Cyclic AMP directs IP3-evoked Ca2+ signalling to different intracellular Ca2+ stores

Tovey, Stephen C.; Taylor, Colin W.

doi:10.1242/jcs.126144

Cited by 20 publications

(29 citation statements)

References 44 publications

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“…Since localization in lipid rafts can impact Ca 2+ signaling by influencing G-protein activation and IP 3 production, 21,22 the effect of LA on CD36 and GPR120 membrane distribution was explored. Treatment of human or mice fungiform TBC for 20 min with LA did not alter protein levels of CD36 and GPR120 (not shown) but did cause changes in membrane distribution.…”

Section: Resultsmentioning

confidence: 99%

“…This effect is greatly exaggerated by consumption of a HFD, which also decreases total CD36, probably reflecting the effect of chronic exposure to excess FA. Localization in membrane rafts as compared to non raft detergent-soluble domains would modulate IP3 release and Ca 2+ signaling, 21,22 events integral to TBC CD36 and GPR120 function. In addition to modulating CD36 membrane localization, FA exposure would regulate CD36 internalization and ubiquitination 30 possibly involving the activation of CD36 associated src kinases.…”

Section: Discussionmentioning

confidence: 99%

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CD36- and GPR120-Mediated Ca2+ Signaling in Human Taste Bud Cells Mediates Differential Responses to Fatty Acids and Is Altered in Obese Mice

et al. 2014

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Background & Aims It is important to increase our understanding of gustatory detection of dietary fat and its contribution to fat preference. We studied the roles of the fat taste receptors CD36 and GPR120 and their interactions via Ca2+ signaling in fungiform taste bud cells (TBC). Methods We measured Ca2+ signaling in human TBC, transfected with small interfering RNAs (siRNAs) against mRNAs encoding CD36 and GPR120 (or control siRNAs). We also studied Ca2+ signaling in TBC from CD36−/− mice and from wild-type lean and obese mice. Additional studies were conducted with mouse enteroendocrine cell line STC-1 that express GPR120 and stably transfected with human CD36. We measured release of serotonin and GLP-1 from human and mice TBC in response to CD36 and GPR120 activation. Results High concentrations of linoleic acid induced Ca2+ signaling via CD36 and GPR120 in human and mice TBC as well as in STC-1 cells, whereas low concentrations induced Ca2+ signaling via only CD36. Incubation of human and mice fungiform TBC with lineoleic acid downregulated CD36 and upregulated GPR120 in membrane lipid rafts. Obese mice had decreased spontaneous preference for fat. Fungiform TBC from obese mice had reduced Ca2+ and serotonin responses but increased release of GLP1, along with reduced levels of CD36 and increased levels of GPR120 in lipid rafts. Conclusions CD36 and GPR120 have non-overlapping roles in TBC signaling during oro-gustatory perception of dietary lipids; these are differentially regulated by obesity.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

CD36- and GPR120-Mediated Ca2+ Signaling in Human Taste Bud Cells Mediates Differential Responses to Fatty Acids and Is Altered in Obese Mice

et al. 2014

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“…Possibly the presence of two such homologs reflects the R. baltica compartmentalized cell structure with two types of membranes, the CM and the ICM. It is interesting to suggest that as in eukaryotes, lipid signaling might be a mechanism for intercompartmental signaling in R. baltica [80]. …”

Section: Resultsmentioning

confidence: 99%

Bioinformatic analyses of integral membrane transport proteins encoded within the genome of the planctomycetes species, Rhodopirellula baltica

