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
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00087-P