Cholesterol regulates membrane binding and aggregation by annexin 2 at submicromolar Ca 2+ concentration

Autor: Louise-Anne Pradel, Jesus Ayala-Sanmartin, Jean-Pierre Henry
Přispěvatelé: Biologie cellulaire et moléculaire de la sécrétion (BCMS), Centre National de la Recherche Scientifique (CNRS), This work was supported by the Centre National de la Recherche Scientifique (UPR 1929) and the Association pour la Recherche sur le Cancer (contract 9275)., Ayala-Sanmartin, Jesus
Rok vydání: 2001
Předmět:
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
Biophysics
[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
[SDV.BC.IC] Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]
Biochemistry
Exocytosis
Membrane Lipids
chemistry.chemical_compound
Annexin
[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]
Chromaffin granule
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
membrane binding
[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Annexin A2
Cyclodextrins
Liposome
Dose-Response Relationship
Drug
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
Cholesterol
beta-Cyclodextrins
aggregation
cholesterol
chromaffin granules
Intracellular Membranes
Annexin 2
Cell Biology
Phosphatidylserine
[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
EGTA
Membrane
chemistry
Liposomes
Calcium
lipids (amino acids
peptides
and proteins)
Protein Binding
Zdroj: Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, 2001, 1510 (1-2), pp.18-28. ⟨10.1016/s0005-2736(00)00262-5⟩
ISSN: 0005-2736
1879-2642
DOI: 10.1016/s0005-2736(00)00262-5
Popis: International audience; Annexin 2 is a member of the annexin family which has been implicated in calcium-regulated exocytosis. This contention is largely based on Ca(2+)-dependent binding of the protein to anionic phospholipids. However, annexin 2 was shown to be associated with chromaffin granules in the presence of EGTA. A fraction of this bound annexin 2 was released by methyl-beta-cyclodextrin, a reagent which depletes cholesterol from membranes. Restoration of the cholesterol content of chromaffin granule membranes with cholesterol/methyl-beta-cyclodextrin complexes restored the Ca(2+)-independent binding of annexin 2. The binding of both, monomeric and tetrameric forms of annexin 2 was also tested on liposomes of different composition. In the absence of Ca(2+), annexin 2, especially in its tetrameric form, bound to liposomes containing phosphatidylserine, and the addition of cholesterol to these liposomes increased the binding. Consistent with this observation, liposomes containing phosphatidylserine and cholesterol were aggregated by the tetrameric form of annexin 2 at submicromolar Ca(2+) concentrations. These results indicate that the lipid composition of membranes, and especially their cholesterol content, is important in the control of the subcellular localization of annexin 2 in resting cells, at low Ca(2+) concentration. Annexin 2 might be associated with membrane domains enriched in phosphatidylserine and cholesterol.
Databáze: OpenAIRE
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