powis, David; Clark, Carolyn L.; O'Brien, K.J.

doi:10.1016/0304-3940(96)12346-6

Cited by 23 publications

(22 citation statements)

References 24 publications

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“…However, the contribution of capacitative Ca 2ϩ entry to catecholamine release from chromaffin cells remains unsettled. 34,35 The lack of requirement of ryanodine/caffeine-sensitive stores for sustained secretion induced by PACAP (see Results) argues against participation of these stores in long-term catecholamine release. On the other hand, the less than additive stimulatory effect of combined PACAP and SERCA inhibition on the prolonged secretion ( Figure 8A), together with the inhibitory effect of the SOCC (non-VOCC) blocker SKF96365 ( Figure 8B), suggests that PACAP-mediated PLC-␤ activation may trigger Ca 2ϩ release from IP 3 -sensitive intracellular stores, eventuating in the subsequent capacitative (SOCC) Ca 2ϩ influx.…”

Section: Sustained Secretionmentioning

confidence: 99%

“…34,35 SERCA inhibition by agents such as thapsigargin characteristically triggers sustained, capacitative Ca 2ϩ entry. 31,32 As shown in Figure 8A, depletion of intracellular Ca 2ϩ stores of PC12 cells by continuous exposure to thapsigargin (1 mol/L) stimulated norepinephrine release, which showed only little desensitization for a period of up to 100 minutes.…”

Section: Characterization Of the Role Of Specific Cell Surface Vocc Smentioning

confidence: 99%

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Time-Dependent Effects of the Neuropeptide PACAP on Catecholamine Secretion

Taupenot

Mahata

et al. 1999

Hypertension

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Abstract-Pituitary adenylyl cyclase-activating polypeptide (PACAP) is a potent endogenous secretagogue for chromaffin cells. We previously reported that PACAP coupled to the PAC1 receptor to evoke dihydropyridine-sensitive early (15 to 20 minutes) catecholamine secretion and cAMP response element binding protein-mediated trans-activation of the secretory protein chromogranin A promoter in PC12 pheochromocytoma cells. In this report, we studied whether the secretory and transcriptional responses elicited by PACAP were subject to desensitization. We found that PACAP evoked distinct immediate (initial, 0 to 20 minutes) and long-lasting (20 to 180 minutes) effects on catecholamine secretion. Initial secretory and chromogranin A trans-activation responses induced by PACAP were desensitized in a dose-dependent fashion after preexposure of cells to PACAP, and the IC 50 doses of PACAP for desensitization were Ϸ18-to Ϸ32-fold lower than the EC 50 activating doses for secretion or transcription. Desensitization of the initial secretion response was associated with decreased Ca 2ϩ influx through L-type voltage-operated Ca 2ϩ channels. Acute exposure to PACAP also triggered long-lasting (up to 3 hours), extracellular Ca 2ϩ -dependent, pertussis toxin-insensitive catecholamine secretion; indeed, even after short-term (20 minutes) exposure to PACAP and removal of the secretagogue, PC12 cells continued to secrete norepinephrine up to 76.9Ϯ0.22% of cellular norepinephrine content after 3 hours. A phospholipase C-␤ inhibitor (U-73122) blocked this extended secretory response, which was dependent on low-magnitude Ca 2ϩ influx resistant to several L-, N-, P/Q-, or T-type Ca 2ϩ channel antagonists, but sensitive to Zn 2ϩ , Ni 2ϩ , Cd 2ϩ , or to the store-operated Ca 2ϩ channel blocker SKF96365. A less than additive effect of the sarcoendoplasmic reticulum Ca 2ϩ -ATPase inhibitor thapsigargin plus PACAP on this sustained secretion also supported a contribution of store-operated Ca 2ϩ entry to the sustained secretory response. We propose that PACAP-evoked secretion and transcription are subject to homologous desensitization in PC12 cells; however, PACAP also induces long-lasting secretion, even under dose and time circumstances in which acute, dihydropyridine-sensitive secretion has been desensitized. Although initial secretion is mediated by an L-type voltage-operated Ca 2ϩ channel, extended secretion may involve a store-operated Ca 2ϩ channel that is activated through a G q/11 /phospholipase C-␤/phosphoinositide signaling pathway. (Hypertension. 1999;34:1152-1162.)

