Endonexin (annexin IV)-mediated lateral segregation of phosphatidylglycerol in phosphatidylglycerol/phosphatidylcholine membranes.

作者: Matthew Junker , Carl E. Creutz

DOI: 10.1021/BI00089A012

关键词: AnnexinMembranePhosphatidylcholinePyrenePhosphatidylglycerolVesicleBiologyBinding proteinMolecular biologyBiological membrane

摘要: Endonexin (annexin IV) is a member of the annexin family homologous proteins that share ability to bind pure lipid membranes and aggregate vesicles in Ca(2+)-dependent fashion. appears preferentially interact with certain types lipids such as phosphatidylglycerol (PG) PG/phosphatidylcholine (PC) mixed membranes. Such preferential binding should result localization PG membrane regions where endonexin bound. This was tested using derivative containing fluorophore pyrene, which exhibits fluorescence sensitive molecular collision frequency. Motional restriction pyrene-PG upon endonexin-membrane evident from decreased ratios excimer-to-monomer (E/M) pyrene 97% PG/3% vesicles. A maximum decrease 30% suggests average diffusion constant molecules or 53% assuming only outer-monolayer endonexin. In 5% 10% PC, segregation observed increases E/M 14.2 +/- 1.8% 6.8 0.1%, respectively, presence either 10 mM (5% pyrene-PG) 2 (10% free Ca2+. At higher concentrations Ca2+ (> for > pyrene-PG), smaller endonexin-dependent are at high surface densities compete limited pool pyrene-PG. The nature these interactions systems has implications way annexins may modulate structure cells.

参考文章(17)
C E Creutz, W J Zaks, H C Hamman, S Crane, W H Martin, K L Gould, K M Oddie, S J Parsons, Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36. Journal of Biological Chemistry. ,vol. 262, pp. 1860- 1868 ,(1987) , 10.1016/S0021-9258(19)75719-6
H A Andree, C P Reutelingsperger, R Hauptmann, H C Hemker, W T Hermens, G M Willems, Binding of vascular anticoagulant alpha (VAC alpha) to planar phospholipid bilayers. Journal of Biological Chemistry. ,vol. 265, pp. 4923- 4928 ,(1990) , 10.1016/S0021-9258(19)34062-1
Grant R. Bartlett, Phosphorus Assay in Column Chromatography Journal of Biological Chemistry. ,vol. 234, pp. 466- 468 ,(1959) , 10.1016/S0021-9258(18)70226-3
D D Schlaepfer, H T Haigler, Characterization of Ca2+-dependent phospholipid binding and phosphorylation of lipocortin I. Journal of Biological Chemistry. ,vol. 262, pp. 6931- 6937 ,(1987) , 10.1016/S0021-9258(18)48333-0
D. D. Schlaepfer, T. Mehlman, W. H. Burgess, H. T. Haigler, Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein Proceedings of the National Academy of Sciences of the United States of America. ,vol. 84, pp. 6078- 6082 ,(1987) , 10.1073/PNAS.84.17.6078
C. Creutz, The annexins and exocytosis Science. ,vol. 258, pp. 924- 931 ,(1992) , 10.1126/SCIENCE.1439804
L.D. Mayer, M.J. Hope, P.R. Cullis, Vesicles of variable sizes produced by a rapid extrusion procedure Biochimica et Biophysica Acta. ,vol. 858, pp. 161- 168 ,(1986) , 10.1016/0005-2736(86)90302-0
Paul Meers, Location of tryptophans in membrane-bound annexins. Biochemistry. ,vol. 29, pp. 3325- 3330 ,(1990) , 10.1021/BI00465A025
Mohammad D. Bazzi, Gary L. Nelsestuen, Association of protein kinase C with phospholipid vesicles. Biochemistry. ,vol. 26, pp. 115- 122 ,(1987) , 10.1021/BI00375A017
Paula J. Shadle, Klaus Weber, Calcium binding protein from porcine intestine binds to phosphatidylserine vesicles in the presence of calcium Biochimica et Biophysica Acta. ,vol. 897, pp. 502- 506 ,(1987) , 10.1016/0005-2736(87)90448-2