| Literature DB >> 1459245 |
N O Concha1, J F Head, M A Kaetzel, J R Dedman, B A Seaton.
Abstract
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 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.Entities:
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Year: 1992 PMID： 1459245 DOI： 10.1016/0014-5793(92)80964-i
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124