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

Neuroendocrinology. 2007;86(4):243-8. doi: 10.1159/000107795. Epub 2007 Aug 30.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Calcium Signaling / genetics
  • Calcium Signaling / physiology*
  • Humans
  • Neurons / enzymology*
  • Neurons / physiology
  • Neurosecretory Systems / cytology
  • Neurosecretory Systems / enzymology*
  • Neurosecretory Systems / physiology
  • Phosphoinositide Phospholipase C / genetics
  • Phosphoinositide Phospholipase C / physiology*
  • Protein Kinase C / genetics
  • Protein Kinase C / physiology*


  • Protein Kinase C
  • PLCH1 protein, human
  • Phosphoinositide Phospholipase C