Annexin V forms calcium‐dependent trimeric units on phospholipid vesicles

FEBS Letters

Concha, Nestor O.¹  Seaton, Barbara A.¹  Head, James F.¹  Kaetzel, Marcia A.²  Dedman, John R.² 

[1] Department of Physiology, Boston University School of Medicine, Boston, MA 02118-2394, USA;Department of Physiology and Biophysics, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267, USA

关键词: Calcium;    Annexin;    Cytoskeleton;    Cross-linking;    Fluidity;    EGTA;    ethylene glycol bis (beta-aminoethyl ether)-N;    N;    N′;    N′-tetraacetic acid;    SDS-PAGE;    sodium dodecyl sulfate poly-acrilamide gel electrophoresis;    DMS;    dimethyl suberimidate;    PS;    phosphatidylserine;    DOPC;    dioleoylphosphatidylcholine;    DOPG;    dioleoylphosphatidylglycerol;    DOPA;    dioleoylphosphatidic acid;    CL;    cardiolipin;    HEPPS;    4-(2-hydroxyethyl)-1-piperazinepropanesulfonic acid.;   

DOI  :  10.1016/0014-5793(92)80964-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The quaternary structure of annexin V, a calcium-dependent phospholipid binding protein, was investigated by chemical cross-linking. Calcium was found to induce the formation of trimers, hexamers, and higher aggregates only when anionic phospholipids were present. Oligomerization occurred under the same conditions as annexin—vesicle binding. A model is proposed in when cell stimulation leads to calcium-induced organization of arrays of annexin V lining the inner membrane surface, thus altering properties such as permeability and fluidity.

【 授权许可】

Unknown