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Langman, L. J., A. B. Leichtman, W. F. Weitzel, and R. W. Yatscoff. "Steady-state concentration of cyclosporin G (OG37-325) and its metabolites in renal transplant recipients." Clinical Chemistry 40, no. 4 (April 1, 1994): 613–16. http://dx.doi.org/10.1093/clinchem/40.4.613.
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Abstract The steady-state concentrations of cyclosporin G (OG37-325) (CsG) and six of its metabolites (GM1, GM9, GM4N, GM1c, GM1c9, GM19) were measured throughout the 12-h dosing interval in six renal transplant recipients receiving CsG as prophylaxis against acute cellular rejection. The mean 12-h whole-blood trough concentrations (micrograms/L) were CsG, 131 +/- 26; GM1, 79 +/- 55; GM9, 110 +/- 114; GM4N, 28 +/- 18; GM1c, 31 +/- 18; GM1c9, 216 +/- 145; and GM19, 303 +/- 217. The relative concentration of the primary metabolites (GM1, GM9, GM4N) remained stable with respect to CsG throughout the dosing interval, whereas that of the secondary metabolites increased. The secondary metabolites GM19 and GM1c9 exhibited extensive between-patient variation. We investigated the effect of these metabolites on commercially available monoclonal antibody-based fluorescence polarization immunoassays (FPIA) and RIAs adapted for measurement of CsG. The 12-h whole-blood trough concentrations measured by FPIA and RIA exceed those measured by HPLC by 19% and 36%, respectively. These measured biases corresponded closely with the calculated biases (FPIA 19%, RIA 28%) based on the known cross-reactivities of CsG metabolites and their concentrations. These results suggest that cross-reactivity with metabolites account for a large part of the bias observed in immunoassays of CsG.
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Yamazaki, Yasuhiro, Yasuhiro Horibata, Yasuko Nagatsuka, Yoshio Hirabayashi, and Tsutomu Hashikawa. "Fucoganglioside α-fucosyl(α-galactosyl)-GM1: a novel member of lipid membrane microdomain components involved in PC12 cell neuritogenesis." Biochemical Journal 407, no. 1 (September 12, 2007): 31–40. http://dx.doi.org/10.1042/bj20070090.
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In order to search for novel components of lipid membrane microdomains involved in neural signalling pathways, mAbs (monoclonal antibodies) were raised against the detergent-insoluble membrane fraction of PC12 (pheochromocytoma) cells. Among the 22 hybrid clones, mAb PR#1 specifically detected a fucoganglioside Fuc(Gal)-GM1 [α-fucosyl(α-galactosyl)-GM1], a ganglioside homologous with GM1a (II3NeuAc,GgOse4Cer), as a novel member of microdomain components with biological functions. In the presence of mAb PR#1 in the culture medium, the outgrowth of neurites was induced in PC12 cells in a dose-dependent manner, with no effects on cell proliferation, suggesting that Fuc(Gal)-GM1 is preferentially involved in PC12 cell neuritogenesis. Effects through Fuc(Gal)-GM1 were different from those through GM1a during differentiation, e.g. under PR#1 treatment on Fuc(Gal)-GM1, round cell bodies with thinner cell processes were induced, whereas treatment with CTB (cholera toxin B subunit), a specific probe for GM1a, produced flattened cell bodies with thicker pro-cesses. Molecular analysis demonstrated that the PR#1–Fuc(Gal)-GM1 pathway was associated with Fyn and Yes of the Src family of kinases, although Src itself was not involved. No association was found with TrkA (tropomyosin receptor kinase A) and ERKs (extracellular-signal-regulated kinases), which are responsible for GM1a-induced differentiation. From these findings, it is suggested that a fucoganglioside Fuc(Gal)-GM1 provides a functional platform distinct from that of GM1a for signal transduction in PC12 cell differentiation.
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Alrebdi, Haifa I., and Thabit Barakat. "The Radiative Δ(1600) → γN Decay in the Light-Cone QCD Sum Rules." Universe 7, no. 8 (July 21, 2021): 255. http://dx.doi.org/10.3390/universe7080255.
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Within the framework of the light-cone QCD sum rules method (LCSR’s), the radiative Δ(1600)→γN decay is studied. In particular, the magnetic dipole moment GM1(0) and the electric quadrupole moment GE1(0) are estimated. We also calculate the ratio REM=−GE1(0)GM1(0) and the decay rate. The predicted multipole moments and the decay rate strongly agree with the existing experimental results as well as with the other available phenomenological approaches.
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IWAMORI, Masao, and Steven E. DOMINO. "Tissue-specific loss of fucosylated glycolipids in mice with targeted deletion of alpha(1,2)fucosyltransferase genes." Biochemical Journal 380, no. 1 (May 15, 2004): 75–81. http://dx.doi.org/10.1042/bj20031668.
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Glycolipids in epithelial tissues of the gastrointestinal tract act as receptors for enteric bacteria and are implicated in the activation of the intestinal immune system. To clarify the genes involved in the fucosylation of the major glycolipids, substrate glycolipids and fucosylated products were measured in tissues of wild-type and mutant mice lacking α(1,2)fucosyltransferase genes FUT1 or FUT2. Quantitative determination was performed by TLC-immunostaining for GA1 (Gg4Cer), FGA1 (fucosyl GA1), GM1 (II3NeuAc-Gg4Cer), FGM1 (fucosyl GM1), and Forssman glycolipids. Both FGM1 and FGA1 completely disappeared from the antrum, cecum, and colon of FUT2-null mice, but not those of FUT1-null and wild-type mice. Precursor glycolipids, GM1 and GA1, accumulated in tissues of FUT2-null mice, indicating that the FUT2-encoded enzyme preferentially participates in the fucosylation of GA1 and GM1 in these tissues. Female reproductive organs were similarly found to utilize FUT2 for the fucosylation of glycolipids FGA1 (uterus and cervix), and FGM1 (ovary), due to their absence in FUT2-null mice. In FUT1-null mice FGA1 was lost from the pancreas, but was present in wild-type and FUT2-null mice, indicating that FUT1 is essential for fucosylation of GA1 in the pancreas. Ulex europaeus agglutinin-I lectin histochemistry for α(1,2)fucose residues confirmed the absence of α(1,2)fucose residues from the apical surface of pancreatic acinar glands of FUT1-null mice. Ileum, epididymis, and testis retained specific fucosylated glycolipids, irrespective of targeted deletion of either gene, indicating either compensation for or redundancy of the α(1,2)fucosyltransferase genes in these tissues.
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Bisel, Blaine, Francesco S. Pavone, and Martino Calamai. "GM1 and GM2 gangliosides: recent developments." BioMolecular Concepts 5, no. 1 (March 1, 2014): 87–93. http://dx.doi.org/10.1515/bmc-2013-0039.
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AbstractGM1 and GM2 gangliosides are important components of the cell membrane and play an integral role in cell signaling and metabolism. In this conceptual overview, we discuss recent developments in our understanding of the basic biological functions of GM1 and GM2 and their involvement in several diseases. In addition to a well-established spectrum of disorders known as gangliosidoses, such as Tay-Sachs disease, more and more evidence points at an involvement of GM1 in Alzheimer’s and Parkinson’s diseases. New emerging methodologies spanning from single-molecule imaging in vivo to simulations in silico have complemented standard studies based on ganglioside extraction.
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&NA;. "GM1." Inpharma Weekly &NA;, no. 839 (May 1992): 11. http://dx.doi.org/10.2165/00128413-199208390-00017.
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Sugimoto, Mamoru, Masaaki Numata, Katsuya Koike, Yoshiaki Nakahara, and Tomoya Ogawa. "Total synthesis of gangliosides GM1 and GM2." Carbohydrate Research 156 (November 1986): C1—C5. http://dx.doi.org/10.1016/s0008-6215(00)90125-3.
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Park, Hyun Jung, Gil-Ja Jhon, Seong Jun Han, and Young Kee Kang. "Conformational study of asialo-GM1 (GA1) ganglioside." Biopolymers 42, no. 1 (July 1997): 19–35. http://dx.doi.org/10.1002/(sici)1097-0282(199707)42:1<19::aid-bip3>3.0.co;2-4.
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LI, Su-Chen, Yu-Teh LI, Setsuko MORIYA, and Taeko MIYAGI. "Degradation of GM1 and GM2 by mammalian sialidases." Biochemical Journal 360, no. 1 (November 8, 2001): 233–37. http://dx.doi.org/10.1042/bj3600233.
