β-Adrenergic agonists stimulate Mg2+ uptake in mouse distal convoluted tubule cells

2000 ◽  
Vol 279 (6) ◽  
pp. F1116-F1123 ◽  
Author(s):  
Hyung Sub Kang ◽  
Dirk Kerstan ◽  
Long-Jun Dai ◽  
Gordon Ritchie ◽  
Gary A. Quamme
Keyword(s):  
Protein Kinase ◽  
Intracellular Signaling ◽  
Distal Tubule ◽  
Distal Convoluted Tubule ◽  
Maximal Response ◽  
Intracellular Camp ◽  
Thick Ascending Limb ◽  
Dependent Manner ◽  
Adrenergic Agonists ◽  
Concentration Dependent Manner

β-Adrenergic agonists influence electrolyte reabsorption in the proximal tubule, loop of Henle, and distal tubule. Although isoproterenol enhances magnesium absorption in the thick ascending limb, it is unclear what effect, if any, β-adrenergic agonists have on tubular magnesium handling. The effects of isoproterenol were studied in immortalized mouse distal convoluted tubule (MDCT) cells by measuring cellular cAMP formation with radioimmunoassays and Mg2+ uptake with fluorescence techniques. Intracellular free Mg2+ concentration ([Mg2+]i) was measured in single MDCT cells by using microfluorescence with mag-fura-2. To assess Mg2+uptake, MDCT cells were first Mg2+ depleted to 0.22 ± 0.01 mM by culturing in Mg2+-free media for 16 h and then placed in 1.5 mM MgCl2, and the changes in [Mg2+]i were determined. [Mg2+]i returned to basal levels, 0.53 ± 0.02 mM, with a mean refill rate, d([Mg2+]i)/d t, of 168 ± 11 nM/s. Isoproterenol stimulated Mg2+ entry in a concentration-dependent manner, with a maximal response of 252 ± 11 nM/s, at a concentration of 10−7 M, that represented a 50 ± 7% increase in uptake rate above control values. This was associated with a sixfold increase in intracellular cAMP generation. Isoproterenol-stimulated Mg2+ uptake was completely inhibited with RpcAMPS, a protein kinase A inhibitor, and U-73122, a phospholipase C inhibitor, and partially blocked by RO 31–822, a protein kinase C inhibitor. Accordingly, isoproterenol-mediated Mg2+ entry rates involve multiple intracellular signaling pathways. Aldosterone potentiated isoproterenol-stimulated Mg2+ uptake (326 ± 31 nM/s), whereas elevation of extracellular Ca2+ inhibited isoproterenol-mediated cAMP accumulation and Mg2+ uptake, 117 ± 37 nM/s. These studies demonstrate that isoproterenol stimulates Mg2+ uptake in a cell line of mouse distal convoluted tubules that is modulated by hormonal and extracellular influences.

PGE2 stimulates Mg2+ uptake in mouse distal convoluted tubule cells

1998 ◽  
Vol 275 (5) ◽  
pp. F833-F839 ◽  
Author(s):  
Long-Jun Dai ◽  
Brian Bapty ◽  
Gordon Ritchie ◽  
Gary A. Quamme
Keyword(s):  
Protein Kinase ◽  
Intracellular Signaling ◽  
Distal Convoluted Tubule ◽  
Maximal Response ◽  
Prostaglandin E ◽  
Intracellular Camp ◽  
Thick Ascending Limb ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Camp Generation

