title: Characterization and ultrastructural localization of annexin VI from mitochondria.
abstract: 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.
authors.affiliation: Département de Biochimie, UFR Biomédicale des Saints-Pères, Université René Descartes, Paris, France.
authors.forename: D
authors.initials: D
authors.lastname: Rainteau
authors.forename: P
authors.initials: P
authors.lastname: Mansuelle
authors.forename: H
authors.initials: H
authors.lastname: Rochat
authors.forename: S
authors.initials: S
authors.lastname: Weinman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017317:Annexin A6 / Q000378:metabolism*; D015220:Calcium Channels / Q000378:metabolism; D002417:Cattle; D006868:Hydrolysis; D016253:Microscopy, Immunoelectron; D008930:Mitochondria, Liver / Q000378:metabolism* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D051381:Rats; D017386:Sequence Homology, Amino Acid
chemical_list: D017317:Annexin A6; D015220:Calcium Channels