Postnatal development of inositol 1,4,5-trisphosphate receptors: a disparity with protein kinase C

Brain Res Dev Brain Res. 1995 Mar 16;85(1):109-18. doi: 10.1016/0165-3806(94)00181-x.

Abstract

Ligand-stimulated phosphoinositide hydrolysis activates a bifurcating second messenger system, releasing inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DG), which activates protein kinase C (PKC). Yet, in developing cat visual cortex and hippocampus, high levels of [3H]PDBu binding (labelling PKC) appear much earlier than do [3H]IP3 labelled sites. Binding distributions for the two ligands also appear to be complimentary in both brain regions. Moreover, early surgical removal of input to the visual cortex increases [3H]PDBu binding without affecting that of [3H]IP3. Our results suggest that, (1) at certain developmental stages, IP3 and PKC may act individually or complimentarily rather than synergistically in the visual cortex and hippocampus; (2) in neonatal cortex, IP3 metabolites rather than IP3 itself may act as second messengers; (3) although both IP3 receptors and PKC are localized in intracortical cells, their expression is regulated by different mechanisms during development.

Publication types

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

MeSH terms

  • Animals
  • Animals, Newborn / growth & development*
  • Binding Sites / physiology
  • Calcium Channels
  • Cats
  • Hippocampus / chemistry
  • Hippocampus / metabolism
  • Humans
  • Inositol 1,4,5-Trisphosphate Receptors
  • Phorbol 12,13-Dibutyrate
  • Protein Kinase C / metabolism*
  • Receptors, Cytoplasmic and Nuclear
  • Second Messenger Systems / physiology
  • Visual Cortex / chemistry
  • Visual Cortex / metabolism

Substances

  • Calcium Channels
  • ITPR1 protein, human
  • Inositol 1,4,5-Trisphosphate Receptors
  • Receptors, Cytoplasmic and Nuclear
  • Phorbol 12,13-Dibutyrate
  • Protein Kinase C