Comparative studies on the effects of pH and Ca2+ on bilayers of various negatively charged phospholipids and their mixtures with phosphatidylcholine

Dijck, P.W.M. Van; Kruijff, Ben de; Verkleij, Arie J.; Deenen, L.L.M. Van; Gier, J. De

doi:10.1016/0005-2736(78)90219-5

Cited by 314 publications

(164 citation statements)

References 29 publications

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“…Phosphatidylserine is the component most likely to be affected by the conditions used, as the pH and the concentration of ions can strongly influence its physicochemical properties via effects on the charged polar head group [50]. Both a low pH [51] and the presence of calcium [ 52] have been shown to raise the phase transition temperature of phosphatidylserine dramatically. Calcium has been shown to induce lateral [53,54] and structural [51] phase separations in mixtures of phosphatidylserine and phosphatidylcholine.…”

Section: Discussionmentioning

confidence: 99%

“…Both a low pH [51] and the presence of calcium [ 52] have been shown to raise the phase transition temperature of phosphatidylserine dramatically. Calcium has been shown to induce lateral [53,54] and structural [51] phase separations in mixtures of phosphatidylserine and phosphatidylcholine. Also, in mixtures of phosphatidylserine and phosphatidylethanolamine calcium-induced phase separations have been observed (van Echteld, C., unpublished results).…”

Section: Discussionmentioning

confidence: 99%

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The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

Gerritsen

Verkleij

Deenen

1979

Biochimica et Biophysica Acta (BBA) - Biomembranes

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SummaryTriton X-100 (in concentrations which did not cause a significant solubilization of membrane material) caused aggregation of the intramembrane particles of human erythrocyte ghosts.Ghosts from which the extrinsic proteins had been removed by alkali treatment showed a temperature-induced aggregation of the particles. With virtually no spectrin present, the particles in these stripped ghosts could still be aggregated by manipulations with ionic strength and pH, or by the addition of calcium.Recombinant vesicles were made from a Triton X-100 extract and a mixture of phospholipids with a composition which resembled that of the inner monolayer of erythrocyte membrane. In these recombinants the same manipulations with ionic strength and pH and the addition of calcium caused a rearrangement of the particles, resulting in the appearance of particle-free areas. In recombinants prepared from a Triton X-100 extract and egg phosphatidylcholine the lateral distribution of the particles was not altered by these manipulations.It is concluded that in the erythrocyte membrane the intramembrane particles can be aggregated by effects of external agents on lipid components. In this light the role of spectrin in stabilizing the membrane by interactions with lipids in the inner monolayer is discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

Gerritsen

Verkleij

Deenen

1979

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…A plot of the dye release versus pH generates a sigmoidal curve for all lipids, PtdGro, PtdSer, PtdIns and PtdH, and indicated a pK, of approximately 6.5. It has been shown previously that altering pH in the range 4-8 affects the protonation of histidine residues of peptides, but has no effect on vesicles composed of the following lipids: PtdSer; PtdGro; PtdH; and PtdIns (Van Dijck et al, 1978). AAP/?-( 1 -40)-peptide and AAPP-( 1 -42)-peptide have three histidine residues, at positions 6, 13 and 14; our data suggests that one or more of these residues are important for membrane interaction.…”

Section: Lipidmentioning

confidence: 97%

Characterization of the Interactions of Alzheimer β‐Amyloid Peptides with Phospholipid Membranes

McLaurin

Chakrabartty

1997

European Journal of Biochemistry

196

182

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Increasing evidence suggests that Alzheimer P-amyloid peptides (AAPP) may be toxic agents in Alzheimer disease. We investigated the possibility that the toxicity may be the result of peptide-lipid interactions, involving either the cell membrane or the intracellular vesicular system. The interaction of the AAPP-(1-40), AAPP-(1-42), AAPP-(9-25) and AAPP-(25-35)-peptides with acidic and zwitterionic phospholipids was investigated by means of circular dichroism, vesicle disruption and lipid-aggregation assays. These studies were undertaken at peptide concentrations approaching in vivo levels and at physiological salt concentrations. Circular-dichroism studies demonstrate that acidic phospholipids induce a conformational change from random coil to P structure in AAPP-(I -40)-peptide and AAPD-(I -42)-peptide at pH 6.0. In contrast, at pH 7.0, only AAPP-(l-42)-peptide was induced to adopt P structure. Phosphatidylinositol was the most efficient inducer of P structure in AAPP-( 1 -42)-peptide. To further investigate the peptide-lipid interactions, we examined the ability of the AAPP peptides to disrupt andlor aggregate phospholipid vesicles. These properties were found to be mediated predominantly through electrostatic interactions with the phospholipid headgroup. The data presented in this paper have implications for AAPD toxicity and senile-plaque formation.

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“…1,6-diphenyl-1,3,5-hexatriene (DPH) steady state fluorescence anisotropy and Laurdan general polarization values were also observed to increase in the presence of Zn 2+ in a concentration-dependent manner, indicating a less fluid bilayer. Effects of Ca 2+ on binary lipid models of various negatively charged phospholipid MLVs with PC have been investigated using freeze-fracture electron microscopy, ITC and DSC (Vandijck et al, 1978;Blume, 1985;Sinn et al, 2006). Although PG, PS and PA all contain one negative charge, they were shown to exhibit distinct mixing behaviors in the presence of Ca 2+ (Vandijck et al, 1978).…”

Section: I M Y R I S T O Y L P H O S P H a T I D I C A C I D ( D M mentioning

confidence: 99%

“…PE, another zwitterionic lipid species, can form the non-lamellar inverted hexagonal phase, affecting lipid-packing properties for membrane fusion or liposome budding. Negatively charged phospholipids like PS affect membrane functioning as the charge is influenced by pH and divalent ions like Ca 2+ and Mg 2+ (Vandijck et al, 1978). Moreover, PS has been shown to be an important lipid species in apoptotic processes in the presence of Hg 2+ , for example (Eisele et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Biomimetic Model Membrane Systems Serve as Increasingly Valuable in Vitro Tools

Le¹,

Litzenberger²,

Prenner³

2011

Advances in Biomimetics

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Comparative studies on the effects of pH and Ca2+ on bilayers of various negatively charged phospholipids and their mixtures with phosphatidylcholine

Cited by 314 publications

References 29 publications

The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

Characterization of the Interactions of Alzheimer β‐Amyloid Peptides with Phospholipid Membranes

Biomimetic Model Membrane Systems Serve as Increasingly Valuable in Vitro Tools

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