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Characterization and ultrastructural localization of annexin VI from mitochondria
Author(s) -
Rainteau Dominique,
Mansuelle Pascal,
Rochat Hervé,
Weinman Serge
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00087-p
Subject(s) - mitochondrion , annexin , annexin a2 , intracellular , chemistry , microbiology and biotechnology , pi , biochemistry , inner membrane , calcium , biology , apoptosis , organic chemistry
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.