Prostaglandins have diverse effects on renal electrolyte reabsorption, inhibiting NaCl absorption in the thick ascending limb and modulating sodium and calcium transport in cortical collecting cells. It is unclear what effect, if any, prostaglandins have on tubular magnesium handling. The effects of prostaglandin E2(PGE2) were studied on immortalized mouse distal convoluted tubule (MDCT) cells by measuring cellular cAMP formation with radioimmunoassays and Mg2+ uptake with fluorescence techniques. Intracellular free Mg2+ concentration ([Mg2+]i) was measured on single MDCT cells using microfluorescence with mag-fura 2. To assess Mg2+ uptake, MDCT cells were first Mg2+ depleted to 0.22 ± 0.01 mM by culturing in Mg2+-free media for 16 h and then placed in 1.5 mM MgCl2, and the changes in [Mg2+]iwere determined. [Mg2+]ireturned to basal levels, 0.53 ± 0.02 mM, with a mean refill rate, d([Mg2+]i)/d t, of 173 ± 8 nM/s. Indomethacin, 5 μM, diminished basal Mg2+ uptake, suggesting that endogenous prostaglandins may stimulate Mg2+ entry in control cells. PGE2 stimulated Mg2+ entry in a concentration-dependent manner with maximal response of 311 ± 12 nM/s, at a concentration of 10−7 M, which represented an 80 ± 3% increase in uptake rate above control values. This was associated with a sixfold increase in intracellular cAMP generation. PGE2-stimulated Mg2+ uptake was completely inhibited with the Rp diastereoisomer of adenosine 3′,5′-cyclic monophosphothionate (Rp-cAMPS), a protein kinase A inhibitor, and U-73122, a phospholipase C inhibitor, and partially by chelerythrine, a protein kinase C inhibitor. Accordingly, PGE2-mediated Mg2+ entry rates involve multiple intracellular signaling pathways. These studies demonstrate that PGE2 stimulates Mg2+ uptake in a cell line of MDCT.

scholarly journals Insulin stimulates Mg2+ uptake in mouse distal convoluted tubule cells

1999 ◽  
Vol 277 (6) ◽  
pp. F907-F913 ◽  
Author(s):  
Long-Jun Dai ◽  
Gordon Ritchie ◽  
Brian W. Bapty ◽  
Dirk Kerstan ◽  
Gary A. Quamme
Keyword(s):  
Kinase Inhibitor ◽  
Insulin Receptors ◽  
Distal Tubule ◽  
Fold Increase ◽  
Distal Convoluted Tubule ◽  
Maximal Response ◽  
Thick Ascending Limb ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Camp Formation

Insulin has been shown to be a magnesium-conserving hormone acting, in part, through stimulation of magnesium absorption within the thick ascending limb. Although the distal convoluted tubule possesses the most insulin receptors, it is unclear what, if any, actions insulin has in the distal tubule. The effects of insulin were studied on immortalized mouse distal convoluted tubule (MDCT) cells by measuring cellular cAMP formation with radioimmunoassays and Mg2+ uptake with fluorescence techniques using mag-fura 2. To assess Mg2+ uptake, MDCT cells were first Mg2+ depleted to 0.22 ± 0.01 mM by culturing in Mg2+-free media for 16 h and then placed in 1.5 mM MgCl2, and the changes in intracellular Mg2+ concentration ([Mg2+]i) were measured with microfluorescence. [Mg2+]i returned to basal levels, 0.53 ± 0.02 mM, with a mean refill rate, d([Mg2+]i)/d t, of 164 ± 5 nM/s. Insulin stimulated Mg2+ entry in a concentration-dependent manner with maximal response of 214 ± 12 nM/s, which represented a 30 ± 5% increase in the mean uptake rate above control values. This was associated with a 2.5-fold increase in insulin-mediated cAMP generation (52 ± 3 pmol ⋅ mg protein−1 ⋅ 5 min−1). Genistein, a tyrosine kinase inhibitor, diminished insulin-stimulated Mg2+ uptake (169 ± 11 nM/s), but did not change insulin-mediated cAMP formation (47 ± 5 pmol ⋅ mg protein−1 ⋅ 5 min−1). PTH stimulates Mg2+ entry, in part, through increases in cAMP formation. Insulin and PTH increase Mg2+ uptake in an additive fashion. In conclusion, insulin mediates Mg2+ entry, in part, by a genistein-sensitive mechanism and by modifying hormone-responsive transport. These studies demonstrate that insulin stimulates Mg2+ uptake in MDCT cells and suggest that insulin acts in concert with other peptide and steroid hormones to control magnesium conservation in the distal convoluted tubule.

