ANNEXIN-V FORMS CALCIUM-DEPENDENT TRIMERIC UNITS ON PHOSPHOLIPID-VESICLES

被引：84

作者：

CONCHA, NO

HEAD, JF

KAETZEL, MA

DEDMAN, JR

SEATON, BA ^{[1
]}

机构：

[1] BOSTON UNIV, SCH MED, DEPT PHYSIOL, BOSTON, MA 02118 USA

[2] UNIV CINCINNATI, COLL MED, DEPT PHYSIOL & BIOPHYS, CINCINNATI, OH 45267 USA

来源：

FEBS LETTERS | 1992年 / 314卷 / 02期

关键词：

CALCIUM; ANNEXIN; CYTOSKELETON; CROSS-LINKING; FLUIDITY;

D O I：

10.1016/0014-5793(92)80964-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 which 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.

引用

页码：159 / 162

页数：4

共 32 条

[1] SIMPLE SYSTEM FOR THE MEASUREMENT OF ION ACTIVITIES WITH SOLVENT POLYMERIC MEMBRANE ELECTRODES [J].