Binding of vascular anticoagulant alpha (VAC alpha) to planar phospholipid bilayers.

Vascular anticoagulant alpha (VAC alpha, annexin V) is a member of the family of calcium and phospholipid binding proteins, the annexins. The binding properties of VAC alpha to phospholipid bilayers were studied by ellipsometry. Adsorption was calcium-dependent and completely reversible upon calcium depletion. Half-maximal adsorptions to phospholipid bilayers consisting of 100, 20, 5, and 1% dioleoyl-phosphatidylserine (DOPS) supplemented with dioleoyl-phosphatidylcholine (DOPC) were reached at Ca2+ concentrations of 0.04, 0.22, 1.5, and 8.6 mM. These surfaces all showed the same maximal adsorption of 0.22 +/- 0.01 micrograms of VAC alpha/cm2 (mean +/- S.D.). The adsorption to bilayers containing more than 10% DOPS was independent of VAC alpha concentrations in the range of 0.5-100 nM. Dissociation constants for VAC alpha binding to these surfaces were estimated to be below 2 x 10(-10) M. No adsorption was observed on pure DOPC bilayers at a Ca2+ concentration of 3 mM. The ability to mediate VAC alpha binding to 20% DOPS/80% DOPC bilayers was highly specific for Ca2+. The use of other divalent cations resulted in decreased binding in the order Cd2+ greater than Zn2+ greater than Mn2+ greater than Co2+ greater than Ba2+ greater than Mg2+. Zinc ions had a synergistic effect on Ca2(+)-dependent VAC alpha binding. The Ca2+ concentration needed for half-maximal binding to cardiolipin, dioleoyl-phosphatidylglycerol, DOPS, phosphatidylinositol, phosphatidic acid, dioleoyl-phosphatidylethanolamine, and sphingomyelin increased in that order. Adsorption was independent of the overall surface charge of the phospholipid membrane.

• Publication year

  1990

• Venue

  Journal of Biological Chemistry

• Publication date

  1990-03-25

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)34062-1PMID 2138622
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• The Ca2+ concentration needed for half-maximal binding rises across the compared phospholipid species in the order cardiolipin, dioleoyl-phosphatidylglycerol, DOPS, phosphatidylinositol, phosphatidic acid, dioleoyl-phosphatidylethanolamine, and sphingomyelin.

  Confidence 0.97

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• Ca2+-dependent VAC alpha binding is highly specific for Ca2+, is weaker with other divalent cations in the order Cd2+ > Zn2+ > Mn2+ > Co2+ > Ba2+ > Mg2+, and Zn2+ has a synergistic effect on binding.

  Confidence 0.96

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• On DOPS/DOPC bilayers, lowering DOPS content shifts half-maximal adsorption to higher Ca2+ concentrations, while bilayers with more than 10% DOPS show concentration-independent adsorption and subnanomolar apparent dissociation constants; pure DOPC bilayers show no adsorption at 3 mM Ca2+.

  Confidence 0.98

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• VAC alpha adsorption to planar phospholipid bilayers is calcium-dependent and fully reversible after calcium depletion.

  Confidence 0.99

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review

• calcium ions

  ions

  Ca2+ ions used as the divalent cation required for VAC alpha binding in the experiments.

  Aliases: Ca2+

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• compared phospholipid species

  lipids

  The set of membrane lipids compared for calcium-dependent binding, including cardiolipin, phosphatidylglycerol, DOPS, phosphatidylinositol, phosphatidic acid, phosphatidylethanolamine, and sphingomyelin.

  Aliases: tested phospholipids

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• dioleoyl-phosphatidylcholine (dopc)

  lipids

  A phosphatidylcholine-containing membrane lipid used as the neutral bilayer component in the adsorption measurements.

  Aliases: DOPC

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• dioleoyl-phosphatidylserine (dops)

  lipids

  A phosphatidylserine-containing membrane lipid used to vary bilayer composition in the adsorption measurements.

  Aliases: DOPS

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• other divalent cations

  ions

  Divalent metal ions other than calcium that were tested for their ability to support VAC alpha binding.

  Aliases: divalent cations

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• phospholipid bilayers

  membranes

  Planar membrane bilayers made from phospholipids and used as the binding surface in the assays.

  Aliases: lipid bilayers, planar bilayers

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• vac alpha

  proteins

  Vascular anticoagulant alpha, also called annexin V, is the calcium- and phospholipid-binding protein examined in the bilayer assays.

  Aliases: annexin V

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review
• zinc ions

  ions

  Zn2+ ions tested both as alternative divalent cations and as a possible synergistic cofactor for calcium-dependent binding.

  Aliases: Zn2+

  박진우 (dztg5apj7m) extractionB (s683577b42) reviewjihoonc (k5vuy3tzcm) reviewq (76h6bfydm6) review

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