Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure. - Archive ouverte HAL Access content directly
Journal Articles Molecular and Cellular Biochemistry Year : 1998

Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.

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1
Uwe Schlattner
  • Function : Author
  • PersonId : 863804
Max Dolder
  • Function : Author

Abstract

The membrane binding properties of cytosolic and mitochondrial creatine kinase isoenzymes are reviewed in this article. Differences between both dimeric and octameric mitochondrial creatine kinase (Mi-CK) attached to membranes and the unbound form are elaborated with respect to possible biological function. The formation of crystalline mitochondrial inclusions under pathological conditions and its possible origin in the membrane attachment capabilities of Mi-CK are discussed. Finally, the implications of these results on mitochondrial energy transduction and structure are presented.
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Dates and versions

inserm-00390792 , version 1 (02-06-2009)

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  • HAL Id : inserm-00390792 , version 1
  • PUBMED : 9746318

Cite

Olaf Stachowiak, Uwe Schlattner, Max Dolder, Théo Wallimann. Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.. Molecular and Cellular Biochemistry, 1998, 184 (1-2), pp.141-51. ⟨inserm-00390792⟩

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