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In mammalian tissues, the pathway known for the catabolism ofGM1[Galβ3GalNAcβ4(Neu5Acα3)Galβ4GlcCer;where Cer is ceramide] is the conversion of this ganglioside into GM2 [GalNAcβ4(Neu5Acα3)Galβ4GlcβCer] by β-galactosidase followed by the conversion of GM2 into GM3 (Neu5Acα3Galβ4GlcβCer) by β-N-acetylhexosaminidase A (Hex A). However, the question of whether or not GM1 and GM2 can also be respectively converted into asialo-GM1 (Galβ3GalNAcβ4Galβ4GlcCer; GA1) and asialo-GM2 (GalNAcβ4Galβ4GlcβCer, GA2) by mammalian sialidases has not been resolved. This is due to the fact that sialidases purified from mammalian tissues always contained detergents that interfered with the in vitro hydrolysis of GM1 and GM2 in the presence of an activator protein. The mouse model of human type B Tay–Sachs disease created by the disruption of the Hexa gene showed no neurological abnormalities, with milder clinical symptoms than the human counterpart, and the accumulation of GM2 in the brains of affected mice was only limited to certain regions [Sango, Yamanaka, Hoffmann, Okuda, Grinberg, Westphal, McDonald, Crawley, Sandhoff, Suzuki and Proia (1995) Nat. Genet. 11, 170–176]. These results suggest the possible presence of an alternative catabolic pathway (the GA2 pathway) in mouse to convert GM2 into GA2 by sialidase. To show the existence of this pathway, we have used recombinant mammalian cytosolic sialidase and membrane-associated sialidase to study the desialylation of GM1 and GM2. We found that the mouse membrane-bound sialidase was able to convert GM1 and GM2 into their respective asialo-derivatives in the presence of human or mouse GM2 activator protein. The cytosolic sialidase did not exhibit this activity. Our results suggest that, in vivo, the stable NeuAc of GM1 and GM2 may be removed by the mammalian membrane-associated sialidase in the presence of GM2 activator protein. They also support the presence of the GA2 pathway for the catabolism of GM2 in mouse.
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Santi, P. A., P. Mancini, and C. Barnes. "Identification and localization of the GM1 ganglioside in the cochlea using thin-layer chromatography and cholera toxin." Journal of Histochemistry & Cytochemistry 42, no. 6 (June 1994): 705–16. http://dx.doi.org/10.1177/42.6.8189033.
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Using high-performance thin-layer chromatography, we identified GM1, GM3, GD3, GD1a, GT1b, GQ1b, and other gangliosides in chinchilla cochlea and cerebellum. GM1 was also identified on chromatograms with the B-subunit of cholera toxin (BCT). BCT was also used to determine the distribution of GM1 in fixed and unfixed tissues from cochlea, cerebellum, and sciatic nerve. Positive control tissues showed expected labeling of GM1 by BCT. Negative controls showed expected suppression of BCT binding to GM1 after GM1 extraction and GM1 absorption. In the cochlea, GM1 appeared abundant in plasma membranes of most epithelial cells lining the endolymphatic surface of the scala media, including the interdental, inner supporting, pillar, Deiters, Hensen, Claudius, Boettcher, spiral prominence, and external sulcus. GM1 appeared less abundant in cells of the stria vascularis, Reissner's membrane, and in nerve fibers. In hair cells, the stereocilia appeared to contain GM1; however, the endolymphatic surface of the cuticular plate and the body of the outer hair cells appeared to contain little GM1. In addition, the tectorial membrane, connective tissue of the spiral limbus, and amorphous layer of the basilar membrane also appeared to contain little GM1. Enzymatic degradation of glycoproteins and transformation of polysialogangliosides to GM1 increased the reactivity of BCT to cochlear GM1. This further supported the presence of GM1 and other gangliosides in the cochlea. Although the functional significance of GM1 and other gangliosides in the cochlea is not yet known, they are likely to play important roles in membrane function.
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Barros Filho, Tarcísio Eloy Pessoa, and Ciro da Silva Filho. "Titration of serum anti-ganglioside antibodies in patients with chronic medular injury previous to treatment with GM1 ganglioside." Acta Ortopédica Brasileira 11, no. 2 (April 2003): 69–71. http://dx.doi.org/10.1590/s1413-78522003000200001.
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Anti-ganglioside serum titers were evaluated by ELISA in 150 patients with complete spinal cord lesion for 6 to 12 months (IgG monosialo GM1, IgM monosialo GM1, IgG asialo GM1, IgM asialo GM1, IgG disialo GD1b e IgM disialo GD1b) prior to treatment with GM1 100 mg/day i.m. Only 4 patients showed positive titers for anti-asialo-GM1 (IgM) antibodies . All patients were clinically examined during and after treatment. No important side effects were observed with GM1 therapy. These results suggest that GM1-ganglioside administration in patients with chronic spinal cord injury is safe.
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Eikelberg, Deborah, Annika Lehmbecker, Graham Brogden, Witchaya Tongtako, Kerstin Hahn, Andre Habierski, Julia B. Hennermann, et al. "Axonopathy and Reduction of Membrane Resistance: Key Features in a New Murine Model of Human GM1-Gangliosidosis." Journal of Clinical Medicine 9, no. 4 (April 2, 2020): 1004. http://dx.doi.org/10.3390/jcm9041004.
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GM1-gangliosidosis is caused by a reduced activity of β-galactosidase (Glb1), resulting in intralysosomal accumulations of GM1. The aim of this study was to reveal the pathogenic mechanisms of GM1-gangliosidosis in a new Glb1 knockout mouse model. Glb1−/− mice were analyzed clinically, histologically, immunohistochemically, electrophysiologically and biochemically. Morphological lesions in the central nervous system were already observed in two-month-old mice, whereas functional deficits, including ataxia and tremor, did not start before 3.5-months of age. This was most likely due to a reduced membrane resistance as a compensatory mechanism. Swollen neurons exhibited intralysosomal storage of lipids extending into axons and amyloid precursor protein positive spheroids. Additionally, axons showed a higher kinesin and lower dynein immunoreactivity compared to wildtype controls. Glb1−/− mice also demonstrated loss of phosphorylated neurofilament positive axons and a mild increase in non-phosphorylated neurofilament positive axons. Moreover, marked astrogliosis and microgliosis were found, but no demyelination. In addition to the main storage material GM1, GA1, sphingomyelin, phosphatidylcholine and phosphatidylserine were elevated in the brain. In summary, the current Glb1−/− mice exhibit a so far undescribed axonopathy and a reduced membrane resistance to compensate the functional effects of structural changes. They can be used for detailed examinations of axon–glial interactions and therapy trials of lysosomal storage diseases.
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Yohe, H. C., C. L. Cuny, L. J. Macala, M. Saito, W. J. McMurray, and J. L. Ryan. "The presence of sialidase-sensitive sialosylgangliotetraosyl ceramide (GM1b) in stimulated murine macrophages. Deficiency of GM1b in Escherichia coli-activated macrophages from the C3H/HeJ mouse." Journal of Immunology 146, no. 6 (March 15, 1991): 1900–1908. http://dx.doi.org/10.4049/jimmunol.146.6.1900.
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Abstract The stimulated murine macrophage was found to contain 11 major gangliosides of which 8 were determined to be monosialylated. The thin-layer chromatographic patterns were complicated by the presence of both sialic acid and ceramide fatty acid heterogeneity. N-glycolyl and N-acetylneuraminic acid-containing species were present for each ganglioside characterized. Although C18 sphingosine was the only long chain base detected, ceramide fatty acid ranged from C16 to C24 carbon moieties. Based on gas-liquid chromatographic and antibody analyses, all major tetraosyl structure gangliosides were ganglio series types. Comprising 43 to 60% of thioglycollate-stimulated cells and 60 to 70% of Escherichia coli-activated cells, monosialosyl-gangliotetraosyl ceromides (Gm1 gangliosides) were the major monosialo species of which four were present: sialidase-resistant NeuGc-GM1a and NeuAc-GM1a and sialidase sensitive NeuGc-GM1b and NeuAc-GM1b. Analyses of thioglycollate-elicited murine peritoneal macrophage ganglioside patterns from four strains of mice, including the C3H/HeJ strain, indicated that, in the absence of any expression of a genetic defect, the pattern is conserved. However, when E. coli was used as the activating agent, the normal C3H/HeN macrophage contained little Gm1a with the sialidase-sensitive Gm1b predominant; the converse was true for the congenic endotoxin hyporesponsive C3H/HeJ strain. Therefore, C3H/HeJ mice are not defective in ganglioside metabolism per se but in the processing of an endotoxin stimulus such that one manifestation is an altered macrophage ganglioside pattern deficient in Gm1b.
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Pestronk, Alan, and Rati Choksi. "Multifocal motor neuropathy." Neurology 49, no. 5 (November 1997): 1289–92. http://dx.doi.org/10.1212/wnl.49.5.1289.
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IgM anti-GM1 antibodies occur with increased frequency in the serum of patients with multifocal motor neuropathy (MMN). We tested the ability of serum IgM from patients with MMN to bind to GM1 ganglioside covalently bound to secondary amino groups on ELISA plates (Co-GM1). The Co-GM1 technique detected high titer (>1,800), selective, serum IgM binding to GM1 ganglioside in 85% of our MMN patients (23/27), a significantly greater frequency compared with figures of 37% and 52% found using our previous testing methods. Selective IgM anti-GM1 antibodies showed disease specificity. The only other patients with selective, high-titer IgM anti-GM1 antibodies had either chronic motor neuropathy without conduction block or acute immune neuropathy in China. No patient from the amyotrophic lateral sclerosis, chronic inflammatory demyelinating polyneuropathy, Guillain-Barré, or systemic immune disorder control groups had selective IgM anti-GM1 antibodies at titers greater than 1,800 detected using Co-GM1 ganglioside as ELISA antigen. Titers of IgM anti-GM1 antibodies in MMN(averaging 31,000 ± 15,000) were more than fourfold higher with Co-GM1 than with previous anti-GM1 assay methods, using conventional ELISA plates with GM-1 antigen alone (7,200 ± 4,400) or in a lipid environment(3,600 ± 1,300). We conclude that using ELISA testing with Co-GM1 antigen, serum anti-GM1 autoantibodies are a useful marker for MMN, because they are present in 85% of MMN patients and, at titers greater than 1,800, have strong specificity for immune-mediated motor neuropathies.
