Annexin V forms calcium-dependent trimeric units on phospholipid vesicles

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...

Full description

Saved in:
Bibliographic Details
Published inFEBS letters Vol. 314; no. 2; pp. 159 - 162
Main Authors Concha, Nestor O., Head, James F., Kaetzel, Marcia A., Dedman, John R., Seaton, Barbara A.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 14.12.1992
Elsevier
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)80964-I