Activation of mitogen-activated protein kinase (MAPK) by GnRH is cell-context dependent

Mol Cell Endocrinol. 2006 Jun 27;252(1-2):184-90. doi: 10.1016/j.mce.2006.03.035. Epub 2006 May 8.

Abstract

The interaction of GnRH with its cognate receptor (GnRHR) in pituitary gonadotropes includes activation of Gq/G11 and phospholipase Cbeta (PLCbeta), which generates the second messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG), which are required for Ca2+ mobilization and PKC isoforms activation. Activation of PKC in pituitary gonadotropes leads to the activation of the major members of the mitogen-activated protein kinase superfamily (MAPK), namely: extracellular signal-regulated kinase (ERK), jun-N-terminal Kinase (JNK) and p38MAPK. The above pathways mediate GnRH-induced gonadotropin release and synthesis. Here we summarise the diverse mechanisms utilized by GnRH to activate the MAPK members and show that they depend on "cell-context".

Publication types

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

MeSH terms

  • Animals
  • Enzyme Activation
  • Gonadotropin-Releasing Hormone / physiology*
  • Gonadotropins / genetics
  • Mammals
  • Mitogen-Activated Protein Kinases / metabolism*
  • Pituitary Gland / enzymology
  • Protein Subunits / genetics
  • Signal Transduction
  • Transcription, Genetic

Substances

  • Gonadotropins
  • Protein Subunits
  • Gonadotropin-Releasing Hormone
  • Mitogen-Activated Protein Kinases