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Ghidoni, R., M. Trinchera, B. Venerando, A. Fiorilli, S. Sonnino, and G. Tettamanti. "Incorporation and metabolism of exogenous GM1 ganglioside in rat liver." Biochemical Journal 237, no. 1 (July 1, 1986): 147–55. http://dx.doi.org/10.1042/bj2370147.
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The pathways of metabolic processing of exogenously administered GM1 ganglioside in rat liver was investigated at the subcellular level. The GM1 used was 3H-labelled at the level of long-chain base ([Sph(sphingosine)-3H]GM1) or of terminal galactose ([Gal-3H]GM1). The following radioactive compounds, derived from exogenous GM1, were isolated and chemically characterized: gangliosides GM2, GM3, GD1a and GD1b (nomenclature of Svennerholm [(1964) J. Lipid Res. 5, 145-155] and IUPAC-IUB Recommendations [(1977) Lipids 12, 455-468]); lactosylceramide, glucosylceramide and ceramide; sphingomyelin. GM2, GM3, lactosylceramide, glucosylceramide and ceramide, relatively more abundant shortly after GM1 administration, were mainly present in the lysosomal fraction and reflected the occurrence of a degradation process. 3H2O was also produced in relevant amounts, indicating complete degradation of GM1, although no free long-chain bases could be detected. GD1a and GD1b, relatively more abundant later on after administration, were preponderant in the Golgi-apparatus fraction and originated from a biosynthetic process. More GD1a was produced starting from [Sph-3H]GM1 than from [Gal-3H]GM1, and radioactive GD1b was present only after [Sph-3H]GM1 injection. This indicates the use of two biosynthetic routes, one starting from a by-product of GM1 degradation, the other implicating direct sialylation of GM1. Both routes were used to produce GD1a, but only the first one for producing GD1b. Sphingomyelin was the major product of GM1 processing, especially at the longer times after injection, and arose from a by-product of GM1 degradation, most likely ceramide.
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Suttles, J., G. A. Schwarting, and R. D. Stout. "Flow cytometric analysis reveals the presence of asialo GM1 on the surface membrane of alloimmune cytotoxic T lymphocytes." Journal of Immunology 136, no. 5 (March 1, 1986): 1586–91. http://dx.doi.org/10.4049/jimmunol.136.5.1586.
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Abstract Previous studies have demonstrated that natural killer (NK) cells express the glycolipid asialo GM1, as evidenced by the sensitivity of NK cells to treatment with anti-asialo GM1 serum and complement. Because alloimmune cytotoxic T lymphocytes (CTL) were found to be insensitive to treatment with anti-asialo GM1 serum and complement, it was concluded that asialo GM1 is expressed by NK but not by CTL. However, fluorescence studies indicated that a significant proportion of peripheral T cells did express asialo GM1. Flow cytometric studies were undertaken to determine the extent to which alloimmune CTL express asialo GM1. Affinity-purified, monospecific IgG anti-asialo GM1 antibodies were used to label cells from mixed lymphocyte cultures. Separation of asialo GM1-positive and -negative fractions by cell sorting revealed that the majority of CTL activity resides in the asialo GM1-positive population. When these studies are compared with similar studies of splenic NK activity, it is apparent that, despite the relative insensitivity of CTL to treatment with anti-asialo GM1 and complement, both CTL and NK activity are enriched in the asialo GM1-positive cell population obtained by cell sorting.
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LI, Su-Chen, Yu-Teh LI, Setsuko MORIYA, and Taeko MIYAGI. "Degradation of GM1 and GM2 by mammalian sialidases." Biochemical Journal 360, no. 1 (November 15, 2001): 233. http://dx.doi.org/10.1042/0264-6021:3600233.
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Rabin, Stuart J., Alessia Bachis, and Italo Mocchetti. "Gangliosides Activate Trk Receptors by Inducing the Release of Neurotrophins." Journal of Biological Chemistry 277, no. 51 (October 17, 2002): 49466–72. http://dx.doi.org/10.1074/jbc.m203240200.
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We used NIH-3T3 fibroblasts expressing the different Trk receptors to examine whether GM1 ganglioside and its semisynthetic derivative LIGA20 activate various neurotrophin receptors. GM1 induced autophosphorylation of TrkC more potently than TrkA or TrkB receptors. In contrast, LIGA20 activated TrkB tyrosine phosphorylation only. Therefore, Scatchard analysis was performed to determine whether GM1 binds to TrkC. GM1 failed to displace neurotrophin-3 binding, suggesting that this ganglioside does not act as a ligand for Trk receptors. In addition, GM1 failed to induce autophosphorylation of a chimeric receptor consisting of the extracellular domain of the tumor necrosis factor receptor and the intracellular domain of TrkA, suggesting that GM1 does not affect the tyrosine kinase domain. We next determined whether GM1 induces the release of neurotrophins from fibroblast cells. GM1 induced a rapid and significant increase in the amount of neurotrophin-3, but not other neurotrophins. This effect was independent of the presence of Trk because K252a did not prevent GM1-mediated release of neurotrophin-3. Moreover, GM1-mediated TrkC autophosphorylation was blocked by TrkC-IgG (but not TrkB-IgG) receptor bodies, further suggesting that GM1 activates TrkC by inducing the release of neurotrophin-3. This hypothesis was also tested in cultured cerebellar granule cells. GM1 induced neurotrophin-3 (but not brain-derived neurotrophic factor or nerve growth factor) release. In contrast, LIGA20 increased the secretion of brain-derived neurotrophic factor. Our data show that gangliosides may activate different Trk receptors by differentially affecting the release of neurotrophins.
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Weng, N. P., L. Y. Yu-Lee, I. Sanz, B. M. Patten, and D. M. Marcus. "Structure and specificities of anti-ganglioside autoantibodies associated with motor neuropathies." Journal of Immunology 149, no. 7 (October 1, 1992): 2518–29. http://dx.doi.org/10.4049/jimmunol.149.7.2518.
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Abstract Autoantibodies that bind to GM1 ganglioside and asialo GM1 (GA1) have been implicated in the pathogenesis of motor neuropathies. To investigate the structure and specificity of these autoantibodies, peripheral blood B cells from patients with motor neuron diseases and from normal individuals were immortalized by EBV, and B cells secreting anti-GM1 or GA1 antibodies were cloned. We report an analysis of the structure and specificities of eight autoantibodies from patients with motor neuropathy, and two from normal individuals. Four antibodies were IgM, six were IgG, and all bound predominantly to GA1. The sequences of V domains of H and L chains were determined by a reverse transcription-polymerase chain reaction procedure. A variety of V genes were used to encode these antibodies: four VH1, two VH3, three VH4, one VH5, two V kappa I, two V kappa II, three V kappa III, and two V lambda II. Most V genes (13/19) exhibited less than 95% similarity to known germ-line genes, which suggests that somatic mutation was required to generate these autoantibodies, or that the relevant germ-line genes have not been identified. The average length of the H chain CDR3 was 16 amino acids, and in three antibodies this segment contained more than 20 amino acids. It was not possible to identify amino acid sequences that were encoded by germ-line D segments by conventional alignment of sequences. Partial analogies could be identified by introducing gaps, allowing mismatches and searching for D-D fusions and inversions. These results indicate that anti-GA1 antibodies can be encoded by a variety of VH-VL pairs, that the antibodies exhibit extensive somatic mutation, and that the CDR3 segments are generated by a number of nonconventional mechanisms.
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Satoh, Hiroyuki, Toyofumi Yamauchi, Masahiro Yamasaki, Yoshimitsu Maede, Akira Yabuki, Hye-Sook Chang, Taketoshi Asanuma, and Osamu Yamato. "Rapid detection of GM1 ganglioside in cerebrospinal fluid in dogs with GM1 gangliosidosis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry." Journal of Veterinary Diagnostic Investigation 23, no. 6 (October 24, 2011): 1202–7. http://dx.doi.org/10.1177/1040638711425592.
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The concentration of GM1 (monosialotetrahexosyl ganglioside) in cerebrospinal fluid (CSF) is markedly increased in dogs with GM1 gangliosidosis due to GM1 accumulation in the central nervous system and leakage to the CSF. The present study established a rapid and simple method for detection of accumulated GM1 in the CSF in dogs with GM1 gangliosidosis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI TOF MS) and discusses the usefulness of this method for the rapid diagnosis and/or high-risk screening of this disease in domestic animals. Cerebrospinal fluid was collected from normal dogs and 4- to 11-month-old Shiba dogs with GM1 gangliosidosis. The MALDI TOF MS analysis was carried out in combination with a special sample plate and a simple desalting step on the plate. Specific signs of GM1 could be detected in the standard GM1 solutions at concentrations of 50 nmol/l or more. The signs were also clearly detected in CSF (131–618 nmol/l) in affected dogs, but not in normal canine CSF (12 ± 5 nmol/l, mean ± standard deviation). The results demonstrated that MALDI TOF MS can detect GM1 accumulated in canine CSF even in the early stage of the disease. In conclusion, the rapid detection of increased CSF GM1 using MALDI TOF MS is a useful method for diagnosis and/or screening for canine GM1 gangliosidosis.
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Yagi-Utsumi, Maho, Koichi Matsuo, Katsuhiko Yanagisawa, Kunihiko Gekko, and Koichi Kato. "Spectroscopic Characterization of Intermolecular Interaction of AmyloidβPromoted on GM1 Micelles." International Journal of Alzheimer's Disease 2011 (2011): 1–8. http://dx.doi.org/10.4061/2011/925073.
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Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloidβ(Aβ) to its toxicβ-structured aggregates. We have previously shown that Aβ(1–40) accommodated on the hydrophobic/hydrophilic interface of lyso-GM1 or GM1 micelles assumesα-helical structures under ganglioside-excess conditions. For better understanding of the mechanisms underlying theα-to-βconformational transition of Aβon GM1 clusters, we performed spectroscopic characterization of Aβ(1–40) titrated with GM1. It was revealed that the thioflavin T- (ThT-) reactiveβ-structure is more populated in Aβ(1–40) under conditions where the Aβ(1–40) density on GM1 micelles is high. Under this circumstance, the C-terminal hydrophobic anchor Val39-Val40shows two distinct conformational states that are reactive with ThT, while such Aβspecies were not generated by smaller lyso-GM1 micelles. These findings suggest that GM1 clusters promote specific Aβ-Aβinteractions through their C-termini coupled with formation of the ThT-reactiveβ-structure depending on sizes and curvatures of the clusters.
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Lunghi, Giulia, Maria Fazzari, Erika Di Biase, Laura Mauri, Sandro Sonnino, and Elena Chiricozzi. "Modulation of calcium signaling depends on the oligosaccharide of GM1 in Neuro2a mouse neuroblastoma cells." Glycoconjugate Journal 37, no. 6 (November 17, 2020): 713–27. http://dx.doi.org/10.1007/s10719-020-09963-7.
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AbstractRecently, we demonstrated that the oligosaccharide portion of ganglioside GM1 is responsible, via direct interaction and activation of the TrkA pathway, for the ability of GM1 to promote neuritogenesis and to confer neuroprotection in Neuro2a mouse neuroblastoma cells. Recalling the knowledge that ganglioside GM1 modulates calcium channels activity, thus regulating the cytosolic calcium concentration necessary for neuronal functions, we investigated if the GM1-oligosaccharide would be able to overlap the GM1 properties in the regulation of calcium signaling, excluding a specific role played by the ceramide moiety inserted into the external layer of plasma membrane. We observed, by calcium imaging, that GM1-oligosaccharide administration to undifferentiated Neuro2a cells resulted in an increased calcium influx, which turned out to be mediated by the activation of TrkA receptor. The biochemical analysis demonstrated that PLCγ and PKC activation follows the TrkA stimulation by GM1-oligosaccharide, leading to the opening of calcium channels both on the plasma membrane and on intracellular storages, as confirmed by calcium imaging experiments performed with IP3 receptor inhibitor. Subsequently, we found that neurite elongation in Neuro2a cells was blocked by subtoxic administration of extracellular and intracellular calcium chelators, suggesting that the increase of intracellular calcium is responsible of GM1-oligosaccharide mediated differentiation. These results suggest that GM1-oligosaccharide is responsible for the regulation of calcium signaling and homeostasis at the base of the neuronal functions mediated by plasma membrane GM1.
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Schroeder, Torsten H., Tanweer Zaidi, and Gerald B. Pier. "Lack of Adherence of Clinical Isolates ofPseudomonas aeruginosa to Asialo-GM1 on Epithelial Cells." Infection and Immunity 69, no. 2 (February 1, 2001): 719–29. http://dx.doi.org/10.1128/iai.69.2.719-729.2001.
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ABSTRACT Numerous studies have reported that asialo-GM1, gangliotetraosylceramide, or moieties serve as epithelial cell receptors for Pseudomonas aeruginosa. Usually this interaction is confirmed with antibodies to asialo-GM1. However, few, if any, of these reports have evaluated the binding of fresh clinical isolates of P. aeruginosa to asialo-GM1 or the specificity of the antibodies for the asialo-GM1 antigen. We confirmed that asialo-GM1 dissolved in dimethyl sulfoxide could be added to the apical membrane of Madin-Darby canine kidney cells growing as a polarized epithelium on Transwell membranes (J. C. Comolli, L. L. Waite, K. E. Mostov, and J. N. Engel, Infect. Immun. 67:3207–3214, 1999) and that such treatment enhanced the binding of P. aeruginosa strain PA103. However, no otherP. aeruginosa strain, including eight different clinical isolates, exhibited enhanced binding to asialo-GM1-treated cells. Studies with commercially available antibodies to asialo-GM1 showed that these preparations had high titers of antibody to P. aeruginosa antigens, including whole cells, purified lipopolysaccharide (LPS), and pili. Inhibition studies showed that adsorption of an antiserum to asialo-GM1 withP. aeruginosa cells could remove the reactivity of antibodies to asialo-GM1, and adsorption of this serum with asialo-GM1 removed antibody binding to P. aeruginosa LPS. Antibodies in sera raised to asialo-GM1 were observed to bind to P. aeruginosa cells by immunoelectron microscopy. Antibodies to asialo-GM1 inhibited formation of a biofilm by P. aeruginosa in the absence of mammalian cells, indicating a direct inhibition of bacterial cell-cell interactions. These findings demonstrate that asialo-GM1 is not a major cellular receptor for clinical isolates of P. aeruginosa and that commercially available antibodies raised to this antigen contain high titers of antibody to multiple P. aeruginosa antigens, which do not interfere with the binding of P. aeruginosa to mammalian cells but possibly interfere with the binding of P. aeruginosa cells to each other.
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Constantini, Shlomo, and Wise Young. "The effects of methylprednisolone and the ganglioside GM1 on acute spinal cord injury in rats." Journal of Neurosurgery 80, no. 1 (January 1994): 97–111. http://dx.doi.org/10.3171/jns.1994.80.1.0097.
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✓ Recent clinical trials have reported that methylprednisolone sodium succinate (MP) or the monosialic ganglioside GM1 improves neurological recovery in human spinal cord injury. Because GM1 may have additive or synergistic effects when used with MP, the authors compared MP, GM1, and MP+GM1 treatments in a graded rat spinal cord contusion model. Spinal cord injury was caused by dropping a rod weighing 10 gm from a height of 1.25, 2.5, or 5.0 cm onto the rat spinal cord at T-10, which had been exposed via laminectomy. The lesion volumes were quantified from spinal cord Na and K shifts at 24 hours after injury and the results were verified histologically in separate experiments. A single dose of MP (30 mg/kg), given 5 minutes after injury, reduced 24-hour spinal cord lesion volumes by 56% (p = 0.0052), 28% (p = 0.0065), and 13% (p > 0.05) in the three injury-severity groups, respectively, compared to similarly injured control groups treated with vehicle only. Methylprednisolone also prevented injury-induced hyponatremia and increased body weight loss in the spine-injured rats. When used alone, GM1 (10 to 30 mg/kg) had little or no effect on any measured variable compared to vehicle controls; when given concomitantly with MP, GM1 blocked the neuroprotective effects of MP. At a dose of 3 mg/kg, GM1 partially prevented MP-induced reductions in lesion volumes, while 10 to 30 mg/kg of GM1 completely blocked these effects of MP. The effects of MP on injury-induced hyponatremia and body weight loss were also blocked by GM1. Thus, GM1 antagonized both central and peripheral effects of MP in spine-injured rats. Until this interaction is clarified, the authors recommend that MP and GM1 not be used concomitantly to treat acute human spinal cord injury. Because GM1 modulates protein kinase activity, protein kinases inhibit lipocortins, and lipocortins mediate anti-inflammatory effects of glucocorticoids, it is proposed that the neuroprotective effects of MP are partially due to anti-inflammatory effects and that GM1 antagonizes the effects of MP by inhibiting lipocortin. Possible beneficial effects of GM1 reported in central nervous system injury may be related to the effects on neural recovery rather than acute injury processes.
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Gouy, H., P. Deterre, P. Debré, and G. Bismuth. "Cell calcium signaling via GM1 cell surface gangliosides in the human Jurkat T cell line." Journal of Immunology 152, no. 7 (April 1, 1994): 3271–81. http://dx.doi.org/10.4049/jimmunol.152.7.3271.
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Abstract The cell surface ganglioside GM1 is the specific receptor for the B subunit of cholera toxin. We show here that in the human Jurkat T cell line an increase in intracellular free Ca2+ concentration can be elicited by using B subunits to ligate GM1 molecules. This Ca2+ signaling effect is clearly mediated through GM1 because it can be observed after direct insertion of exogenous GM1 in a Jurkat cell variant deficient in GM1 expression. The observed Ca2+ response clearly involves both the release of Ca2+ from intracellular stores and a Ca2+ influx from extracellular spaces. It is sustained in the presence of 1 mM extracellular Ca2+, whereas it becomes transient in Ca(2+)-free medium. We show that the GM1-mediated stimulation partially empties the CD3-dependent and inositol 1,4,5-trisphosphate-sensitive intracellular Ca2+ pool suggesting a dependence of the Ca2+ response from activation of phospholipase C (PLC) metabolism. Accordingly, tyrosine phosphorylation of PLC gamma-1 can be evidenced but only in Jurkat cells highly expressing GM1. GM1 stimulation results in an IL-2 production comparable to that obtained after CD3 activation. Finally, the GM1-linked cell Ca2+ activation pathway is also observed in a Jurkat cell clone lacking Ag-specific receptor expression suggesting that the presence of functional CD3/TCR molecules is not essential for GM1-induced cell Ca2+ response. Altogether, these data show that cell surface gangliosides GM1 may act as a signaling molecule in Jurkat T cells possibly by a new pathway, a finding of importance when considering a possible function for ubiquitous membrane carbohydrate structures in T cell recognition systems.
