Gangliosides in the human brain development and aging

Kračun, Ivica; Rösner, Harald; Drnovsek, Valerija; Vukelić, Željka; Ćosović, Čedomir; Trbojević-Čepe, Milica; Kubat, Milovan

doi:10.1016/0197-0186(92)90057-x

Cited by 103 publications

(73 citation statements)

References 36 publications

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“…Our findings suggest that decreasing GM 1 levels (reported to occur with age)7, 8a, 19 could lead to reduced protection from the oligomerization‐triggering effect of Sph and thus contribute to spark AD's onset. The provided molecular insights support reports on the neuroprotective effects of GM 1 in cell cultures and rat models of AD 9, 20.…”

mentioning

confidence: 74%

GM₁ Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

et al. 2016

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Abstractβ‐Amyloid (Aβ) oligomers are neurotoxic and implicated in Alzheimer's disease. Neuronal plasma membranes may mediate formation of Aβ oligomers in vivo. Membrane components sphingomyelin and GM1 have been shown to promote aggregation of Aβ; however, these studies were performed under extreme, non‐physiological conditions. We demonstrate that physiological levels of GM1, organized in nanodomains do not seed oligomerization of Aβ40 monomers. We show that sphingomyelin triggers oligomerization of Aβ40 and that GM1 is counteractive thus preventing oligomerization. We propose a molecular explanation that is supported by all‐atom molecular dynamics simulations. The preventive role of GM1 in the oligomerization of Aβ40 suggests that decreasing levels of GM1 in the brain, for example, due to aging, could reduce protection against Aβ oligomerization and contribute to the onset of Alzheimer's disease.

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confidence: 74%

GM₁ Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

et al. 2016

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“…Ganglioside composition is dependant on both species and cell type. Specific changes occur during brain development, maturation, and aging, and due to disease or neurodegeneration processes [21][22][23]. They are therefore regarded as tissue stage-and/or diagnostic markers, and therefore potentially as therapeutic agents.…”

mentioning

confidence: 99%

Fully-automated chip-based nanoelectrospray tandem mass spectrometry of gangliosides from human cerebellum

Zamfir

Vukelić

Bîndilă

et al. 2004

J. Am. Soc. Mass Spectrom.

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The introduction of chip-based electrospray (ESI) ion sources into biological mass spectrometry (MS) addressed the fundamental issue of how to analyze minute amounts of complex biological systems. The automation of sample delivery into the MS combined with the chip-based ESI allows for high quality bioanalysis in a high-throughput fashion. These advantages have already been demonstrated in proteomics, direct screening of drugs and drug discovery. As part of our continuing effort to implement automated chip-based mass spectrometry into the field of complex carbohydrate analysis, we hereby report the development of a chipESI MS and MS/MS methodology for the screening of gangliosides. A strategy to characterize a complex ganglioside mixture from human cerebellar tissue, by automated ESIchip-quadrupole time-of-flight (QTOF) MS and MS/MS is presented here. The feasibility of this method, and the general experimental requirements for automated chipESI MS analysis of these carbohydrate species is

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“…They are abundant components of the central nervous system and their compositions undergo changes during brain development, maturation, aging, and neurodegeneration processes [39][40][41]. For these reasons, gangliosides are considered as tissue stage or diagnostic markers and potentially therapeutic agents.…”

Section: Gangliosidesmentioning

confidence: 99%

Chip electrospray mass spectrometry for carbohydrate analysis

Zamfir¹,

Bîndilă²,

Lion³

et al. 2005

Electrophoresis

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Currently two types of chip systems are used in conjunction with MS: out-of-plane devices, where hundreds of nozzles, nanospray emitters are integrated onto a single silicon substrate from which electrospray is established perpendicular to the substrate, and planar microchips, embedding a microchannel at the end of which electrospray is generated in-plane, on the edge of the microchip. In the last two years, carbohydrate research greatly benefited from the introduction and implementation of the chip-based MS. In two laboratories the advantages of the chip electrospray in terms of ionization efficiency, sensitivity, reproducibility, quality of data in combination with high mass accuracy, and resolution of detection were systematically explored for several carbohydrate classes: O-and N-glycopeptides, oligosaccharides, gangliosides and glycoprotein-derived O-and N-glycans, and glycopeptides. The current state-of-the-art in interfacing the chip electrospray devices to high-performance MS for carbohydrate analysis, and the particular requirements for method optimization in both positive and negative ion modes are reviewed here. The recent applications of these miniaturized devices and their general potential for glycomic-based surveys are highlighted.

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Gangliosides in the human brain development and aging

Cited by 103 publications

References 36 publications

GM₁ Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

GM₁ Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

Fully-automated chip-based nanoelectrospray tandem mass spectrometry of gangliosides from human cerebellum

Chip electrospray mass spectrometry for carbohydrate analysis

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Gangliosides in the human brain development and aging

Cited by 103 publications

References 36 publications

GM1 Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

GM1 Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

Fully-automated chip-based nanoelectrospray tandem mass spectrometry of gangliosides from human cerebellum

Chip electrospray mass spectrometry for carbohydrate analysis

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Product

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GM₁ Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

GM₁ Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin