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


Journal Article

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

Full Text

Cited Authors

  • Mengesdorf, T; Althausen, S; Mies, G; Oláh, L; Paschen, W

Published Date

  • June 2002

Published In

Volume / Issue

  • 27 / 6

Start / End Page

  • 477 - 484

PubMed ID

  • 12199152

Pubmed Central ID

  • 12199152

Electronic International Standard Serial Number (EISSN)

  • 1573-6903

International Standard Serial Number (ISSN)

  • 0364-3190

Digital Object Identifier (DOI)

  • 10.1023/a:1019844518704


  • eng