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Phospholipase C-η enzymes as putative protein kinase C and Ca2+ signalling components in neuronal and neuroendocrine tissues

Research output: Contribution to journalArticle



Alan James Stewart, K Morgan, C Farquharson, RP Millar

School/Research organisations


Phosphoinositol-specific phospholipase C enzymes (PLCs) are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C activation. A sixth class of phosphoinositol-specific PLC with a novel domain structure, PLC-eta (PLCeta) has recently been discovered in mammals. Recent research, reviewed here, shows that this class consists of two enzymes, PLCeta1 and PLCeta2. Both enzymes hydrolyze phosphatidylinositol 4,5-bisphosphate and are more sensitive to Ca2+ than other PLC isozymes and are likely to mediate G-protein-coupled receptor (GPCR) signalling pathways. Both enzymes are expressed in neuron-enriched regions, being abundant in the brain. We demonstrate that they are also expressed in neuroendocrine cell lines. PLCeta enzymes therefore represent novel proteins influencing intracellular Ca2+ dynamics and protein kinase C activation in the brain and neuroendocrine systems as putative mediation of GPCR regulation.


Original languageEnglish
Pages (from-to)243-248
Number of pages6
Issue number4
Publication statusPublished - Nov 2007

    Research areas

  • Ca2+ Signalling, Protein Kinase C, Receptor-Mediated Signalling, Neuroendocrine, Neuron, Ca2+ signalling, protein kinase C, receptor-mediated signalling, neuroendocrine, neuron, SYNAPTIC VESICLE EXOCYTOSIS, PLECKSTRIN HOMOLOGY DOMAIN, G-BETA-GAMMA, TRANSCRIPTIONAL ACTIVATION, MOLECULAR-CLONING, RECEPTOR, CELLS, SECRETION, BIND, IDENTIFICATION

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