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Studies on the mechanism of membrane fusion: evidence for an intermembrane calcium(2+) ion-phospholipid complex, synergism with magnesium(2+) ion, and inhibition by spectrin
Abstract
The interaction of Ca2+ and Mg2+ with phosphatidylserine (PS) vesicles in 0.1 M NaCl aqueous solution was studied by equilibrium dialysis binding, X-ray diffraction, batch microcalorimetry, kinetics of cation-induced vesicle aggregation, release of vesicle contents, and fusion. Addition of either cation causes aggregation of PS vesicles and produces complexes with similar stoichiometry (1:2 cation/PS) at saturating concentrations, although the details of the interactions and the resulting complexes are quite different. Addition of Ca2+ to PS vesicles at T greater than or equal to 25 degrees C induces the formation of an "anhydrous" complex of closely apposed membranes with highly ordered crystalline acyl chains and a very high transition temperature (Tc greater than 100 degrees C). The formation of this complex is accompanied by a release of heat (5.5 kcal/mol), rapid release of vesicle contents, and fusion of the vesicles into larger membranous structures. By contrast, addition of Mg2+ produces a complex with PS which is much more hydrated, has no crystallization of the acyl chains at T greater than or equal to 20 degrees C, and has comparatively little fusion. Studies with both Ca2+ and Mg2+ added simultaneously indicate that there is a synergistic effect between the two cations, which results in an enhancement of the ability of Ca2+ to form its specific complex with PS at lower concentrations. The presence of the erythrocyte protein "spectrin" inhibits this synergism and interferes with the formation of the specific PS/Ca complex. It also inhibits the fusion of PS vesicles. It is proposed that the unique PS/Ca complex, which involves close apposition of vesicle membranes, is an intermembrane "trans" complex. We further propose that such a complex is a key step for the resultant phase transition and fusion of PS vesicles. By contrast, the PS/Mg complex is proposed to be a "cis" complex with respect to each membrane. The results are discussed in terms of the mechanism of membrane fusion.
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Cites
Papahadjopoulos, D., & Bangham, A. D. (1966) · Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis · doi:10.1016/0926-6585(66)90053-7 · Cited by 110
Self-citation
Cited by
Hydration forces between phospholipid bilayers
Rand, R. P., & Parsegian, V. A. (1989) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(89)90010-5 · Cited by 1,125
INTERACTIONS BETWEEN NEUTRAL PHOSPHOLIPID BILAYER MEMBRANES
LIS, L. J., MCALISTER, M., FULLER, N., RAND, R. P., & PARSEGIAN, V. A. (1982) · Biophysical Journal · doi:10.1016/s0006-3495(21)00385-4 · Cited by 758
Holland, J. W., Hui, C., Cullis, P. R., & Madden, T. D. (1996) · Biochemistry · doi:10.1021/bi952000v · Cited by 223
Energetics of stalk intermediates in membrane fusion are controlled by lipid composition
Aeffner, S., Reusch, T., Weinhausen, B., & Salditt, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119442109 · Cited by 185
Adrian Parsegian, V. (1982) · Advances in Colloid and Interface Science · doi:10.1016/0001-8686(82)85005-7 · Cited by 29
Metadata
- Authors
- Portis, A., Newton, C., Pangborn, W., & Papahadjopoulos, D.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1979-03-06
- Volume
- 18
- Issue
- 5
- Pages
- 780-790
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1976319018
- Cited by
- 472
- References
- 1
- FWCI
- 17.02
- Type
- journal article
- Language
- en
- Open access
- closed
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- Portis, A., Newton, C., Pangborn, W., & Papahadjopoulos, D. (1979). Studies on the mechanism of membrane fusion: evidence for an intermembrane calcium(2+) ion-phospholipid complex, synergism with magnesium(2+) ion, and inhibition by spectrin. Biochemistry. https://doi.org/10.1021/bi00572a007
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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