Phosphorylation state, solubility, and activity of calcium/calmodulin-dependent protein kinase IIα in transient focal ischemia in mouse brain

Thorsten Mengesdorf, Sonja Althausen, Günter Mies, Laszlo Oláh, Wulf Paschen

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

During and after middle cerebral artery occlusion in mice, CaMKIIα protein was irreversibly translocated from the soluble to the Triton X-100-nonsoluble fraction. This decrease in solubility had a strong effect on activity: CaMKIIα was almost completely inactivated after being translocated. Results from solubilization experiments suggest that different mechanisms underlie the conversion of CaMKIIα protein from a soluble to a detergent nonsoluble form in ischemic as opposite to nonischemic tissue. Analysis of the phosphorylation state of CaMKIIα revealed that in the total homogenate and the Triton X-100-nonsoluble fraction, CaMKIIα phosphorylated at only one site was the dominant phosphorylated form, whereas in the soluble fraction CaMKII phosphorylated at two sites was the predominant phosphorylated species. Investigation of the mechanisms underlying ischemia-induced changes in the solubility of CaMKIIα could help to elucidate processes triggered by transient focal cerebral ischemia that lead to neuronal cell injury.

Original languageEnglish
Pages (from-to)477-484
Number of pages8
JournalNeurochemical research
Volume27
Issue number6
DOIs
Publication statusPublished - Jun 1 2002

Keywords

  • CaMKIIα
  • Mouse
  • Phosphorylation
  • Solubility
  • Transient focal cerebral ischemia
  • Translocation

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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