Calcium-ganglioside interactions and synaptic plasticity: effect of calcium on specific ganglioside/peptide (valinomycin, gramicidin A)-complexes in mixed mono- and bilayers

Rahmann, H.; Schifferer, Florian; Beitinger, Heinz

doi:10.1016/0197-0186(92)90047-u

Cited by 24 publications

(12 citation statements)

References 54 publications

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“…Due to the gangliosidic physicochemical properties, these molecules might function as neuromodulators in connection with Ca ϩϩ . As Ca ϩϩ -binders, gangliosides may be involved in synaptic transmission as a modulator of the lipid bilayer, influencing the calcium current flow by changing the negative surface potential or by conformational changes of functional proteins in the synapse plasma membrane (Rahmann et al, 1992;Tanaka et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Immunostaining of ganglioside GD1b, GD3 and GM1 in rat cerebellum: Cellular layer and cell type specific associations

et al. 2000

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We have studied the cellular distribution of gangliosides GD1b, GD3 and GM1 in rat cerebellum by immunostaining, using monoclonal antibodies and confocal microscopy. Antibodies against astroglial, neuronal and synaptic vesicle associated molecules were used for colocalization analyses. In the gray matter, the anti-GD1b antibody stained thin strands in the molecular layer (ML), interpreted as Bergman glia fibers based on colocalized staining with anti-glial fibrillary acidic protein (GFAP). The neuropil in the granule (GL) and Purkinje (PL) cell layers was also anti-GD1b positive. The anti-GD3 antibody stained the ML, the neuropil in the GL and PL and also the granule and Purkinje cell bodies, appearing intracytoplasmically and vesicle associated. Anti-GD1b and anti-GD3 staining in the GL glomeruli were colocalized with anti-synaptophysin staining. The anti-GM1 antibody stained cell bodies in the ML but they could not be characterized in colocalization experiments. The GL and PL were not stained with the anti-GM1 antibody. In the white matter, different staining patterns were seen for the gangliosides, the anti-GM1 staining being the most intense. This study shows cellular layer and cell type specific associations of the investigated gangliosides and localization of GD1b and GD3 at synaptic sites, warranting further studies on their role in synaptic mechanisms.

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Section: Discussionmentioning

confidence: 99%

Immunostaining of ganglioside GD1b, GD3 and GM1 in rat cerebellum: Cellular layer and cell type specific associations

et al. 2000

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“…packing in the hydrophobic region of the lipid (44). This interaction does not disrupt the lipid bilayer organization.…”

Section: Effect Of Relative Ganglioside Concentration On A␤-gangliosimentioning

confidence: 94%

Structural Transitions Associated with the Interaction of Alzheimer β-Amyloid Peptides with Gangliosides

McLaurin¹,

Franklin²,

Fraser³

et al. 1998

Journal of Biological Chemistry

176

155

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Alzheimer's disease is characterized pathologically by the presence of neurofibrillary tangles and amyloid plaques. The principal component of the plaque is the ␤-amyloid peptide (A␤), a 39 -43-residue peptide. The conformational change required for the conversion of soluble peptide into amyloid fibrils is modulated by pH, A␤ concentration, addition of kinetic and thermodynamic enhancers, and alterations in the primary sequence of A␤. We report here the ability of gangliosides to induce an ␣-helical structure in A␤ and thereby diminish fibrillogenesis. Circular dichroism and a fluorescence dye release assay data indicate that gangliosides interact with and induce ␣-helix formation in A␤. We find that the sialic acid moiety of gangliosides is necessary for the induction of ␣-helical structure. Differences in the amount and the position of the sialic acid on the carbohydrate backbone also affect the conformational switch. The A␤-ganglioside interaction at pH 7.0, monitored by CD, is stable over time and resistant to high concentrations of NaCl. The induction of ␣-helical structure is greater with A␤1-40 than A␤1-42. The ability of gangliosides to sequester A␤ from fibril formation was also evaluated by electron microscopy.Alzheimer's disease is characterized by the presence of amyloid plaques surrounded by dead and dying neurons in the brain (1, 2). The principal component of the plaque is the ␤-amyloid (A␤) 1 peptide, a 39 -43-residue peptide found in normal human tissue and generated as a cleavage product from the larger amyloid precursor protein (3)(4)(5)(6). A␤ in the plaque is in the form of an amyloid fibril, approximately 100 Å in diameter and several microns long (7). The conformational changes required for the conversion of soluble A␤ into amyloid fibrils have been demonstrated to be a nucleation-dependent process (8, 9) which is modulated by pH, A␤-peptide concentrations, and presence of nucleation seeds, such as proteoglycans and apolipoproteins (10 -14). Alterations in the primary sequence of A␤ peptides greatly affect amyloid fibril formation (15). The E22Q mutation in A␤, found in hereditary cerebral hemorrhage with amyloidosis of the dutch type (16), yields a peptide with increased ability to form amyloid fibrils (17). On the other hand, the single mutation of V18A increases the apparent ␣-helical content of A␤ and diminishes fibrillogenesis (18). We have found that the interaction of A␤40 and A␤42 with mixed ganglioside preparations and GM1 increases the ␣-helical content, and we speculated that this interaction may prevent amyloid fibril formation (19).It has been well documented that amyloid fibrils are intimately associated with neuronal, microglial, and endothethial membranes. Cell processes are extended out into close proximity of amyloid deposits (20,21), and cell culture studies have demonstrated that overexpression of A␤ results in cell surface ruffling (22-24). These results, as well as the studies on A␤-membrane interactions (19,(25)(26)(27)(28)(29)(30)(31), suggested that the interaction...

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“…Physiological functions Functions of gangliosides postulated so far include modulation of membrane proteins, neural development, cell–cell interaction/recognition, temperature adaptation, neuronal Ca 2+ homeostasis, axonal growth, (para)node of Ranvier stability and synaptic transmission (Ando, 1983; Ledeen, 1985; Thomas & Brewer, 1990; Rahmann et al 1992; Wu & Ledeen, 1994; Lloyd & Furukawa, 1998; Ledeen & Wu, 2006; Susuki et al 2007). While older studies assessed function by studying the effects of exogenous ganglioside application on in vitro systems, recent generation of transgenic mice lacking ganglioside‐synthesizing enzymes allowed investigations into the function of endogenous gangliosides (Sheikh et al 1999; Kawai et al 2001; Okada et al 2002; Inoue et al 2002; Sugiura et al 2005; Jennemann et al 2005; Zitman et al 2008, 2009).…”

mentioning

confidence: 99%

Pathophysiological actions of neuropathy‐related anti‐ganglioside antibodies at the neuromuscular junction

Plomp

Willison

2009

The Journal of Physiology

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The outer leaflet of neuronal membranes is highly enriched in gangliosides. Therefore, specific neuronal roles have been attributed to this family of sialylated glycosphingolipids, e.g. in modulation of ion channels and transporters, neuronal interaction and recognition, temperature adaptation, Ca 2+ homeostasis, axonal growth, (para)node of Ranvier stability and synaptic transmission. Recent developmental, ageing and injury studies on transgenic mice lacking subsets of gangliosides indicate that gangliosides are involved in maintenance rather than development of the nervous system and that ganglioside family members are able to act in a mutually compensatory manner. Besides having physiological functions, gangliosides are the likely antigenic targets of autoantibodies present in Guillain-Barré syndrome (GBS), a group of neuropathies with clinical symptoms of motor-and/or sensory peripheral nerve dysfunction. Antibody binding to peripheral nerves is thought to either interfere with ganglioside function or activate complement, causing axonal damage and thereby disturbed action potential conduction. The presynaptic motor nerve terminal at the neuromuscular junction (NMJ) may be a prominent target because it is highly enriched in gangliosides and lies outside the blood-nerve barrier, allowing antibody access. The ensuing neuromuscular synaptopathy might contribute to the muscle weakness in GBS patients. Several groups, including our own, have studied the effects of anti-ganglioside antibodies in ex vivo and in vivo experimental settings at mouse NMJs. Here, after providing a background overview on ganglioside synthesis, localization and physiology, we will review those studies, which clearly show that anti-ganglioside antibodies are capable of binding to NMJs and thereby can exert a variety of pathophysiological effects. Furthermore, we will discuss the human clinical electrophysiological and histological evidence produced so far of the existence of a neuromuscular synaptopathy contributing to muscle weakness in GBS patients.

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Calcium-ganglioside interactions and synaptic plasticity: effect of calcium on specific ganglioside/peptide (valinomycin, gramicidin A)-complexes in mixed mono- and bilayers

Cited by 24 publications

References 54 publications

Immunostaining of ganglioside GD1b, GD3 and GM1 in rat cerebellum: Cellular layer and cell type specific associations

Immunostaining of ganglioside GD1b, GD3 and GM1 in rat cerebellum: Cellular layer and cell type specific associations

Structural Transitions Associated with the Interaction of Alzheimer β-Amyloid Peptides with Gangliosides

Pathophysiological actions of neuropathy‐related anti‐ganglioside antibodies at the neuromuscular junction

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