期刊论文详细信息
FEBS Letters | |
Annexin V forms calcium‐dependent trimeric units on phospholipid vesicles | |
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
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020297207ZK.pdf | 320KB | download |