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Basu, Ipsita, and Chaitali Mukhopadhyay. "In silico phase separation in the presence of GM1 in ternary and quaternary lipid bilayers." Physical Chemistry Chemical Physics 17, no. 26 (2015): 17130–39. http://dx.doi.org/10.1039/c5cp01970b.
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Using coarse grain molecular dynamics simulations, the spontaneous phase separation in the ternary (POPC [1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine]/cholesterol/GM1) and quaternary (POPC/PSM[palmitoyl sphingomyelin]/cholesterol/GM1) lipid bilayers into liquid ordered (Lo) and liquid disordered (Ld) domains, due to self-aggregation of GM1 molecules and co-localization of cholesterol with GM1 in accordance with experiments, is studied.
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Ledeen, Robert, Suman Chowdhury, Zi-Hua Lu, Monami Chakraborty, and Gusheng Wu. "Systemic deficiency of GM1 ganglioside in Parkinson’s disease tissues and its relation to the disease etiology." Glycoconjugate Journal 39, no. 1 (January 1, 2022): 75–82. http://dx.doi.org/10.1007/s10719-021-10025-9.
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AbstractFollowing our initial reports on subnormal levels of GM1 in the substantia nigra and occipital cortex of Parkinson’s disease (PD) patients, we have examined additional tissues from such patients and found these are also deficient in the ganglioside. These include innervated tissues intimately involved in PD pathology such as colon, heart and others, somewhat less intimately involved, such as skin and fibroblasts. Finally, we have analyzed GM1 in peripheral blood mononuclear cells, a type of tissue apparently with no direct innervation, and found those too to be deficient in GM1. Those patients were all afflicted with the sporadic form of PD (sPD), and we therefore conclude that systemic deficiency of GM1 is a characteristic of this major type of PD. Age is one factor in GM1 decline but is not sufficient; additional GM1 suppressive factors are involved in producing sPD. We discuss these and why GM1 replacement offers promise as a disease-altering therapy.
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Bech, E., J. Jakobsen, and T. F. Orntoft. "ELISA-type titertray assay of IgM anti-GM1 autoantibodies." Clinical Chemistry 40, no. 7 (July 1, 1994): 1331–34. http://dx.doi.org/10.1093/clinchem/40.7.1331.
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Abstract We report an ELISA-type titertray assay for autoantibodies against the ganglioside GM1. Trays were coated with ganglioside GM1 and reacted with patients' sera; bound IgM was detected with rabbit antibody to human IgM. High-titer serum from a patient was used as calibrator, another patient's serum as the positive control, and the GM1-specific cholera toxin as the control for GM1 coating. Regression curves of serum titers obtained from different patients were linear and parallel. Intra- and interassay CVs were 4.0-7.8% and 5.5-16%, respectively. We detected antibodies at a titer of 1:250 in normal subjects. Analytical specificity of the calibrator serum against GM1 was demonstrated by immune thin-layer chromatography. Anti-GM1 antibodies were increased in patients with chronic inflammatory demyelinating polyradiculoneuropathy (P < 0.002) or multiple sclerosis (P < 0.01). In Guillain-Barré syndrome, preliminary longitudinal studies showed a decrease in anti-GM1 titer that was related to clinical recovery.
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Dasgupta, Raktim, Markus S. Miettinen, Nico Fricke, Reinhard Lipowsky, and Rumiana Dimova. "The glycolipid GM1 reshapes asymmetric biomembranes and giant vesicles by curvature generation." Proceedings of the National Academy of Sciences 115, no. 22 (May 14, 2018): 5756–61. http://dx.doi.org/10.1073/pnas.1722320115.
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The ganglioside GM1 is present in neuronal membranes at elevated concentrations with an asymmetric spatial distribution. It is known to generate curvature and can be expected to strongly influence the neuron morphology. To elucidate these effects, we prepared giant vesicles with GM1 predominantly present in one leaflet of the membrane, mimicking the asymmetric GM1 distribution in neuronal membranes. Based on pulling inward and outward tubes, we developed a technique that allowed the direct measurement of the membrane spontaneous curvature. Using vesicle electroporation and fluorescence intensity analysis, we were able to quantify the GM1 asymmetry across the membrane and to subsequently estimate the local curvature generated by the molecule in the bilayer. Molecular-dynamics simulations confirm the experimentally determined dependence of the membrane spontaneous curvature as a function of GM1 asymmetry. GM1 plays a crucial role in connection with receptor proteins. Our results on curvature generation of GM1 point to an additional important role of this ganglioside, namely in shaping neuronal membranes.
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Sofer, A., G. Schwarzmann, and A. H. Futerman. "The internalization of a short acyl chain analogue of ganglioside GM1 in polarized neurons." Journal of Cell Science 109, no. 8 (August 1, 1996): 2111–19. http://dx.doi.org/10.1242/jcs.109.8.2111.
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In order to study the endocytosis of membrane lipids during the development of neuronal polarity, we examined the internalization of a short acyl chain fluorescent derivative of ganglioside GM1, N-(6-(4-nitrobenz-2-oxa-1,3-diazole-7-yl)-aminohexanoyl)-GM1 (C6-NBD-GM1), in hippocampal neurons cultured at low density. C6-NBD-GM1 was internalized by temperature- and energy-dependent mechanisms, and after short times of incubation, accumulated in endosomes in the axon, cell body and dendrites of neurons maintained for up to 4–5 days in culture. C6-NBD-GM1 was subsequently transported in a retrograde direction to a pool of recycling endosomes in the cell body, with little transport to lysosomes, as indicated by the lack of degradation of C6-NBD-GM1 even after long times, and the re-appearance of intact C6-NBD-GM1 at the cell surface after recycling; similarly, little degradation of C6-NBD-GM1 was detected in N18TG-2 neuroblastoma cells. In hippocampal neurons maintained for longer than 6 days in culture, there was little internalization of C6-NBD-GM1 along the length of axons, but the amount of endocytosis from dendrites was similar to that observed in younger neurons. These results demonstrate that gangliosides turnover rapidly in dendritic membranes at all stages of neuronal development, whereas ganglioside turnover in axons is much less rapid, at least in mature, polarized neurons.
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Detzner, Johanna, Charlotte Püttmann, Gottfried Pohlentz, and Johannes Müthing. "Ingenious Action of Vibrio cholerae Neuraminidase Recruiting Additional GM1 Cholera Toxin Receptors for Primary Human Colon Epithelial Cells." Microorganisms 10, no. 6 (June 20, 2022): 1255. http://dx.doi.org/10.3390/microorganisms10061255.
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For five decades it has been known that the pentamer of B subunits (choleragenoid) of the cholera toxin (CT) of Vibrio cholerae binds with high preference to the ganglioside GM1 (II3Neu5Ac-Gg4Cer). However, the exact structures of CT-binding GM1 lipoforms of primary human colon epithelial cells (pHCoEpiCs) have not yet been described in detail. The same holds true for generating further GM1 receptor molecules from higher sialylated gangliosides with a GM1 core through the neuraminidase of V. cholerae. To avoid the artificial incorporation of exogenous gangliosides from animal serum harboring GM1 and higher sialylated ganglio-series gangliosides, pHCoEpiCs were cultured in serum-free medium. Thin-layer chromatography overlay binding assays using a choleragenoid combined with electrospray ionization mass spectrometry revealed GM1 lipoforms with sphingosine (d18:1) as the sole sphingoid base linked to C14:0, C16:0, C18:0 or C20:0 fatty acyl chains forming the ceramide (Cer) moieties of the main choleragenoid-binding GM1 species. Desialylation of GD1a (IV3Neu5Ac,II3Neu5Ac-Gg4Cer) and GT1b (IV3Neu5Ac,II3(Neu5Ac)2-Gg4Cer) of pHCoEpiCs by V. cholerae neuraminidase was observed. GD1a-derived GM1 species with stable sphingosine (d18:1) and saturated fatty acyl chains varying in chain length from C16:0 up to C22:0 could be identified, indicating the ingenious interplay between CT and the neuraminidase of V. cholerae recruiting additional GM1 receptors of pHCoEpiCs.
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Likun, Zhou, Dingzhi Huang, Rui Liu, Hongli Li, Tao Ning, Le Zhang, Shaohua Ge, et al. "Survival and safety of monosialotetrahexosylganglioside in GI cancer patients with oxaliplatin-induced peripheral neurotoxicity-result from TJMUCH-GI-001 trial." Journal of Clinical Oncology 37, no. 15_suppl (May 20, 2019): 11596. http://dx.doi.org/10.1200/jco.2019.37.15_suppl.11596.
