Alterations of CaMKII after hypoxia-ischemia during brain development

J Neurochem. 2004 Oct;91(2):429-37. doi: 10.1111/j.1471-4159.2004.02733.x.

Abstract

Transient brain hypoxia-ischemia (HI) in neonates leads to delayed neuronal death and long-term neurological deficits. However, the underlying mechanisms are incompletely understood. Calcium-calmodulin-dependent protein kinase II (CaMKII) is one of the most abundant protein kinases in neurons and plays crucial roles in synaptic development and plasticity. This study used a neonatal brain HI model to investigate whether and how CaMKII was altered after HI and how the changes were affected by brain development. Expression of CaMKII was markedly up-regulated during brain development. After HI, CaMKII was totally and permanently depleted from the cytosol and concomitantly deposited into a Triton-insoluble fraction in neurons that were undergoing delayed neuronal death. Autophosphorylation of CaMKII-Thr286 transiently increased at 30 min of reperfusion and declined thereafter. All these changes were mild in P7 pups but more dramatic in P26 rats, consistent with the development-dependent CaMKII expression in neurons. The results suggest that long-term CaMKII depletion from the cytosolic fraction and deposition into the Triton-insoluble fraction may disable synaptic development, damage synaptic plasticity, and contribute to delayed neuronal death and long-term synaptic deficits after transient HI.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Age Factors
  • Animals
  • Brain / growth & development
  • Brain / pathology
  • Brain / physiopathology*
  • Brain Chemistry
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Cell Death
  • Detergents / chemistry
  • Disease Models, Animal
  • Hypoxia-Ischemia, Brain / enzymology
  • Hypoxia-Ischemia, Brain / pathology
  • Hypoxia-Ischemia, Brain / physiopathology*
  • Immunoblotting
  • Neurons / enzymology*
  • Neurons / pathology
  • Phosphorylation
  • Protein Transport
  • Rats
  • Rats, Sprague-Dawley
  • Solubility
  • Subcellular Fractions / enzymology

Substances

  • Detergents
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases