Effects of SK&amp;F 96365, an inhibitor of receptor-mediated Ca2+ entry, on Ca2+ influx and catecholamine secretion in bovine adrenal chromaffin cells

Tachikawa, Eiichi; Takahashi, Saburo; Mizuma, Kenzo; Kondo, Yukiko; Kashimoto, Takeshi; Takahashi, Eiji

doi:10.1016/0304-3940(94)90890-7

Cited by 9 publications

(6 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because others also reported that inhibition of Ca 2ϩ influx using Ca 2ϩ entry blockers or a Na ϩ -free incubation solution only partially blocks the nicotinergic effects (23,25,(43)(44)(45), a similarly arranged two-component signaling system apparently operates in other cells downstream of nAChRs.…”

Section: Discussionmentioning

confidence: 99%

“…Indeed Ca 2ϩ ions that enter KCs through ␣7-containing ACh-gated ion channels can raise the concentration of intracellular free Ca 2ϩ in KCs (11,22), indicating that ionic events contribute to the nicotinergic effects on KCs. However, experiments with several types of non-neuronal cells demonstrated that the nicotinergic effects can be elicited in the absence of Na ϩ or Ca 2ϩ entry (23)(24)(25)(26). Therefore, the downstream signaling from ␣7 nAChR expressed in KCs may also proceed via parallel, ionic, and protein kinase signaling pathways.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Coupling of Ionic Events to Protein Kinase Signaling Cascades upon Activation of α7 Nicotinic Receptor

Chernyavsky

Arredondo

Qian

et al. 2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

Defining the signaling mechanisms and effector proteins mediating phenotypic and mechanical plasticity of keratinocytes (KCs) during wound epithelialization is one of the major goals in epithelial cell biology. The acetylcholine (ACh)-gated ion channels, or nicotinic ACh receptors (nAChRs), mediate the nicotinergic signaling that controls crawling locomotion of KCs. To elucidate relative contributions of the ionic and protein kinase-mediated events elicited due to activation of ␣7 nAChRs, we quantitated expression of ␣ 2 -integrin gene at the mRNA and protein levels and also measured Rho kinase activity in KCs stimulated with the ␣7 agonist AR-R17779 while blocking the Na ؉ or Ca 2؉ entry and/or inhibiting signaling kinases. The results demonstrated the existence of the two-component signaling systems coupling the ionic events and protein kinase signaling cascades downstream of ␣7 nAChR to simultaneous upregulation of ␣ 2 -integrin expression and activation of Rho kinase. The Raf/MEK1/ERK1/2 cascade up-regulating ␣ 2 -integrin was activated due to both Ca 2؉ -dependent recruitment of Ca 2؉ /calmodulin-dependent protein kinase II and protein kinase C and Ca 2؉ -independent activation of Ras. Likewise the phosphatidylinositol 3-kinase-mediated activation of Rho kinase was elicited due to both Ca 2؉ entry-dependent involvement of Ca 2؉ /calmodulin-dependent protein kinase II and Ca 2؉ -independent activation of Jak2. Thus, although the initial signals emanating from activated ␣7 nAChR are different in nature the pathways intersect at common effector molecules providing for a common end point effect. This novel paradigm of nAChR-mediated coordination of the ionic and metabolic signaling events can allow an auto/paracrine ACh to simultaneously alter gene expression and induce reciprocal changes in the cytoskeleton and contractile system of KCs required to compete a particular step of wound epithelialization.Defining the signaling mechanisms and effector proteins mediating phenotypic and mechanical plasticity of epidermal keratinocytes (KCs) 2 during their lateral migration in a wound bed is one of the major goals in epithelial cell biology. The epithelial and some other types of non-neuronal cells synthesize, degrade, and respond to acetylcholine (ACh) that functions outside the nervous system as an auto/paracrine hormone or a cytotransmitter (for a review, see Ref. 1). The non-neuronal ACh exhibits rapid and profound effects on gene expression due to activation of the muscarinic and nicotinic classes of cholinergic receptors coupling multiple signal transduction pathways. The muscarinic receptors are classic G protein-coupled transmembrane glycoproteins that mediate a metabolic response to ACh through the interactions of G proteins with signal transducing enzymes, leading to increases or decreases of second messengers, ion concentrations, and modulations of protein kinase activities. The nicotinic ACh receptors (nAChRs) are classic representatives of the superfamily of ligand-gated ion channel proteins, or ionotropi...

