Annexin V forms calcium-dependent trimeric units on phospholipid vesicles

• Published in: FEBS 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
• Language: English
• Published: Amsterdam Elsevier B.V 14.12.1992; Elsevier
• Subjects: 4-(2-hydroxyethyl)-1-piperazinepropanesulfonic acid; Analytical, structural and metabolic biochemistry; Annexin; Annexin A5 - chemistry; Annexin A5 - drug effects; annexin V; Binding and carrier proteins; Biological and medical sciences; Calcium; Calcium - pharmacology; cardiolipin; Cross-linking; Cross-Linking Reagents; Cytoskeleton; dependent; dimethyl suberimidate; dioleoylphosphatidic acid; dioleoylphosphatidylcholine; dioleoylphosphatidylglycerol; DMS; DOPA; DOPC; DOPG; EGTA; ethylene glycol bis (beta-aminoethyl ether)-N,N,N′,N′-tetraacetic acid; Fluidity; formation; Fundamental and applied biological sciences. Psychology; HEPPS; interaction; lung; Macromolecular Substances; Membranes, Artificial; phosphatidylserine; Phospholipids; pigs; Protein Conformation - drug effects; Proteins; SDS-PAGE; sodium dodecyl sulfate poly-acrilamide gel electrophoresis; trimers; vesicles; HEPPS; DOPG; PS; Calcium; CL; DMS; EGTA; SDS-PAGE; Fluidity; Cross-linking; Cytoskeleton; DOPA; Annexin; DOPC; Binding protein; Oligomerization; Quaternary structure; Lipocortin; Liposome; Phospholipid; Crosslinking; Property structure relationship

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...