Paparoditis

Västermark

et al. 2014

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Rhodopirellula baltica (R. baltica) is a Planctomycete, known to have intracellular membranes. Because of its unusual cell structure and ecological significance, we have conducted comprehensive analyses of its transmembrane transport proteins. The complete proteome of R. baltica was screened against the Transporter Classification Database (TCDB) to identify recognizable integral membrane transport proteins. 342 proteins were identified with a high degree of confidence, and these fell into several different classes. R. baltica encodes in its genome channels (12%), secondary carriers (33%), and primary active transport proteins (41%) in addition to classes represented in smaller numbers. Relative to most non-marine bacteria, R. baltica possesses a larger number of sodium-dependent symporters but fewer proton-dependent symporters, and it has dimethylsulfoxide (DMSO) and trimethyl-amine-oxide (TMAO) reductases, consistent with its Na+-rich marine environment. R. baltica also possesses a Na+-translocating NADH:quinone dehydrogenase (Na+-NDH), a Na+ efflux decarboxylase, two Na+-exporting ABC pumps, two Na+-translocating F-type ATPases, two Na+:H+ antiporters and two K+:H+ antiporters. Flagellar motility probably depends on the sodium electrochemical gradient. Surprisingly, R. baltica also has a complete set of H+-translocating electron transport complexes similar to those present in β-proteobacteria and eukaryotic mitochondria. The transport proteins identified proved to be typical of the bacterial domain with little or no indication of the presence of eukaryotic-type transporters. However, novel functionally uncharacterized multispanning membrane proteins were identified, some of which are found only in Rhodopirellula species, but others of which are widely distributed in bacteria. The analyses lead to predictions regarding the physiology, ecology and evolution of R. baltica.

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“…), and high concentrations of cAMP sensitize IP 3 Rs to IP 3 via a direct effect (Tovey et al . ; Tovey & Taylor, ). Second, IP 3 Rs are more abundant in atria and the SAN compared to the ventricle (Lipp et al .…”

Section: Discussionmentioning

confidence: 99%

Regulation of calcium clock‐mediated pacemaking by inositol‐1,4,5‐trisphosphate receptors in mouse sinoatrial nodal cells

Kapoor

Tran

Kang

et al. 2015

The Journal of Physiology

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Key pointsr Inositol-1,4,5-trisphosphate receptors (IP 3 Rs) modulate pacemaking in embryonic heart, but their role in adult sinoatrial node (SAN) pacemaking is uncertain. r These findings support development of IP 3 signalling modulators for regulation of heart rate, particularly in heart failure where IP 3 Rs are upregulated.Abstract Cardiac pacemaking initiated by the sinus node is attributable to the interplay of several membrane currents. These include the depolarizing 'funny current' (I f ) and the sodium-calcium exchanger current (I NCX ). The latter is activated by ryanodine receptor (RyR)-mediated calcium (Ca 2+ ) release from the sarcoplasmic reticulum (SR). Another SR Ca 2+ release channel, the inositol-1,4,5-triphosphate receptor (IP 3 R), has been implicated in the generation of spontaneous Ca 2+ release in atrial and ventricular cardiomyocytes. Whether IP 3 R-mediated Ca 2+ release also influences SAN automaticity is controversial, in part due to the confounding influence of periodic Ca 2+ flux through the sarcolemma accompanying each beat. We took advantage of atrial-specific sodium-calcium exchanger (NCX) knockout (KO) SAN cells to study the influence of IP 3 signalling on cardiac pacemaking in a system where periodic intracellular Ca 2+ cycling persists despite the absence of depolarization or Ca 2+ flux across the sarcolemma. We recorded confocal line scans of spontaneous Ca 2+ release in WT and NCX KO SAN cells in the presence or absence of an IP 3 R blocker (2-aminoethoxydiphenyl borate, 2-APB), or during block of IP 3 production by the phospholipase C inhibitor U73122. 2-APB and U73122 decreased the frequency of spontaneous Ca 2+ transients and waves in WT and NCX KO cells, respectively. Alternatively, increased IP 3 production induced by phenylephrine increased Ca 2+ transient and wave frequency. We conclude that IP 3 R-mediated SR Ca 2+ flux is crucial for initiating and modulating the RyR-mediated Ca 2+ cycling that regulates SAN pacemaking. Our results in NCX KO SAN cells also demonstrate that RyRs, but not NCX, are required for IP 3 to modulate Ca 2+ clock frequency.

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Cyclic AMP directs IP3-evoked Ca2+ signalling to different intracellular Ca2+ stores

Cited by 20 publications

References 44 publications

CD36- and GPR120-Mediated Ca2+ Signaling in Human Taste Bud Cells Mediates Differential Responses to Fatty Acids and Is Altered in Obese Mice

CD36- and GPR120-Mediated Ca2+ Signaling in Human Taste Bud Cells Mediates Differential Responses to Fatty Acids and Is Altered in Obese Mice

Bioinformatic analyses of integral membrane transport proteins encoded within the genome of the planctomycetes species, Rhodopirellula baltica

Regulation of calcium clock‐mediated pacemaking by inositol‐1,4,5‐trisphosphate receptors in mouse sinoatrial nodal cells

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