Calcium-ganglioside interactions and synaptic plasticity: effect of calcium on specific ganglioside/peptide (valinomycin, gramicidin A)-complexes in mixed mono- and bilayers☆
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2021, Progress in Biophysics and Molecular BiologyCitation Excerpt :These lipids can carry up to seven charged groups of sialic acid and they are estimated to be 15% of the total lipid of central gray matter (for literature see Fernandes de Lima et al., 1997b). Rahmann et al. (1992) proposed that the charged heads would function as attractors to screening calcium ions and therefore would contribute to excitability control within the neuropil. In short, the glycosides would diminish the calcium activity.
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2004, Brain ResearchCitation Excerpt :However, nuclear magnetic resonance studies have found that although the sialic acid rings of gangliosides are extended into the aqueous phase their carboxyl groups remain sufficiently close to the membrane surface to be able to contribute to the membrane surface charge [2]. At this time, we cannot rule out that GD1a could also produce channel conformational changes, as it has been reported in gramicidin A channels [38]. Regardless of the mechanism, the observation that GD1a affects the voltage-dependent properties of voltage-dependent sodium channels is important since GD1a is the major ganglioside in brain cortex and basal brain [4].
Membrane dipole potential modulates proton conductance through gramicidin channel: Movement of negative ionic defects inside the channel
2002, Biophysical JournalCitation Excerpt :The main difference between the two variants of the model shown in Fig. 6 consists in the sign of the localized charge being negative to account for the dipole potential effect on the proton conduction. It should be noted that in contrast to modulation of the membrane dipole potential, varying the surface potential of BLMs produced qualitatively similar effects on the proton and the alkali metal conductance of gramicidin channels; in particular, creation of the negative surface potential upon admixing DPhPG to BLM led to the increase in the gramicidin proton conductance in our experiments, similarly to the earlier data on the influence of negatively charged lipids on alkali metal cation fluxes through gA channels (Apell et al., 1979; Rahmann et al., 1992; Mittler-Neher and Knoll, 1993; Rostovtseva et al., 1998). These results imply that movement of protons outside gA channels is necessarily involved in the electric current flowing across BLMs, and the translocation of negative defects inside the channels does not solely determine the total rate of proton transport.
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- ☆
Parts of the results of this refereed paper were presented at the ESN workshop on Glycoconjugates and Neuronal Membrane Function held in Leipzig, 23–28 July 1990. The workshop was organized by Dr G. Tettamanti, Milano, Italy, and Dr H. Rahmann, Stuttgart, Fed. Rep. Germany.