Phospholipase C-γ Is Required for Agonist-Induced Ca2+ Entry

Patterson, Randen L.; Rossum, Damian B. van; Ford, Diana L.; Hurt, K. Joseph; Bae, Sun Sik; Suh, Pann Ghill; Kurosaki, Tomohiro; Snyder, Solomon H.; Gill, Donald L.

doi:10.1016/s0092-8674(02)01045-0

Cited by 176 publications

(199 citation statements)

References 59 publications

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“…Activation of the lipase activity of PLC c2 leads to an increase in the IP 3 concentration, leading subsequently to an increase in the Ca 2+ concentration (Berridge 1993;Carpenter and Ji 1999;Patterson et al 2002;Nishida et al 2003). However, the treatment of PC12 cells with forskolin increases the intracellular concentration of cAMP but not Ca 2+ (data not shown), suggesting that PLCc2 mediates the phosphorylation of CREB in a Ca 2+ -independent manner following the activation of the cAMP signaling pathway.…”

Section: Discussionmentioning

confidence: 90%

“…Interestingly, siPLCc2 completely abolished the activation of CREB induced by treatment of cells with ionomycin, indicating that PLCc2 is essential for the activation of CREB by Ca 2+ signaling in PC12 cells. A previous report has demonstrated that PLCc2 amplifies the Ca 2+ signaling (Patterson et al 2002;Nishida et al 2003). Additionally, numerous studies have indicated that an increase in the intracellular Ca 2+ concentration leads to activation of CaMKs and PKCs (Nishizuka 1988;Schulman et al 1992;Hook and Means 2001;Elgersma et al 2004;Griffith 2004).…”

Section: Discussionmentioning

confidence: 98%

“…We determined that these sequences are unique to the corresponding genes by a BLAST search of the GenBank TM database. The target sequence for PLCc1 was determined in a previous report (Patterson et al 2002). We constructed pSUPER-GFP, pSUPER-PLCc1 and pSUPER-PLCc2 using GeneTailor TM Site-Directed Mutagenesis System (Invitrogen, CA).…”

Section: Rnaimentioning

confidence: 99%

“…We characterized the ability of siPLCc1 and siPLCc2 to reduce the expression of PLCc1 and 2, using siGFP as a negative control. Importantly, a previous report has shown that both PLCc1 and PLCc2 are expressed and functional in PC12 cells (Patterson et al 2002). We first transiently transfected pmyc-PLCc1 with pSU-PER, pSUPER-GFP, pSUPER-PLCc1 or pSU-PER-PLCc2 into PC12 cells and examined the expression level of exogenous PLCc1 (myc-PLCc1) by Western blot analysis.…”

Section: Siplcc1 and Siplcc2 Reduce Plcc1 Or Plcc2 Expression Respecmentioning

confidence: 99%

“…The PLC isozymes have been divided into three families: PLC-b, PLC-c and PLC-d. PLC-b is activated by G proteinactivated receptors (GPCR), whereas PLC-c isoforms (PLC-c1 and PLC-c2) are activated by tyrosine kinase receptors and nonreceptor tyrosine kinases (Rhee and Choi 1992;Berridge 1993;Liao et al 1993;Park et al 1993;Rebecchi and Pentyala 2000). Importantly, PLCcs also potentiate Ca 2+ responses in a lipase-independent manner (Patterson et al 2002;Nishida et al 2003). Additionally, recent studies have demonstrated that PLCcs function as downstream signal transducers of PKAinduced signaling pathways (Yu et al 1996).…”

