Characterization and ultrastructural localization of annexin VI from mitochondria

Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca 2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which...

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Veröffentlicht in:FEBS letters 1995-02, Vol.360 (1), p.80-84
Hauptverfasser: Rainteau, Dominique, Mansuelle, Pascal, Rochat, Hervé, Weinman, Serge
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creator Rainteau, Dominique
Mansuelle, Pascal
Rochat, Hervé
Weinman, Serge
description Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca 2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria.
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subjects Amino Acid Sequence
Animals
Annexin A6 - metabolism
Annexin VI
Calcium Channels - metabolism
Cattle
Chemical Sciences
Hydrolysis
Microscopy, Immunoelectron
Mitochondria
Mitochondria, Liver - metabolism
Mitochondria, Liver - ultrastructure
Molecular Sequence Data
Organic chemistry
Rats
Sequence Homology, Amino Acid
title Characterization and ultrastructural localization of annexin VI from mitochondria
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