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11596 Background: TJMUCH-GI-001 Trial was a randomized, double-blind, placebo-controlled phase III trial to study the efficacy of Monosialotetrahexosylganglioside (GM1) for oxaliplatin-induced peripheral neurotoxicity (OIPN) in GI cancer patients. Majority patients (> 80%) in both arms continued receiving oxaliplatin on the trial. The results showed GM1 effectively reduced OIPN in GI cancer patients. Here we report the survival and safety results of this trial. Methods: Patients were randomized in a 1:1 ratio to receive GM1 or placebo. Patients with OIPN > = G2 by CTCAE 4.03 persisting during or after oxaliplatin-based chemotherapy were eligible. The patients who remained on oxaliplatin after enrollment, received concurrent placebo or GM1 x 7 days with each chemotherapy cycle. The patients who stopped taking oxaliplatin, were treated with placebo or GM1 x 14 days every 3 weeks. GM1 was dosed at 60mg daily for every 3-week or 40mg daily for every 2-week schedule. Trial was continued until modified EORTC QLQ-CIPN20 ( MCIPN) increased by 30% or stayed unchanged after two more treatments beyond completion of oxaliplatin. Survival data for the treatment arms were compared using a log-rank test and Chi-square tests were used for safety analysis. Results: From May 2015 to Dec 2017, 73 patients were enrolled in GM1 and 72 in placebo arm. The median follow-up was 16.6 months (0.8-43.1 months) as of Dec.2018. Four patients lost to follow up. There was no deleterious impact of GM1 on survival. As a matter of fact, receiving GM1 was associated with a trend toward improved PFS and OS (HR=0.74,95%CI, 0.469 - 1.156 for PFS and HR=0.76, 95%CI0.469 - 1.156 for OS). The most frequent Grade 3 or 4 adverse events included neutropenia (8 patients in GM1 group VS. 4 in placebo group) and hypoleukemia (4 patients in GM1 group VS. 1 in placebo group). Other 3 or 4 adverse events (all less than 3 patients) included anorexia, hypercalcemia, nausea, vomiting, proteinuria, hyperbilirubinemia, hypokalemia, hypertension and appendicitis. All the 3 or 4 adverse events were related to chemotherapy, not to GM1. Conclusion: In this placebo-controlled phase III trial, GM1 showed acceptable toxicity with trends favorable PFS and OS in GI cancer patients. Clinical trial information: NCT02486198.
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Taube, Stefan, Jeffrey W. Perry, Kristen Yetming, Sagar P. Patel, Heather Auble, Liming Shu, Hesham F. Nawar, et al. "Ganglioside-Linked Terminal Sialic Acid Moieties on Murine Macrophages Function as Attachment Receptors for Murine Noroviruses." Journal of Virology 83, no. 9 (February 25, 2009): 4092–101. http://dx.doi.org/10.1128/jvi.02245-08.
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ABSTRACT Noroviruses are the major cause of nonbacterial gastroenteritis in humans. However, little is known regarding the norovirus life cycle, including cell binding and entry. In contrast to human noroviruses, the recently discovered murine norovirus 1 (MNV-1) readily infects murine macrophages and dendritic cells in culture. Many viruses, including the related feline calicivirus, use terminal sialic acids (SA) as receptors for infection. Therefore, we tested whether SA moieties play a role during MNV-1 infection of murine macrophages. Competition with SA-binding lectins and neuraminidase treatment led to a reduction in MNV-1 binding and infection in cultured and primary murine macrophages, suggesting a role for SA during the initial steps of the MNV-1 life cycle. Because SA moieties can be attached to glycolipids (i.e., gangliosides), we next determined whether MNV-1 uses gangliosides during infection. The gangliosides GD1a, GM1, and asialo-GM1 (GA1) are natural components of murine macrophages. MNV-1 bound to ganglioside GD1a, which is characterized by an SA on the terminal galactose, but not to GM1 or asialo-GM1 in an enzyme-linked immunosorbent assay. The depletion of gangliosides using an inhibitor of glycosylceramide synthase (d-threo-P4) led to a reduction of MNV-1 binding and infection in cultured and primary murine macrophages. This defect was specifically rescued by the addition of GD1a. A similar phenotype was observed for MNV field strains WU11 (GV/WU11/2005/USA) and S99 (GV/Berlin/2006/DE). In conclusion, our data indicate that MNV can use terminal SA on gangliosides as attachment receptors during binding to murine macrophages.
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Sugimoto, Mamoru, Toshio Horisaki, and Tomoya Ogawa. "Stereoselective synthesis of asialo-GM1- and asialo-GM2-ganglioside." Glycoconjugate Journal 2, no. 1 (March 1985): 11–15. http://dx.doi.org/10.1007/bf01225109.
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Campanero-Rhodes, Maria A., Alicia Smith, Wengang Chai, Sandro Sonnino, Laura Mauri, Robert A. Childs, Yibing Zhang, et al. "N-Glycolyl GM1 Ganglioside as a Receptor for Simian Virus 40." Journal of Virology 81, no. 23 (September 12, 2007): 12846–58. http://dx.doi.org/10.1128/jvi.01311-07.
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ABSTRACT Carbohydrate microarrays have emerged as powerful tools in analyses of microbe-host interactions. Using a microarray with 190 sequence-defined oligosaccharides in the form of natural glycolipids and neoglycolipids representative of diverse mammalian glycans, we examined interactions of simian virus 40 (SV40) with potential carbohydrate receptors. While the results confirmed the high specificity of SV40 for the ganglioside GM1, they also revealed that N-glycolyl GM1 ganglioside [GM1(Gc)], which is characteristic of simian species and many other nonhuman mammals, is a better ligand than the N-acetyl analog [GM1(Ac)] found in mammals, including humans. After supplementing glycolipid-deficient GM95 cells with GM1(Ac) and GM1(Gc) gangliosides and the corresponding neoglycolipids with phosphatidylethanolamine lipid groups, it was found that GM1(Gc) analogs conferred better virus binding and infectivity. Moreover, we visualized the interaction of NeuGc with VP1 protein of SV40 by molecular modeling and identified a conformation for GM1(Gc) ganglioside in complex with the virus VP1 pentamer that is compatible with its presentation as a membrane receptor. Our results open the way not only to detailed studies of SV40 infection in relation to receptor expression in host cells but also to the monitoring of changes that may occur with time in receptor usage by the virus.
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Dong, Lingli, Shaoxian Hu, Fang Chen, Xiaomei Lei, Wei Tu, Yikai Yu, Liu Yang, et al. "Increased Expression of Ganglioside GM1 in Peripheral CD4+ T Cells Correlates Soluble Form of CD30 in Systemic Lupus Erythematosus Patients." Journal of Biomedicine and Biotechnology 2010 (2010): 1–8. http://dx.doi.org/10.1155/2010/569053.
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Gangliosides GM1 is a good marker of membrane microdomains (lipid rafts) with important function in cellular activation processes. In this study we found that GM1 expression on CD4+ T cells and memory T cells (CD45RO/CD4) were dramatic increased after stimulation with phytohaemagglutinin in vitro. Next, we examined the GM1 expression on peripheral blood CD4+ T cells and CD8+ T cells from 44 patients with SLE and 28 healthy controls by flow cytometry. GM1 expression was further analyzed with serum soluble CD30 (sCD30), IL-10, TNF-alpha and clinical parameters. The mean fluorescence intensity of GM1 on CD4+ T cells from patients with SLE was significantly higher than those from healthy controls, but not on CD8+ T cells. Increased expression of GM1 was more marked on CD4+/CD45RO+ memory T cells from active SLE patients. Patients with SLE showed significantly elevated serum sCD30 and IL-10, but not TNF-alpha levels. In addition, we found that enhanced GM1 expression on CD4+ T cells from patients with SLE positively correlated with high serum levels of sCD30 and IgG as well as disease activity (SLEDAI scores). Our data suggested the potential role of aberrant lipid raft/GM1 on CD4+ T cells and sCD30 in the pathogenesis of SLE.
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Hertz, Ellen, Marcus Saarinen, and Per Svenningsson. "GM1 Is Cytoprotective in GPR37-Expressing Cells and Downregulates Signaling." International Journal of Molecular Sciences 22, no. 23 (November 27, 2021): 12859. http://dx.doi.org/10.3390/ijms222312859.
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G-protein-coupled receptors (GPCRs) are commonly pharmacologically modulated due to their ability to translate extracellular events to intracellular changes. Previously, studies have mostly focused on protein–protein interactions, but the focus has now expanded also to protein–lipid connections. GM1, a brain-expressed ganglioside known for neuroprotective effects, and GPR37, an orphan GPCR often reported as a potential drug target for diseases in the central nervous system, have been shown to form a complex. In this study, we looked into the functional effects. Endogenous GM1 was downregulated when stably overexpressing GPR37 in N2a cells (N2aGPR37-eGFP). However, exogenous GM1 specifically rescued N2aGPR37-eGFP from toxicity induced by the neurotoxin MPP+. The treatment did not alter transcription levels of GPR37 or the enzyme responsible for GM1 production, both potential mechanisms for the effect. However, GM1 treatment inhibited cAMP-dependent signaling from GPR37, here reported as potentially consecutively active, possibly contributing to the protective effects. We propose an interplay between GPR37 and GM1 as one of the many cytoprotective effects reported for GM1.
