Changes in Rabbit Brain Cytosolic and Membrane‐Bound Gangliosides During Prenatal Life

Sonnino, Sandro; Ghidoni, Riccardo; Masserini, Massimo; Aporti, F.; Tettamanti, Guido

doi:10.1111/j.1471-4159.1981.tb02398.x

Cited by 51 publications

(9 citation statements)

References 39 publications

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“…Although the main site of ganglioside deposition is the plasma membrane, small amounts of gangliosides occur in soluble form in the brain of different animals and in cultured cells [2][3][4][5][6][7]. In calf [3] and rat [6] brain cytosolic gangliosides were shown to be present as lipoprotein complexes having varying ganglioside and protein composition.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

Formation of a cytosolic ganglioside‐protein complex following administration of photoreactive ganglioside GM1 to human fibroblasts in culture

et al. 1990

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A GM 1 ganglioside derivative bearing a photoreactive nitrophenyl azide group and tritium labeled at the acetyl group of N-acetylneuraminic acid, has been administered to cultured human fibroblasts. With photolabeling experiments we found that a portion of the ganglioside in the cell cytosol was associated with a soluble protein of about 30 kDa.Photoreactive GM 1; Cytosolic complex; Ganglioside-protein interaction

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Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

Formation of a cytosolic ganglioside‐protein complex following administration of photoreactive ganglioside GM1 to human fibroblasts in culture

et al. 1990

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“…1996), but very little is known about the mechanisms of escape from the lysosome and the transfer of these intermediates to the Golgi or other cellular districts, nor on the regulation of these processes. The presence of soluble ganglioside/protein complexes in the cytosol reported by some Authors (Sonnino et al. 1979, 1981, 1984; Chigorno et al.…”

Section: Glycosphingolipid Intracellular Traffic and Metabolismmentioning

confidence: 90%

Modulation of cell functions by glycosphingolipid metabolic remodeling in the plasma membrane

Prinetti

Chigorno

Mauri

et al. 2007

Journal of Neurochemistry

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The endoplasmic reticulum and the Golgi apparatus are the subcellular sites for glycosphingolipid neobiosynthesis. In addition to this very well-established knowledge, it is now emerging that post-Golgi changes in glycosphingolipid structures occurring at the plasma membrane are an important opportunity to modulate cell glycosphingolipid composition and to affect consequently a number of signaling processes. In fact, it is possible to modify very rapidly the membrane organization by the modulation of plasma membrane-associated enzymes through external stimuli, thus affecting the membrane environment and the functional properties of plasma membrane proteins involved in cell signaling. The number of enzymes for glycosphingolipid metabolism that have been shown to be associated with the plasma membrane and the information on their features are growing very rapidly, and today some of these enzymes have been deeply characterized. In this review, we focus on the possible role and on the involvement of these plasma membrane-associated enzymes in modulating cell functions.

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“…1) constitutes the primary type of sialoglycoconjugate in vertebrate neurons and is predominantly localized in the plasma membranes of those cells (Ledeen 1989;Ledeen and Wu 1992). There is also considerable evidence for the existence of intracellular pools (Sonnino et al 1981;Ledeen et al 1988;Gillard et al 1993), which, although quantitatively minor, may fulfill important signaling, transport, and regulatory functions. An early study reported gangliosides as being present in every subcellular fraction of bovine mammary gland and rat liver, the level in nuclei from the latter being comparable to that in total homogenate (Keenan et al 1972).…”

Section: Gangliosides Of the Cell And Nucleusmentioning

confidence: 98%

GM1 ganglioside: another nuclear lipid that modulates nuclear calcium. GM1 potentiates the nuclear sodium–calcium exchangerThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell.

Ledeen

2006

Can. J. Physiol. Pharmacol.

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The nuclear envelope (NE) enclosing the cell nucleus, although morphologically and chemically distinct from the plasma membrane, has certain features in common with the latter including the presence of GM1 as an important modulatory molecule. This ganglioside influences Ca(2+) flux across both membranes, but by quite different mechanisms. GM1 in the NE contributes to regulation of nuclear Ca(2+) through potentiation of a Na(+)/Ca(2+) exchanger in the inner nuclear membrane, whereas in the cell membrane, it regulates cytosolic Ca(2+) through modulation of a nonvoltage-gated Ca(2+) channel. Studies with neuroblastoma cells suggest GM1 concentration becomes elevated in the NE with onset of axonogenesis. However, the nuclear GM1/exchanger complex is not limited to neuronal cells but also occurs in NE of astrocytes, C6 cells, and certain non-neural cells. Immunoprecipitation and immunoblot experiments have shown high affinity association of the nuclear Na(+)/Ca(2+) exchanger with GM1, in contrast to Na(+)/Ca(2+) exchangers of the plasma membrane, which bind GM1 less avidly or not at all. This is believed to be due to different isoforms of the exchanger and a difference in topology of GM1 relative to the large inner loop of the exchanger in the 2 membranes. Cultured neurons from mice genetically engineered to lack GM1 suffered Ca(2+) dysregulation as seen in their high vulnerability to Ca(2+)-induced apoptosis. They were rescued by GM1 and more effectively by LIGA20, a membrane-permeant derivative of GM1. The mutant animals were highly susceptible to kainate-induced seizures, which are also a reflection of Ca(2+) dysregulation. The seizures were effectively attenuated by LIGA20 in parallel with the ability of this agent to enter brain cells, insert into the NE, and potentiate Na(+)/Ca(2+) exchange activity in the nucleus. The Na(+)/Ca(2+) exchanger of the NE, in association with nuclear GM1, is thus seen contributing to independent regulation of Ca(2+) by the nucleus in a manner that provides cytoprotection against Ca(2+)-induced apoptosis.

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Changes in Rabbit Brain Cytosolic and Membrane‐Bound Gangliosides During Prenatal Life

Cited by 51 publications

References 39 publications

Formation of a cytosolic ganglioside‐protein complex following administration of photoreactive ganglioside GM1 to human fibroblasts in culture

Formation of a cytosolic ganglioside‐protein complex following administration of photoreactive ganglioside GM1 to human fibroblasts in culture

Modulation of cell functions by glycosphingolipid metabolic remodeling in the plasma membrane

GM1 ganglioside: another nuclear lipid that modulates nuclear calcium. GM1 potentiates the nuclear sodium–calcium exchangerThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell.

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