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

Alan J Stewart, Kevin Morgan, Colin Farquharson, Robert P Millar

Research output: Contribution to journalArticlepeer-review

Abstract

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)243-8
Number of pages6
JournalNeuroendocrinology
Volume86
Issue number4
DOIs
Publication statusPublished - 2007

Keywords

  • Animals
  • Calcium Signaling
  • Humans
  • Neurons
  • Neurosecretory Systems
  • Phosphoinositide Phospholipase C
  • Protein Kinase C

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