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Valentino, P., A. Labate, R. Nisticò, D. Pirritano, A. Cerasa, M. Liguori, L. Bastone, L. Crescibene, and A. Quattrone. "Anti-GM1 antibodies are not associated with cerebral atrophy in patients with multiple sclerosis." Multiple Sclerosis Journal 15, no. 1 (January 2009): 114–15. http://dx.doi.org/10.1177/1352458508096685.
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Objectives The aim of this study was to correlate the brain atrophy with serum levels of anti-GM1 antibodies in patients with relapsing–remitting multiple sclerosis (RRMS). Methods Plasma sample from 52 patients with RRMS and 65 healthy controls were examined for anti-GM1 antibodies. Patients with RRMS underwent to MRI study with automated method called SIENAX that calculated an estimate of gray matter (GMV) and white matter (WMV) volumes. Results The percentage of RRMS patients with increased anti-GM1 was 37.8%. Elevated levels of anti-GM1 antibodies did not correlate with brain atrophy. Conclusions Anti-GM1 antibodies do not represent a marker of axonal damage in patients with RRMS.
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Ledeen, Robert W., and Gusheng Wu. "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." Canadian Journal of Physiology and Pharmacology 84, no. 3-4 (March 2006): 393–402. http://dx.doi.org/10.1139/y05-133.
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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 Ca2+ flux across both membranes, but by quite different mechanisms. GM1 in the NE contributes to regulation of nuclear Ca2+ through potentiation of a Na+/Ca2+ exchanger in the inner nuclear membrane, whereas in the cell membrane, it regulates cytosolic Ca2+ through modulation of a nonvoltage-gated Ca2+ 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+/Ca2+ exchanger with GM1, in contrast to Na+/Ca2+ 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 Ca2+ dysregulation as seen in their high vulnerability to Ca2+-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 Ca2+ 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+/Ca2+ exchange activity in the nucleus. The Na+/Ca2+ exchanger of the NE, in association with nuclear GM1, is thus seen contributing to independent regulation of Ca2+ by the nucleus in a manner that provides cytoprotection against Ca2+-induced apoptosis.
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Bianco, I. D., G. D. Fidelio, and B. Maggio. "Modulation of phospholipase A2 activity by neutral and anionic glycosphingolipids in monolayers." Biochemical Journal 258, no. 1 (February 15, 1989): 95–99. http://dx.doi.org/10.1042/bj2580095.
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The effect of neutral (galactocerebroside and asialo-ganglioside GM1) or anionic (sulphatide and gangliosides GM1, GD1a and GT1b) glycosphingolipids on the activity of phospholipase A2 from pig pancreas was studied in mixed monolayers of dilauroyl phosphatidylcholine with the glycosphingolipids in different molar fractions at various constant surface pressures. The activity of the enzyme depends on the proportion and type of glycosphingolipid in the interface. Sulphatide activates the enzyme at all proportions, whereas galactocerebroside shows inhibition or activation depending on its proportion in the film. Asialo-ganglioside GM1 and gangliosides GM1, GD1a and GT1b can strongly inhibit the enzyme at relatively low molar fractions in the film in the following order: asialo-ganglioside GM1 less than ganglioside GM1 less than ganglioside GT1b less than ganglioside GD1a. The changes of activity are not due to a direct action of the lipids on the active centre or interfacial recognition region of the enzyme.
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Marcus, D. M., L. Perry, S. Gilbert, J. L. Preud'homme, and R. Kyle. "Human IgM monoclonal proteins that bind 3-fucosyllactosamine, asialo-GM1, and GM1." Journal of Immunology 143, no. 9 (November 1, 1989): 2929–32. http://dx.doi.org/10.4049/jimmunol.143.9.2929.
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Abstract Analysis of monoclonal human Ig that occur in association with lymphoproliferative diseases has provided valuable information about antibody structure and idiotypes. We analyzed 940 human sera that contained monoclonal IgM proteins for their ability to bind to four carbohydrate epitopes. Ten sera bound asialo-GM1, five of these sera also bound GM1, 10 bound to 3-fucosyllactosamine (3-FL), and one each bound to levan and galactan. Although the antibody activity in each serum was associated with a single L chain isotype, both kappa and lambda isotypes were represented among the proteins that bound to asialo-GM1 and to 3-FL. Some antibodies against asialo-GM1 were highly specific for this compound, whereas others cross-reacted with the structurally related gangliosides GM1 and GD1b. The antibodies to asialo-GM1 also varied considerably in their ability to lyse liposomes that contain asialo GM1. An association of IgM mAb against gangliosides with peripheral neuropathies has been reported recently, but only one of five patients whose antibodies reacted with GM1 ganglioside had a neuropathy. The antibodies that bound 3-FL exhibited narrower specificity, and less than 10% cross reactivity was noted with structurally related carbohydrates. The frequency of monoclonal proteins that bound 3-FL and asialo-GM1, approximately 1:100 sera for each specificity, was surprisingly high in view of the fact that both of these epitopes are expressed in human tissues. We suggest that these antibodies may be poly-specific and/or that the subset of B lymphocytes that synthesizes these anti-carbohydrate antibodies undergoes malignant transformation more frequently than other B lymphocytes.
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Weesner, Jason Andrew, Ida Annunziata, Tianhong Yang, Walter Acosta, Elida Gomero, Huimin Hu, Diantha van de Vlekkert, et al. "Preclinical Enzyme Replacement Therapy with a Recombinant β-Galactosidase-Lectin Fusion for CNS Delivery and Treatment of GM1-Gangliosidosis." Cells 11, no. 16 (August 19, 2022): 2579. http://dx.doi.org/10.3390/cells11162579.
Full textAbstract:
GM1-gangliosidosis is a catastrophic, neurodegenerative lysosomal storage disease caused by a deficiency of lysosomal β-galactosidase (β-Gal). The primary substrate of the enzyme is GM1-ganglioside (GM1), a sialylated glycosphingolipid abundant in nervous tissue. Patients with GM1-gangliosidosis present with massive and progressive accumulation of GM1 in the central nervous system (CNS), which leads to mental and motor decline, progressive neurodegeneration, and early death. No therapy is currently available for this lysosomal storage disease. Here, we describe a proof-of-concept preclinical study toward the development of enzyme replacement therapy (ERT) for GM1-gangliosidosis using a recombinant murine β-Gal fused to the plant lectin subunit B of ricin (mβ-Gal:RTB). We show that long-term, bi-weekly systemic injection of mβ-Gal:RTB in the β-Gal−/− mouse model resulted in widespread internalization of the enzyme by cells of visceral organs, with consequent restoration of enzyme activity. Most importantly, β-Gal activity was detected in several brain regions. This was accompanied by a reduction of accumulated GM1, reversal of neuroinflammation, and decrease in the apoptotic marker caspase 3. These results indicate that the RTB lectin delivery module enhances both the CNS-biodistribution pattern and the therapeutic efficacy of the β-Gal ERT, with the potential to translate to a clinical setting for the treatment of GM1-gangliosidosis.
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Zhong, Liyun, Zhun Zhang, Xiaoxu Lu, Shengde Liu, Crystal Y. Chen, and Zheng W. Chen. "NSOM/QD-Based Visualization of GM1 Serving as Platforms for TCR/CD3 Mediated T-Cell Activation." BioMed Research International 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/276498.
Full textAbstract:
Direct molecular imaging of nanoscale relationship between T-cell receptor complexes (TCR/CD3) and gangliosidosis GM1 before and after T-cell activation has not been reported. In this study, we made use of our expertise of near-field scanning optical microscopy(NSOM)/immune-labeling quantum dots- (QD-)based dual-color imaging system to visualize nanoscale profiles for distribution and organization of TCR/CD3, GM1, as well as their nanospatial relationship and their correlation with PKCθsignaling cascade during T-cell activation. Interestingly, after anti-CD3/anti-CD28 Ab co-stimulation, both TCR/CD3 and GM1 were clustered to form nanodomains; moreover, all of TCR/CD3 nanodomains were colocalized with GM1 nanodomains, indicating that the formation of GM1 nanodomains was greatly correlated with TCR/CD3 mediated signaling. Specially, while T-cells were pretreated with PKCθsignaling inhibitor rottlerin to suppress IL-2 cytokine production, no visible TCR/CD3 nanodomains appeared while a lot of GM1 nanodomains were still observed. However, while T-cells are pretreated with PKCαβsignaling inhibitor GÖ6976 to suppress calcium-dependent manner, all of TCR/CD3 nanodomains were still colocalized with GM1 nanodomains. These findings possibly support the notion that the formation of GM1 nanodomains indeed serves as platforms for the recruitment of TCR/CD3 nanodomains, and TCR/CD3 nanodomains are required for PKCθsignaling cascades and T-cell activation
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Di Biase, Erika, Giulia Lunghi, Margherita Maggioni, Maria Fazzari, Diego Yuri Pomè, Nicoletta Loberto, Maria Grazia Ciampa, et al. "GM1 Oligosaccharide Crosses the Human Blood–Brain Barrier In Vitro by a Paracellular Route." International Journal of Molecular Sciences 21, no. 8 (April 19, 2020): 2858. http://dx.doi.org/10.3390/ijms21082858.