Endothelin activation of phospholipase D: dual modulation by protein kinase C and Ca2+

1993 ◽  
Vol 264 (5) ◽  
pp. F845-F853
Author(s):  
M. M. Friedlaender ◽  
D. Jain ◽  
Z. Ahmed ◽  
D. Hart ◽  
R. L. Barnett ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Intracellular Signaling ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Kinase C ◽  
Eta Receptor ◽  
Ca2 Channels ◽  
Stimulation Of

Previous work from this laboratory has identified an endothelin (ET) type A (ETA) receptor on cultured rat renal medullary interstitial cells (RMIC), coupled to phosphatidylinositol-specific phospholipase C (PI-PLC), dihydropyridine-insensitive receptor-operated Ca2+ channels, and phospholipase A2. The current studies explored a role for ET stimulation of phosphatidylcholine-specific phospholipase D (PC-PLD) in intracellular signaling of this cell type. ET stimulated PLD activation, as measured by phosphatidic acid (PA) or phosphatidylethanol (PEt) accumulation, in a time- and concentration-dependent manner. Inhibition of diacylglycerol (DAG) kinase by ethylene glycol dioctanoate or 6-(2)4-[(4-fluorophenyl)-phenylmethylene]-1-piperadinyl]ethy l-7-methyl-5H - thiaxolo-[3,2-alpyrimidin]-5-one (R 59022) failed to blunt PA accumulation, indicating that PLD, and not DAG, was the source of PA. Inhibition of PA phosphohydrolase (PAP) by propranolol increased late accumulation of PA, suggesting that the prevailing metabolic flow was in the direction of PA to DAG. Phorbol 12-myristate 13-acetate (PMA) augmented ET-evoked PEt accumulation, whereas downregulation of protein kinase C (PKC) obviated agonist-induced PEt production. PMA augmentation of PLD activity proceeded independent of cytosolic free Ca2+ concentration. Ca2+ derived from either intracellular or extracellular sources enhanced ET-related PEt accumulation but was without effect in PKC-downregulated cells. Collectively, these observations indicate that ET stimulates PLD production in RMIC. PKC is the major regulator of this process, with Ca2+ playing a secondary, modulatory role. In addition, these data suggest that PC-PLD is coupled to the ETA receptor.

scholarly journals Melanocortins induce interleukin 6 gene expression and secretion through melanocortin receptors 2 and 5 in 3T3-L1 adipocytes

2010 ◽  
Vol 44 (4) ◽  
pp. 225-236 ◽  
Author(s):  
Dong-Jae Jun ◽  
Kyung-Yoon Na ◽  
Wanil Kim ◽  
Dongoh Kwak ◽  
Eun-Jeong Kwon ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase ◽  
Interleukin 6 ◽  
Membrane Receptors ◽  
Mitogen Activated Protein Kinase ◽  
Melanocortin Receptors ◽  
Intracellular Camp ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Iκb Kinase

Interleukin 6 (IL6) is a pleiotropic cytokine that not only affects the immune system, but also plays an active role in many physiological events in various organs. Notably, 35% of systemic IL6 originates from adipose tissues under noninflammatory conditions. Here, we describe a previously unknown function of melanocortins in regulating Il6 gene expression and production in 3T3-L1 adipocytes through membrane receptors which are called melanocortin receptors (MCRs). Of the five MCRs that have been cloned, MC2R and MC5R are expressed during adipocyte differentiation. α-Melanocyte-stimulating hormone (α-MSH) or ACTH treatment of 3T3-L1 adipocytes induces Il6 gene expression and production in a time- and concentration-dependent manner via various signaling pathways including the protein kinase A, p38 mitogen-activated protein kinase, cJun N-terminal kinase, and IκB kinase pathways. Specific inhibition of MC2R and MC5R expression with short interfering Mc2r and Mc5r RNAs significantly attenuated the α-MSH-induced increase of intracellular cAMP and both the level of Il6 mRNA and secretion of IL6 in 3T3-L1 adipocytes. Finally, when injected into mouse tail vein, α-MSH dramatically increased the Il6 transcript levels in epididymal fat pads. These results suggest that α-MSH in addition to ACTH may function as a regulator of inflammation by regulating cytokine production.

