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
收藏
页码：159 / 162
页数：4
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