Long Lasting Inhibition of Adenylyl Cyclase Selectively Mediated by Inositol 1,4,5-Trisphosphate-evoked Calcium Release

Dyer, Jeanette L.; Liu, Yingjie; Huerga, Irene Pino de la; Taylor, Colin W.

doi:10.1074/jbc.m410045200

Cited by 10 publications

(16 citation statements)

References 51 publications

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“…1A). The response was slightly more sensitive to AVP than were Ca 2+ release and regulation of Ca 2+ entry (EC 50 20 nM [5,6,28] H-AA release declined, but comparison of the responses to brief (3 min) and sustained (9 min) additions shows that the effect of AVP was both reversible and persisted for at least 9 min (Fig. 1B).…”

Section: Resultsmentioning

confidence: 99%

“…] i A7r5 cells grown on 96-well plates were loaded with fluo 4 and fluorescence measured using a FlexStation automated fluorescence plate reader and then calibrated to [Ca 2+ ] i as reported previously [28]. ii.…”

Section: +mentioning

confidence: 99%

“…H-AA release A7r5 cells (originally from the American Type Culture Collection) were cultured in Dulbecco's modified Eagle's medium (DMEM) supplemented with 10% fetal bovine serum, 3.8 mM L L-glutamine and 0.9% non-essential amino acids [28]. For 3 H-AA release assays, cells grown to 70% confluence in 35-mm dishes were incubated for 24 h in medium containing 0.1% fetal bovine serum and supplemented with 3 H-AA (1 lCi/ml).…”

Section: Measurement Ofmentioning

confidence: 99%

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Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca²⁺‐stimulated phospholipase A₂

Liu

Taylor

2006

FEBS Letters

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Section: Resultsmentioning

confidence: 99%

Section: +mentioning

confidence: 99%

Section: Measurement Ofmentioning

confidence: 99%

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Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca²⁺‐stimulated phospholipase A₂

Liu

Taylor

2006

FEBS Letters

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“…It became untenable to think of responses to graded changes in the intensity of the extracellular stimulus as being simply encoded in graded changes in global cytosolic Ca 2þ concentration. Ca 2þ entering the cytosol via one channel can regulate different proteins to Ca 2þ entering via another (Berridge et al 2000;Dyer et al 2005;Willoughby and Cooper 2007). Hence, the spatial organization of the changes in cytosolic Ca 2þ concentration profoundly affects the physiological response, and that presents many opportunities for delivering different Ca 2þ signals in response to different stimuli or different stimulus intensities.…”

Section: Ip 3 Receptorsmentioning

confidence: 99%

“…These observations and accumulating evidence that local Ca 2þ signals can selectively regulate local events (Rizzuto et al 1993;Berridge et al 2000;Dyer et al 2005;Willoughby and Cooper 2007) prompted a re-assessment of the ways in which Ca 2þ signals convey information. It became untenable to think of responses to graded changes in the intensity of the extracellular stimulus as being simply encoded in graded changes in global cytosolic Ca 2þ concentration.…”

Section: Ip 3 Receptorsmentioning

confidence: 99%

IP3 Receptors: Toward Understanding Their Activation

Taylor¹,

Tovey²

2010

Cold Spring Harbor Perspectives in Biology

260

190

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Inositol 1,4,5-trisphosphate receptors (IP 3 R) and their relatives, ryanodine receptors, are the channels that most often mediate Ca 2þ release from intracellular stores. Their regulation by Ca 2þ allows them also to propagate cytosolic Ca 2þ signals regeneratively. This brief review addresses the structural basis of IP 3 R activation by IP 3 and Ca 2þ . IP 3 initiates IP 3 R activation by promoting Ca 2þ binding to a stimulatory Ca 2þ -binding site, the identity of which is unresolved. We suggest that interactions of critical phosphate groups in IP 3 with opposite sides of the clam-like IP 3 -binding core cause it to close and propagate a conformational change toward the pore via the adjacent N-terminal suppressor domain. The pore, assembled from the last pair of transmembrane domains and the intervening pore loop from each of the four IP 3 R subunits, forms a structure in which a luminal selectivity filter and a gate at the cytosolic end of the pore control cation fluxes through the IP 3 R.

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Effects of protease-activated receptors (PARs) on intracellular calcium dynamics of acinar cells in rat lacrimal glands

Oikawa

Saino

Kimura

et al. 2013

Histochem Cell Biol

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Protease-activated receptors (PARs) represent a novel class of seven transmembrane domain G-protein coupled receptors, which are activated by proteolytic cleavage. PARs are present in a variety of cells and have been prominently implicated in the regulation of a number of vital functions. Here, lacrimal gland acinar cell responses to PAR activation were examined, with special reference to intracellular Ca(2+) concentration ([Ca(2+)]i) dynamics. In the present study, detection of acinar cell mRNA specific to known PAR subtypes was determined by reverse transcriptase polymerase chain reaction. Only PAR2 mRNA was detected in acinar cells of lacrimal glands. Both trypsin and a PAR2-activating peptide (PAR2-AP), SLIGRL-NH2, induced an increase in [Ca(2+)]i in acinar cells. The removal of extracellular Ca(2+) and the use of Ca(2+) channel blockers did not inhibit PAR2-AP-induced [Ca(2+)]i increases. Furthermore, U73122 and xestospongin C failed to inhibit PAR2-induced increases in [Ca(2+)]i. The origin of the calcium influx observed after activated PAR2-induced Ca(2+) release from intracellular Ca(2+) stores was also evaluated. The NO donor, GEA 3162, mimicked the effects of PAR2 in activating non-capacitative calcium entry (NCCE). However, both calyculin A (100 nM) and a low concentration of Gd(3+) (5 μM) did not completely block the PAR2-AP-induced increase in [Ca(2+)]i. These findings indicated that PAR2 activation resulted primarily in Ca(2+) mobilization from intracellular Ca(2+) stores and that PAR2-mediated [Ca(2+)]i changes were mainly independent of IP3. RT-PCR indicated that TRPC 1, 3 and 6, which play a role in CCE and NCCE, are expressed in acinar cells. We suggest that PAR2-AP differentially regulates both NCCE and CCE, predominantly NCCE. Finally, our results suggested that PAR2 may function as a key receptor in calcium-related cell homeostasis under pathophysiological conditions such as tissue injury or inflammation.

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Long Lasting Inhibition of Adenylyl Cyclase Selectively Mediated by Inositol 1,4,5-Trisphosphate-evoked Calcium Release

Cited by 10 publications

References 51 publications

Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca²⁺‐stimulated phospholipase A₂

Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca²⁺‐stimulated phospholipase A₂

IP3 Receptors: Toward Understanding Their Activation

Effects of protease-activated receptors (PARs) on intracellular calcium dynamics of acinar cells in rat lacrimal glands

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Long Lasting Inhibition of Adenylyl Cyclase Selectively Mediated by Inositol 1,4,5-Trisphosphate-evoked Calcium Release

Cited by 10 publications

References 51 publications

Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca2+‐stimulated phospholipase A2

Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca2+‐stimulated phospholipase A2

IP3 Receptors: Toward Understanding Their Activation

Effects of protease-activated receptors (PARs) on intracellular calcium dynamics of acinar cells in rat lacrimal glands

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Product

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Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca²⁺‐stimulated phospholipase A₂

Stimulation of arachidonic acid release by vasopressin in A7r5 vascular smooth muscle cells mediated by Ca²⁺‐stimulated phospholipase A₂