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

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

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

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)243-248
Number of pages6
JournalNeuroendocrinology
Volume86
Issue number4
DOIs
Publication statusPublished - Nov 2007

Keywords

  • 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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