Regulation of secretion in cultured tracheal serous cells by protein kinases A and C

1991 ◽  
Vol 261 (2) ◽  
pp. L172-L177 ◽  
Author(s):  
A. Paul ◽  
M. Mergey ◽  
D. Veissiere ◽  
B. Hermelin ◽  
G. Cherqui ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Beta Agonist ◽  
Dependent Manner ◽  
Adrenergic Agonists ◽  
Cellular Mechanisms ◽  
Concentration Dependent Manner ◽  
Beta Adrenergic ◽  
Camp Content ◽  
Beta Adrenergic Agonists ◽  
Kinase C

We recently reported that cultured gland serous cells release chondroitin sulfate proteoglycans (CSPGs) in response to beta-adrenergic agonists. In this study, we analyzed this regulatory pathway and other cellular mechanisms responsible for CSPG secretion. We show the following. 1) Isoproterenol increased CSPG secretion in a concentration-dependent manner, with maximal stimulation (50%) obtained at 10(-5) M; at this concentration, the beta-agonist also stimulated protein kinase A (PKA) by 50%, whereas it increased cellular adenosine 3',5'-cyclic monophosphate (cAMP) content by 300%. 2) Phenylephrine (10(-5) M), 4 beta-phorbol 12 beta-myristate 13 alpha-acetate (1.6 x 10(-7) M), and A23187 (10(-6) M) also stimulated CSPG secretion; this stimulation was concomitant with protein kinase C (PKC) translocation from cytosol to membrane, was blocked by sphingosine (2 x 10(-5) M), and was additive with that elicited by isoproterenol. 3) All PKC activators potentiated the isoproterenol-induced increased in cAMP accumulation without modifying the activation of PKA elicited by the beta-agonist. Our results indicate that although the signaling pathways triggered by alpha- and beta-adrenergic agonists converge at the level of adenylate cyclase in tracheal serous cells, PKA and PKC independently regulate CSPG secretion.

Abstract 2638: Potentiation of Endothelin-1-induced Ca 2+ Sensitization of Myofilament after Subarachnoid Hemorrhage

Stroke ◽  
2012 ◽  
Vol 43 (suppl_1) ◽  
Author(s):  
Yuichiro Kikkawa ◽  
Katsuya Hirano ◽  
Satoshi Matsuo ◽  
Akira Nakamizo ◽  
Tomio Sasaki
Keyword(s):  
Subarachnoid Hemorrhage ◽  
Protein Kinase ◽  
Cerebral Vasospasm ◽  
Basilar Artery ◽  
Intracellular Signaling ◽  
Regulatory Protein ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Intracellular Signaling Pathway ◽  
Endothelin 1

Introduction: Increased vascular reactiveness in response to endothelin-1 (ET-1) plays an important role in the development of cerebral vasospasm. We elucidated some mechanisms of the increased vascular reactiveness to ET-1 using the basilar artery in a rabbit subarachnoid hemorrhage (SAH) model. Material & Methods: The contractile response and the expression of regulatory protein of the isolated basilar artery were evaluated. Results: ET-1 induced greater contraction than other agonists or 118 mM K + depolarization for the extent of [Ca 2+ ] i elevation, suggesting that myofilament Ca 2+ sensitivity is a greater contributor to ET-1-induced contractions than other contractions. ET-1-induced contraction of α-toxin-permeabilized strips was significantly enhanced and sustained in SAH compared to control, suggesting that the ET-1-induced myofilament Ca 2+ sensitization was potentiated after SAH. Therefore, we investigated the intracellular signaling pathway involving Rho-associated coiled-coil protein kinase (ROCK) and protein kinase C (PKC), which are two major signaling molecules that contribute to myofilament Ca 2+ sensitization. ET-1-induced contraction of α-toxin-permeabilized control strips was blocked by inhibitors to ROCK and PKC in a concentration-dependent manner, whereas the concentration-response curve shifted to the right in SAH, suggesting that ET-1-induced myofilament Ca 2+ sensitization became less sensitive to inhibitors of ROCK and PKC after SAH. The expression of PKCα, ROCK2, PKC - potentiated phosphatase inhibitor of 17 kDa (CPI-17), and myosin phosphatase target subunit 1 (MYPT1) was upregulated and the level of phosphorylation of MYPT-1 at T853, and CPI-17 at T38 was increased after SAH. ET-1 induced an enhanced and sustained elevation of the phosphorylation of MYPT1 at both T696 and T853 after SAH. Conclusion: Ca 2+ -sensitizing effect of ET-1 on myofilaments was enhanced and prolonged after SAH. The increased expression and activity of PKCα, ROCK2, CPI-17, and MYPT1 are suggested to underlie the enhanced and prolonged Ca 2+ -sensitization. ET-1-induced potentiation of myofilament Ca 2+ sensitization may cause an increased vascular reactiveness in response to ET-1 after SAH, leading to the development of cerebral vasospasm.