Section: Introductionmentioning

confidence: 99%

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PLCγ2 Activates CREB-dependent Transcription in PC12 Cells Through Phosphorylation of CREB at Serine 133

et al. 2005

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The cAMP and Ca 2+ signaling pathways activate the transcription factor CREB through its phosphorylation at Serine 133. Activation of CREB is involved in the regulation of various biological phenomena. To understand further the mechanisms of the regulation of CREB activity in response to activation of the cAMP and Ca 2+ signaling pathways, we examined the roles of PLCcs in CREB activation in PC12 cells. siRNA-mediated reduction of the expression of PLCc2, but not PLCc1, inhibited both the phosphorylation of CREB at S133 and the activation of CREB-dependent transcription following treatment of cells with forskolin or ionomycin, which increases the intracellular concentrations of cAMP or Ca 2+ , respectively. Importantly, the siRNA targeting PLCc2 completely abolished CREB activation by Ca 2+ signaling but not by cAMP signaling. These results suggest that PLCc2 functions as an essential signal transducer leading to CREB activation in response to activation of the Ca 2+ signaling pathway and that the cAMP signaling pathway might activate CREB through phosphorylation of CREB by PKA and another signaling pathway mediated by PLCc2.

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Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 98%

Section: Rnaimentioning

confidence: 99%

Section: Siplcc1 and Siplcc2 Reduce Plcc1 Or Plcc2 Expression Respecmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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PLCγ2 Activates CREB-dependent Transcription in PC12 Cells Through Phosphorylation of CREB at Serine 133

et al. 2005

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High‐Speed Microwave‐Assisted Synthesis of the Trifluoromethylpyrazol‐Derived Canonical Transient Receptor Potential (TRPC) Channel Inhibitor Pyr3

Glasnov

Kappe

2009

ChemMedChem

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SR‐BI regulates the synergistic mast cell response by modulating the plasma membrane‐associated cholesterol pool

Capellmann,

Kauffmann,

Arock

et al. 2024

Eur J Immunol

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The high‐affinity IgE receptor FcεRI is the mast cell (MC) receptor responsible for the involvement of MCs in IgE‐associated allergic disorders. Activation of the FcεRI is achieved via crosslinking by multivalent antigen (Ag) recognized by IgE resulting in degranulation and proinflammatory cytokine production. In comparison to the T‐ and B‐cell receptor complexes, for which several co‐receptors orchestrating the initial signaling events have been described, information is scarce about FcεRI‐associated proteins. Additionally, it is unclear how FcεRI signaling synergizes with input from other receptors and how regulators affect this synergistic response. We found that the HDL receptor SR‐BI (gene name: Scarb1/SCARB1) is expressed in MCs, functionally associates with FcεRI, and regulates the plasma membrane cholesterol content in cholesterol‐rich plasma membrane nanodomains. This impacted the activation of MCs upon co‐stimulation of the FcεRI with receptors known to synergize with FcεRI signaling. Amongst them, we investigated the co‐activation of the FcεRI with the receptor tyrosine kinase KIT, the IL‐33 receptor, and GPCRs activated by adenosine or PGE2. Scarb1‐deficient bone marrow‐derived MCs showed reduced cytokine secretion upon co‐stimulation conditions suggesting a role for plasma membrane‐associated cholesterol regulating respective MC activation. Mimicking Scarb1 deficiency by cholesterol depletion employing MβCD, we identified PKB and PLCγ1 as cholesterol‐sensitive proteins downstream of FcεRI activation in bone marrow‐derived MCs. When MCs were co‐stimulated with stem cell factor (SCF) and Ag, PLCγ1 activation was boosted, which could be mitigated by cholesterol depletion and SR‐BI inhibition. Similarly, SR‐BI inhibition attenuated the synergistic response to PGE2 and anti‐IgE in the human ROSAKIT WT MC line, suggesting that SR‐BI is a crucial regulator of synergistic MC activation.

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Phospholipase C-γ Is Required for Agonist-Induced Ca2+ Entry

Cited by 176 publications

References 59 publications

PLCγ2 Activates CREB-dependent Transcription in PC12 Cells Through Phosphorylation of CREB at Serine 133

PLCγ2 Activates CREB-dependent Transcription in PC12 Cells Through Phosphorylation of CREB at Serine 133

High‐Speed Microwave‐Assisted Synthesis of the Trifluoromethylpyrazol‐Derived Canonical Transient Receptor Potential (TRPC) Channel Inhibitor Pyr3

SR‐BI regulates the synergistic mast cell response by modulating the plasma membrane‐associated cholesterol pool

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