Limited breakdown of cytoskeletal proteins by an endogenous protease controls Ca2+-induced membrane fusion events in chicken erythrocytes

Paul Thomas, A. R. Limbrick, D. Allan

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The profound morphological changes which follow the treatment of chicken erythrocytes with the ionophore A23187 and Ca2+ are associated with a concomitant breakdown of certain membrane-associated proteins including α-spectrin, goblin and microtubule-associated proteins (MAPS) which undergo a limited proteolysis to give large, well-defined fragments. The Ca2+-sensitive protease responsible for these changes appears to be present in the soluble fraction of the cells. Treatment with TLCK or iodoacetamide inhibits both the major morphological changes and the proteolytic events but these agents do not prevent the dissociation of microtubules or the activation of endogenous sphingomyelinase which occur in cells with raised levels of intracellular Ca2+. It is suggested that the sphingomyelinase is activated as a consequence of a Ca2+-induced loss of phospholipid asymmetry in the plasma membrane.
Original languageEnglish
Pages (from-to)351-358
Number of pages8
JournalBiochimica et Biophysica Acta
Issue number2
Publication statusPublished - 1983

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