scholarly journals Adenosine modulates Mg2+ uptake in distal convoluted tubule cells via A1 and A2purinoceptors

2001 ◽  
Vol 281 (6) ◽  
pp. F1141-F1147 ◽  
Author(s):  
Hyung Sub Kang ◽  
Dirk Kerstan ◽  
Long-Jun Dai ◽  
Gordon Ritchie ◽  
Gary A. Quamme
Keyword(s):  
Protein Kinase ◽  
Intracellular Signaling ◽  
Distal Tubule ◽  
Selective Inhibition ◽  
Distal Convoluted Tubule ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Intracellular Ca ◽  
Free Media ◽  
Camp Formation

tk;1Adenosine plays a role in the control of water and electrolyte reabsorption in the distal tubule. As the distal convoluted tubule is important in the regulation of renal Mg2+ balance, we determined the effects of adenosine on cellular Mg2+ uptake in this segment. The effect of adenosine was studied on immortalized mouse distal convoluted tubule (MDCT) cells, a model of the intact distal convoluted tubule. The rate of Mg2+ uptake was measured with fluorescence techniques using mag-fura 2. To assess Mg2+ uptake, MDCT cells were first Mg2+ depleted to 0.22 ± 0.01 mM by being cultured in Mg2+-free media for 16 h and then placed in 1.5 mM MgCl2; next, changes in intracellular Mg2+ concentration ([Mg2+]i) were determined. [Mg2+]i returned to basal levels, 0.53 ± 0.02 mM, with a mean refill rate, d([Mg2+]i)/d t, of 137 ± 16 nM/s. Adenosine stimulates basal Mg2+ uptake by 41 ± 10%. The selective A1 purinoceptor agonist N 6-cyclopentyladenosine (CPA) increased intracellular Ca2+ and decreased parathyroid hormone (PTH)-stimulated cAMP formation and PTH-mediated Mg2+uptake. On the other hand, the selective A2 receptor agonist 2-[ p-(2-carbonyl-ethyl)-phenylethylamino]-5′- N-ethylcarboxamidoadenosine (CGS) stimulated Mg2+ entry in a concentration-dependent fashion. CGS increased cAMP formation and the protein kinase A inhibitor RpcAMPS inhibited CGS-stimulated Mg2+ uptake. Selective inhibition of phospholipase C, protein kinase C, or mitogen-activated protein kinase enzyme cascades with U-73122, Ro-31-8220, and PD-98059, respectively, diminished A2 agonist-mediated Mg2+ entry. Aldosterone potentiated CGS-mediated Mg2+ entry, and elevation of extracellular Ca2+ diminished CGS-responsive cAMP formation and Mg2+ uptake. Accordingly, MDCT cells possess both A1 and A2 purinoceptor subtypes with intracellular signaling typical of these respective receptors. We conclude that adenosine has dual effects on Mg2+ uptake in MDCT cells through separate A1 and A2purinoceptor pathways.

scholarly journals Growth Promotion or Osmotic Stress Response: How SNF1-Related Protein Kinase 2 (SnRK2) Kinases Are Activated and Manage Intracellular Signaling in Plants

Plants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1443
Author(s):  
Yoshiaki Kamiyama ◽  
Sotaro Katagiri ◽  
Taishi Umezawa
Keyword(s):  
Protein Kinase ◽  
Plant Growth ◽  
Osmotic Stress ◽  
Protein Function ◽  
Intracellular Signaling ◽  
Growth Promotion ◽  
Research Field ◽  
Dependent Manner ◽  
Related Protein ◽  
Wide Range