Full textAbstract:
Ganglioside GM1 (GM1) has been reported to functionally recover degenerated nervous system in vitro and in vivo, but the possibility to translate GM1′s potential in clinical settings is counteracted by its low ability to overcome the blood–brain barrier (BBB) due to its amphiphilic nature. Interestingly, the soluble and hydrophilic GM1-oligosaccharide (OligoGM1) is able to punctually replace GM1 neurotrophic functions alone, both in vitro and in vivo. In order to take advantage of OligoGM1 properties, which overcome GM1′s pharmacological limitations, here we characterize the OligoGM1 brain transport by using a human in vitro BBB model. OligoGM1 showed a 20-fold higher crossing rate than GM1 and time–concentration-dependent transport. Additionally, OligoGM1 crossed the barrier at 4 °C and in inverse transport experiments, allowing consideration of the passive paracellular route. This was confirmed by the exclusion of a direct interaction with the active ATP-binding cassette (ABC) transporters using the “pump out” system. Finally, after barrier crossing, OligoGM1 remained intact and able to induce Neuro2a cell neuritogenesis by activating the TrkA pathway. Importantly, these in vitro data demonstrated that OligoGM1, lacking the hydrophobic ceramide, can advantageously cross the BBB in comparison with GM1, while maintaining its neuroproperties. This study has improved the knowledge about OligoGM1′s pharmacological potential, offering a tangible therapeutic strategy.
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Wolf, Anne A., Michael G. Jobling, David E. Saslowsky, Eli Kern, Kimberly R. Drake, Anne K. Kenworthy, Randall K. Holmes, and Wayne I. Lencer. "Attenuated Endocytosis and Toxicity of a Mutant Cholera Toxin with Decreased Ability To Cluster Ganglioside GM1 Molecules." Infection and Immunity 76, no. 4 (January 22, 2008): 1476–84. http://dx.doi.org/10.1128/iai.01286-07.
Full textAbstract:
ABSTRACT Cholera toxin (CT) moves from the plasma membrane (PM) of host cells to the endoplasmic reticulum (ER) by binding to the lipid raft ganglioside GM1. The homopentomeric B-subunit of the toxin can bind up to five GM1 molecules at once. Here, we examined the role of polyvalent binding of GM1 in CT action by producing chimeric CTs that had B-subunits with only one or two normal binding pockets for GM1. The chimeric toxins had attenuated affinity for binding to host cell PM, as expected. Nevertheless, like wild-type (wt) CT, the CT chimeras induced toxicity, fractionated with detergent-resistant membranes extracted from toxin-treated cells, displayed restricted diffusion in the plane of the PM in intact cells, and remained bound to GM1 when they were immunoprecipitated. Thus, binding normally to two or perhaps only one GM1 molecule is sufficient for association with lipid rafts in the PM and toxin action. The chimeric toxins, however, were much less potent than wt toxin, and they entered the cell by endocytosis more slowly, suggesting that clustering of GM1 molecules by the B-subunit enhances the efficiency of toxin uptake and perhaps also trafficking to the ER.
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Fujita, Akikazu, Jinglei Cheng, Minako Hirakawa, Koichi Furukawa, Susumu Kusunoki, and Toyoshi Fujimoto. "Gangliosides GM1 and GM3 in the Living Cell Membrane Form Clusters Susceptible to Cholesterol Depletion and Chilling." Molecular Biology of the Cell 18, no. 6 (June 2007): 2112–22. http://dx.doi.org/10.1091/mbc.e07-01-0071.
Full textAbstract:
Presence of microdomains has been postulated in the cell membrane, but two-dimensional distribution of lipid molecules has been difficult to determine in the submicrometer scale. In the present paper, we examined the distribution of gangliosides GM1 and GM3, putative raft molecules in the cell membrane, by immunoelectron microscopy using quick-frozen and freeze-fractured specimens. This method physically immobilized molecules in situ and thus minimized the possibility of artifactual perturbation. By point pattern analysis of immunogold labeling, GM1 was shown to make clusters of <100 nm in diameter in normal mouse fibroblasts. GM1-null fibroblasts were not labeled, but developed a similar clustered pattern when GM1 was administered. On cholesterol depletion or chilling, the clustering of both endogenous and exogenously-loaded GM1 decreased significantly, but the distribution showed marked regional heterogeneity in the cells. GM3 also showed cholesterol-dependent clustering, and although clusters of GM1 and GM3 were found to occasionally coincide, these aggregates were separated in most cases, suggesting the presence of heterogeneous microdomains. The present method enabled to capture the molecular distribution of lipids in the cell membrane, and demonstrated that GM1 and GM3 form clusters that are susceptible to cholesterol depletion and chilling.
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Masserini, M., P. Palestini, M. Pitto, V. Chigorno, M. Tomasi, and G. Tettamanti. "Cyclic AMP accumulation in HeLa cells induced by cholera toxin. Involvement of the ceramide moiety of GM1 ganglioside." Biochemical Journal 271, no. 1 (October 1, 1990): 107–11. http://dx.doi.org/10.1042/bj2710107.
Full textAbstract:
The influence of ceramide composition on the rate of GM1 association to HeLa cells has been investigated by incubating the cells in the presence of either native ganglioside or molecular species carrying highly homogeneous long chain base moieties, fractionated from native GM1. The GM1 ganglioside species carrying the unsaturated C18 long chain base moiety proved to have the fastest rate of association, whereas the saturated species carrying 20 carbon atoms had the slowest rate. After having increased the GM1 cell content (65-fold) by incubation with the various ganglioside species, the cells were incubated with cholera toxin and the time course of cyclic AMP accumulation was monitored. Remarkable differences among cells enriched with the various molecular species were found in the duration of the lag time preceding the accumulation of cyclic AMP, the shortest being displayed by the unsaturated C18 species. Moreover, the amount of cyclic AMP accumulated after a given time of incubation with cholera toxin was significantly higher when the C18:1-GM1 species was present than with native GM1. Fluorescence anisotropy experiments, carried out using the probe 1,3-diphenylhexatriene, show that the GM1 ganglioside ceramide moiety was also modifying the cell membrane fluidity of the host.
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Ji, Li, Zhonghui Qiao, Xin Zhang, Xiaolei Cheng, Weiyang Wang, Fan Zhang, Yifa Zhou, and Ye Yuan. "Preparation of Ganglioside GM1 by Supercritical CO2 Extraction and Immobilized Sialidase." Molecules 24, no. 20 (October 16, 2019): 3732. http://dx.doi.org/10.3390/molecules24203732.
Full textAbstract:
Monosialotetrahexosylganglioside (GM1) has good activity on brain diseases and was developed to be a drug applied in clinics for neurological disorders and nerve injury. It is difficult to isolate GM1 in industry scale from the brains directly. In this work, a simple and highly efficient method with high yield was developed for the isolation, conversion, and purification of GM1 from a pig brain. Gangliosides (GLS) were first extracted by supercritical CO2 (SCE). The optimum extraction time of GLS by SCE was 4 h, and the ratio of entrainer to acetone powder from the pig brain was 3:1 (v/w). GM1 was then prepared from GLS by immobilized sialidase and purified by reverse-phase silica gel. Sodium alginate embedding was used for the immobilization of sialidase. Under the optimized method, the yield of high-purity GM1 was around 0.056%. This method has the potential to be applied in the production of GM1 in the industry.
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Karupiah, G., R. V. Blanden, and I. A. Ramshaw. "Interferon gamma is involved in the recovery of athymic nude mice from recombinant vaccinia virus/interleukin 2 infection." Journal of Experimental Medicine 172, no. 5 (November 1, 1990): 1495–503. http://dx.doi.org/10.1084/jem.172.5.1495.
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Athymic nude mice recover from an infection with recombinant vaccinia virus (VV) encoding murine interleukin 2 (IL-2), but treatment with a mAb to IL-2 accentuated infection. Administration of a mAb against interferon gamma (IFN-gamma) to mice infected with the IL-2-encoding virus completely prevented the IL-2-induced mechanisms of recovery. Both asialo-GM1+ (NK) and asialo-GM1- (non-NK) cells were participants in the IFN-gamma-mediated recovery of nude mice from infection with the IL-2-encoding VV recombinant. Depletion of asialo-GM1+ cells exacerbated infection, though not as much as anti-IFN-gamma mAb. In vitro, both asialo-GM1+ and asialo-GM1- nude mouse splenocytes produced IFN-gamma in response to IL-2.
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Mitsumori, Rie, Tomohisa Kato, and Kenichi Hatanaka. "γ-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens: Hydrolysis of Gangliosides." International Journal of Carbohydrate Chemistry 2009 (February 2, 2009): 1–4. http://dx.doi.org/10.1155/2009/398284.
Full textAbstract:
Sialidase is a ubiquitous enzyme that catalyzes the hydrolytic removal of terminal sialic acid residues from oligosaccharides in glycolipids and glycoproteins. Ganglioside GM1 has been usually found to be resistant to various sialidases. Arthrobacter ureafaciens sialidase has been reported to remove sialyl residues of ganglioside GM1 in the presence of bile salts. However, bile salts are difficult to be removed, and disturb HPTLC analysis. Using γ-cyclodextrin (γ-CD) as a novel additive agent, ganglioside GM1 was efficiently hydrolyzed to asialo-GM1 by A. ureafaciens sialidase.