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Coupling of Ionic Events to Protein Kinase Signaling Cascades upon Activation of α7 Nicotinic Receptor

Chernyavsky

Arredondo

Qian

et al. 2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Inhibitors of SOCs, including SKF96365 and lanthanide ions such as Gd 3+ , Eu 3+ and La 3+ , have been successfully used to investigate their function in non‐excitable cells (e.g., Demaurex et al ., 1992; Fatatis et al ., 1992; Fernando & Barritt, 1994; 1995; Zimmermann, 1998). Their use in excitable cells such as chromaffin cells, however, is complicated by their non‐selective effects on other Ca 2+ ‐permeant channels including VOCCs and receptor‐operated channels (Tachikawa et al ., 1994).…”

Section: Introductionmentioning

confidence: 99%

Effect of Gd³⁺ on bradykinin‐induced catecholamine secretion from bovine adrenal chromaffin cells

Bales

Zerbes

Powis

et al. 1999

British J Pharmacology

View full text Add to dashboard Cite

1 The e ects of Gd 3+ on bradykinin-(BK-) induced catecholamine secretion, 45 Ca 2+ e ux and cytosolic [Ca 2+ ] were studied using bovine adrenal chroma n cells. 2 BK increased secretion in a Ca 2+ -dependent manner. From 1 ± 100 mM, Gd 3+ progressively inhibited secretion induced by 30 nM BK to near-basal levels, however from 0.3 ± 3 mM Gd 3+ dramatically enhanced BK-induced secretion to above control levels. Gd 3+ also increased basal catecholamine secretion by 2 ± 3 fold at 1 mM. These e ects were mimicked by Eu 3+ and La 3+ . 3 Gd 3+ enhanced secretion induced by other agonists that mobilize intracellular Ca 2+ stores, but simply blocked the response to K + . 4 Gd 3+ still enhanced basal and BK-induced secretion in Ca 2+ -free solution or in the presence of 30 mM SKF96365, however both e ects of Gd 3+ were abolished after depleting intracellular Ca 2+ stores. 5 Gd 3+ (1 mM) reduced the rate of basal 45 Ca 2+ e ux by 57%. In Ca 2+ -free bu er, BK transiently increased cytosolic [Ca 2+ ] measured with Fura-2. The [Ca 2+ ] response to BK was substantially prolonged in the presence of Gd 3+ (1 mM). 6 The results suggest that Gd 3+ greatly enhances the e cacy of Ca 2+ released from intracellular stores in evoking catecholamine secretion, by inhibiting Ca 2+ extrusion from the cytosol. This suggests that intracellular Ca 2+ stores are fully competent to support secretion in chroma n cells to levels comparable to those evoked by extracellular Ca 2+ entry. Drugs that modify Ca 2+ extrusion from the cell, such as lanthanide ions, will be useful in investigating the mechanisms by which intracellular Ca 2+ -store mobilization couples to Ca 2+ -dependent exocytosis.

show abstract

“…SKF96365 was tested for its ability to prevent the enhancing effect of La 3+ on histamine‐induced secretion. SKF96365 blocks VOCCs and ROCs (e.g., the nicotinic acetylcholine receptor ion channel) in chromaffin cells, as well as capacitative Ca 2+ entry through SOCs in a variety of nonexcitable cells (see Tachikawa et al, 1994). SKF96365 completely blocked the secretory response to histamine (Fig.…”

Section: Resultsmentioning

confidence: 99%

Mobilizing Store Ca²⁺ in the Presence of La³⁺ Evokes Exocytosis in Bovine Chromaffin Cells

Marley¹,

Bales²,

Zerbes³

et al. 2000

Journal of Neurochemistry

View full text Add to dashboard Cite

Abstract:The effect on exocytosis of La 3ϩ , a known inhibitor of plasma membrane Ca 2ϩ -ATPases and Na ϩ / Ca 2ϩ exchangers, was studied using cultured bovine adrenal chromaffin cells. At high concentrations (0.3-3 mM), La 3ϩ substantially increased histamine-induced catecholamine secretion. This action was mimicked by other lanthanide ions (Nd 3ϩ Extracellular fluid is the principal source of Ca 2ϩ in neurons (Berridge, 1998). Neurotransmitter release is essentially dependent on Ca 2ϩ influx through the plasma membrane. In adrenal chromaffin cells, voltage-operated Ca 2ϩ channels (VOCCs) are responsible for the majority of the Ca 2ϩ entry that supports catecholamine release evoked by both depolarizing agonists and agonists acting at G protein-coupled receptors (Burgoyne, 1991;Artalejo et al., 1994;Lomax et al., 1997;O'Farrell and Marley, 1997Lara et al., 1998). Although mobilization of intracellular Ca 2ϩ stores modulates secretion, it fails to evoke significant levels of exocytosis in the absence of Ca 2ϩ (Kim and Westhead, 1989;Pan and Kao, 1997 Schroeder et al., 1994;Robinson et al., 1995Robinson et al., , 1996. VOCCs mediate substantial Ca 2ϩ influx in these cells and are very effective at evoking secretion. Parts of the endoplasmic reticulum come into close contact with the plasma membrane (Berridge, 1998), and some of these Ca 2ϩ stores are suitably located in chromaffin cells to influence membrane events [such as K ϩ channel activity (Kim and Kim, 1998)]. Their lack of efficacy in evoking exocytosis is likely to be because mobilization of store Ca 2ϩ fails to generate a sufficiently high subplasmalemmal [Ca 2ϩ ]. This may be because (a) the stores do not contain sufficient quantities of Ca 2ϩ , (b) the density of channels on the store membrane is too low, (c) insufficient numbers of such channels are activated at any one time, or (d) local Ca 2ϩ buffering and Ca 2ϩ reuptake and extrusion processes prevent high concentrations of Ca 2ϩ being achieved by store mobilization. This last possibility is of particular interest because the activity of the sarco/endoplasmic reticulum Ca 2ϩ -ATPases (SERCAs) and of the plasma membrane Ca 2ϩ -ATPases (PMCAs) and Na ϩ /Ca 2ϩ exchangers is acutely regulated (Verboomen et al., 1995;Matsuda et al., 1997;Guerini, 1998;Pan et al., 1998

show abstract

Effects of SK&F 96365, an inhibitor of receptor-mediated Ca2+ entry, on Ca2+ influx and catecholamine secretion in bovine adrenal chromaffin cells

Cited by 9 publications

References 15 publications

Coupling of Ionic Events to Protein Kinase Signaling Cascades upon Activation of α7 Nicotinic Receptor

Coupling of Ionic Events to Protein Kinase Signaling Cascades upon Activation of α7 Nicotinic Receptor

Effect of Gd³⁺ on bradykinin‐induced catecholamine secretion from bovine adrenal chromaffin cells

Mobilizing Store Ca²⁺ in the Presence of La³⁺ Evokes Exocytosis in Bovine Chromaffin Cells

Contact Info

Product

Resources

About

Effects of SK&F 96365, an inhibitor of receptor-mediated Ca2+ entry, on Ca2+ influx and catecholamine secretion in bovine adrenal chromaffin cells

Cited by 9 publications

References 15 publications

Coupling of Ionic Events to Protein Kinase Signaling Cascades upon Activation of α7 Nicotinic Receptor

Coupling of Ionic Events to Protein Kinase Signaling Cascades upon Activation of α7 Nicotinic Receptor

Effect of Gd3+ on bradykinin‐induced catecholamine secretion from bovine adrenal chromaffin cells

Mobilizing Store Ca2+ in the Presence of La3+ Evokes Exocytosis in Bovine Chromaffin Cells

Contact Info

Product

Resources

About

Effect of Gd³⁺ on bradykinin‐induced catecholamine secretion from bovine adrenal chromaffin cells

Mobilizing Store Ca²⁺ in the Presence of La³⁺ Evokes Exocytosis in Bovine Chromaffin Cells