Reversible phosphorylation is a major mechanism for regulating protein function and controls a wide range of cellular functions including responses to external stimuli. The plant-specific SNF1-related protein kinase 2s (SnRK2s) function as central regulators of plant growth and development, as well as tolerance to multiple abiotic stresses. Although the activity of SnRK2s is tightly regulated in a phytohormone abscisic acid (ABA)-dependent manner, recent investigations have revealed that SnRK2s can be activated by group B Raf-like protein kinases independently of ABA. Furthermore, evidence is accumulating that SnRK2s modulate plant growth through regulation of target of rapamycin (TOR) signaling. Here, we summarize recent advances in knowledge of how SnRK2s mediate plant growth and osmotic stress signaling and discuss future challenges in this research field.

scholarly journals Complex effects of kinase localization revealed by compartment-specific regulation of protein kinase A activity

2021 ◽  
Author(s):  
Rebecca LaCroix ◽  
Benjamin Lin ◽  
Andre Levchenko
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Kinase Activity ◽  
Single Cells ◽  
Regulatory Subunit ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Specific Regulation ◽  
Kinase A

SummaryKinase activity in signaling networks frequently depends on regulatory subunits that can both inhibit activity by interacting with the catalytic subunits and target the kinase to distinct molecular partners and subcellular compartments. Here, using a new synthetic molecular interaction system, we show that translocation of a regulatory subunit of the protein kinase A (PKA-R) to the plasma membrane has a paradoxical effect on the membrane kinase activity. It can both enhance it at lower translocation levels, even in the absence of signaling inputs, and inhibit it at higher translocation levels, suggesting its role as a linker that can both couple and decouple signaling processes in a concentration-dependent manner. We further demonstrate that superposition of gradients of PKA-R abundance across single cells can control the directionality of cell migration, reversing it at high enough input levels. Thus complex in vivo patterns of PKA-R localization can drive complex phenotypes, including cell migration.

scholarly journals Sphingosine Kinase as a Regulator of Calcium Entry through Autocrine Sphingosine 1-Phosphate Signaling in Thyroid FRTL-5 Cells

Endocrinology ◽  
2009 ◽  
Vol 150 (11) ◽  
pp. 5125-5134 ◽  
Author(s):  
Dan Gratschev ◽  
Christoffer Löf ◽  
Jari Heikkilä ◽  
Anders Björkbom ◽  
Pramod Sukumaran ◽  
...  
Keyword(s):  
Intracellular Signaling ◽  
Sphingosine Kinase ◽  
Calcium Entry ◽  
Dominant Negative ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Entry Pathway ◽  
Sphingosine 1 Phosphate ◽  
S1p Receptor ◽  
In Cells

Calcium entry is one of the main regulators of intracellular signaling. Here, we have described the importance of sphingosine, sphingosine kinase 1 (SK1), and sphingosine 1-phosphate (S1P) in regulating calcium entry in thyroid FRTL-5 cells. In cells incubated with the phosphatase inhibitor calyculin A, which evokes calcium entry without mobilizing sequestered intracellular calcium, sphingosine inhibited calcium entry in a concentration-dependent manner. Furthermore, inhibiting SK1 or the ATP-binding cassette ABCC1 multidrug transporter attenuated calcium entry. The addition of exogenous S1P restored calcium entry. Neither sphingosine nor inhibition of SK1 attenuated thapsigargin-evoked calcium entry. Blocking S1P receptor 2 or phospholipase C attenuated calcium entry, whereas blocking S1P receptor 3 did not. Overexpression of wild-type SK1, but not SK2, enhanced calyculin-evoked calcium entry compared with mock-transfected cells, whereas calcium entry was decreased in cells transfected with the dominant-negative G82D SK1 mutant. Exogenous S1P restored calcium entry in G82D cells. Our results suggest that the calcium entry pathway is blocked by sphingosine and that activation of SK1 and the production of S1P, through an autocrine mechanism, facilitate calcium entry through activation of S1P receptor 2. This is a novel mechanism by which the sphingosine-S1P rheostat regulates cellular calcium homeostasis.

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