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Section: Sustained Secretionmentioning

confidence: 99%

Section: Characterization Of the Role Of Specific Cell Surface Vocc Smentioning

confidence: 99%

Time-Dependent Effects of the Neuropeptide PACAP on Catecholamine Secretion

Taupenot

Mahata

et al. 1999

Hypertension

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“…Early experiments demonstrated Ca 2+ influx through SOCCs upon ER Ca 2+ depletion of bovine chromaffin cells [23]; this was corroborated by later experiments [22,[24][25][26][27][28]. A direct proof for the presence of SOCCs was obtained from voltage-clamped bovine chromaffin cells where a small-amplitude, voltage-independent I CRAC carried by Ca 2+ and Na + , was characterised under conditions of Ca 2+ store depletion [29].…”

Section: Store-operated Calcium Channelsmentioning

confidence: 82%

“…Upon repetitive stimulation with bursts of action potentials under stress, CICR may produce partial ER Ca 2+ depletion and give rise to SOCC activation. A modulatory role of this capacitative Ca 2+ entry on exocytosis in chromaffin cells has been suggested, but other pathways for Ca 2+ entry were not under control in these experiments [26]. Later, direct experiments demonstrated that receptor-free activation of Ca 2+ entry via SOCCs is sufficient to trigger and or facilitate exocytosis in these cells [29].…”

Section: Store-operated Calcium Channelsmentioning

confidence: 91%

Cytosolic organelles shape calcium signals and exo–endocytotic responses of chromaffin cells

et al. 2012

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a b s t r a c tfluxes between the different cell compartments support the proposal that the chromaffin cell has developed functional calcium tetrads formed by calcium channels, cytosolic calcium buffers, the endoplasmic reticulum, and mitochondria nearby the exocytotic plasmalemmal sites. These tetrads shape the Ca 2+ transients occurring during cell activation to regulate early and late steps of exocytosis, and the ensuing endocytotic responses. The different patterns of catecholamine secretion in response to stress may thus depend on such local [Ca 2+ ] c transients occurring at different cell compartments, and generated by redistribution and release of Ca 2+ by cytoplasmic organelles. In this manner, the calcium tetrads serve to couple the variable energy demands due to exo-endocytotic activities with energy production and protein synthesis.

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“…However, in non-excitable cells the major Ca 2+ entry pathway is activated by the emptying of intracellular Ca 2+ stores through an as yet undefined mechanism (Clapham 1995;Fasolato et al 1994;Parekh and Penner 1997;Putney and McKay 1999). The presence of such store-operated Ca 2+ entry has also been reported in chromaffin cells from bovine adrenal medulla (Fomina and Nowycky 1999;Powis et al 1996;Robinson et al 1992;Zerbes et al 1998).…”

Section: Introductionmentioning

confidence: 91%

Histamine-induced Ca2+ release in bovine adrenal chromaffin cells

Bödding

2001

Naunyn-Schmied Arch Pharmacol

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The histamine-induced biphasic increase of the intracellular free [Ca2+] ([Ca2+]i) was studied in bovine adrenal chromaffin cells using fura-2 microfluorimetry and the whole-cell patch-clamp technique. Both the rapid, transient Ca2+ rise and the sustained plateau component of elevated [Ca2+]i were independent of extracellular Ca2+. Incubation with the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) blocker thapsigargin diminished histamine-induced changes in [Ca2+]i. When Ca2+ release was either stimulated by IP3 or blocked with the competitive inhibitor heparin, histamine was unable to elicit the typical Ca2+ rise. Ryanodine, tetracaine and ruthenium red, all blockers of Ca2+ release from caffeine-sensitive stores, had only minor effects on the agonist-induced Ca2+ changes. The contribution of mitochondria in shaping the histamine-induced Ca2+ increase was studied using ruthenium red and the two proton ionophores carbonylcyanide m-chlorophenylhydrazone (CCCP) and carbonylcyanide p-(trifluoromethoxy)phenylhydrazone (FCCP). Both mitochondrial uncouplers reversibly increased [Ca2+]i and induced an inward current leading to cell membrane depolarisation. In summary, these results indicate that Ca2+ from IP3-sensitive stores is essential for the generation of both the transient increase and secondary elevation in [Ca2+]i.

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Depleted internal store-activated Ca2+ entry can trigger neurotransmitter release in bovine chromaffin cells

Cited by 23 publications

References 24 publications

Time-Dependent Effects of the Neuropeptide PACAP on Catecholamine Secretion

Time-Dependent Effects of the Neuropeptide PACAP on Catecholamine Secretion

Cytosolic organelles shape calcium signals and exo–endocytotic responses of chromaffin cells

Histamine-induced Ca2+ release in bovine adrenal chromaffin cells

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