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dc.contributor.authorLitjens, T.-
dc.contributor.authorNguyen, T.-
dc.contributor.authorCastro Kraftchenko, J.-
dc.contributor.authorAromataris, E.-
dc.contributor.authorJones, L.-
dc.contributor.authorBarritt, G.-
dc.contributor.authorRychkov, G.-
dc.identifier.citationBiochemical Journal, 2007; 405(2):269-276-
dc.description.abstractRepetitive hormone-induced changes in concentration of free cytoplasmic Ca2+ in hepatocytes require Ca2+ entry through receptor-activated Ca2+ channels and SOCs (store-operated Ca2+ channels). SOCs are activated by a decrease in Ca2+ concentration in the intracellular Ca2+ stores, but the molecular components and mechanisms are not well understood. Some studies with other cell types suggest that PLC-gamma (phospholipase C-gamma) is involved in the activation of receptor-activated Ca2+ channels and/or SOCs, independently of PLC-gamma-mediated generation of IP3 (inositol 1,4,5-trisphosphate). The nature of the Ca2+ channels regulated by PLC-gamma has not been defined clearly. The aim of the present study was to determine if PLC-gamma is required for the activation of SOCs in liver cells. Transfection of H4IIE cells derived from rat hepatocytes with siRNA (short interfering RNA) targeted to PLC-gamma1 caused a reduction (by approx. 70%) in the PLC-gamma1 protein expression, with maximal effect at 72-96 h. This was associated with a decrease (by approx. 60%) in the amplitude of the I(SOC) (store-operated Ca2+ current) developed in response to intracellular perfusion with either IP(3) or thapsigargin. Knockdown of STIM1 (stromal interaction molecule type 1) by siRNA also resulted in a significant reduction (approx. 80% at 72 h post-transfection) of the I(SOC) amplitude. Immunoprecipitation of PLC-gamma1 and STIM1, however, suggested that under the experimental conditions these proteins do not interact with each other. It is concluded that the PLC-gamma1 protein, independently of IP3 generation and STIM1, is required to couple endoplasmic reticulum Ca2+ release to the activation of SOCs in the plasma membrane of H4IIE liver cells.-
dc.description.statementofresponsibilityTom Litjens, Than Nguyen, Joel Castro, Edoardo C. Aromataris, Lynette Jones, Greg J. Barritt And Grigori Y. Rychkov-
dc.publisherPortland Press-
dc.rightsCopyright © 2007 Biochemical Society-
dc.subjectCells, Cultured-
dc.subjectInositol 1,4,5-Trisphosphate-
dc.subjectPhosphatidylinositol 4,5-Diphosphate-
dc.subjectCalcium Channels-
dc.subjectMembrane Glycoproteins-
dc.subjectRNA, Small Interfering-
dc.subjectPhospholipase C gamma-
dc.subjectStromal Interaction Molecule 1-
dc.titlePhospholipase C-γ1 is required for the activation of store-operated Ca²⁺ channels in liver cells-
dc.title.alternativePhospholipase C-gamma1 is required for the activation of store-operated Ca(2+) channels in liver cells-
dc.typeJournal article-
dc.identifier.orcidCastro Kraftchenko, J. [0000-0002-5781-2224]-
dc.identifier.orcidAromataris, E. [0000-0001-7238-5833]-
dc.identifier.orcidRychkov, G. [0000-0002-2788-2977]-
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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