Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “GANGLIOSIDES”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 973 records · Page 54Linked to original sources
PubMed1996

Gangliosides are neuronal ligands for myelin-associated glycoprotein.

Nerve cells depend on specific interactions with glial cells for proper function. Myelinating glial cells are thought to associate with neuronal axons, in part, via the cell-surface adhesion protein, myelin-associated glycoprotein (MAG). MAG is also thought to be a major inhibitor of neurite outgrowth (axon regeneration) in the adult central nervous system. Primary structure and in vitro function place MAG in an immunoglobulin-related family of sialic acid-binding lactins. We report that a limited set of structurally related gangliosides, known to be expressed on myelinated neurons in vivo, are ligands for MAG. When major brain gangliosides were adsorbed as artificial membranes on plastic microwells, only GT1b and GD1a supported cell adhesion of MAG-transfected COS-1 cells. Furthermore, a quantitatively minor ganglioside expressed on cholinergic neurons, GQ1b alpha (also known as Chol-1 alpha-b), was much more potent than GT1b or GD1a in supporting MAG-mediated cell adhesion. Adhesion to either GT1b or GQ1b alpha was abolished by pretreatment of the adsorbed gangliosides with neuraminidase. On the basis of structure-function studies of 19 test glycosphingolipids, an alpha 2,3-N-acetylneuraminic acid residue on the terminal galactose of a gangliotetraose core is necessary for MAG binding, and additional sialic acid residues linked to the other neutral core saccharides [Gal(II) and GalNAc(III)] contribute significantly to binding affinity. MAG-mediated adhesion to gangliosides was blocked by pretreatment of the MAG-transfected COS-1 cells with anti-MAG monoclonal antibody 513, which is known to inhibit oligodendrocyte-neuron binding. These data are consistent with the conclusion that MAG-mediated cell-cell interactions involve MAG-ganglioside recognition and binding.

Animals↗
PubMed1997

Inhibition of endogenous ganglioside synthesis does not block neurite formation by retinoic acid-treated neuroblastoma cells.

Gangliosides are believed to play a critical role in cellular differentiation. To test this concept, we determined the effect of inhibition of endogenous ganglioside synthesis upon neurite formation induced by retinoic acid in LAN-5 human neuroblastoma cells. Ganglioside synthesis and content of LAN-5 cells exposed for 6 days to 10 microM D-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol (D-PDMP) (an inhibitor of glucosylceramide synthase) were reduced by >90%. However, these ganglioside-depleted cells were not blocked from forming neurites when exposed to 10 microM retinoic acid. Even more extensive treatment of LAN-5 cells with 20 microM D-PDMP (6 day pretreatment followed by 6 days together with 10 microM retinoic acid) still did not block the retinoic acid-induced neurite formation. An element of neuroblastoma tumor cell differentiation, neurite formation, is therefore dependent neither on an intact cellular ganglioside complement nor on new ganglioside synthesis.

Down-Regulation↗
PubMed2002

Effect of gangliosides on the distribution of a glycosylphosphatidylinositol-anchored protein in plasma membrane from Chinese hamster ovary-K1 cells.

Glycosylphosphatidylinositol (GPI)-anchored proteins are clustered mainly in sphingolipid-cholesterol microdomains of the plasma membrane. The distribution of GPI-anchored fusion yellow fluorescent protein (GPI-YFP) in the plasma membrane of Chinese hamster ovary (CHO)-K1 cells with different glycolipid compositions was investigated. Cells depleted of glycosphingolipids by inhibiting glucosylceramide synthase activity or cell lines expressing different gangliosides caused by stable transfection of appropriate ganglioside glycosyltransferases or exposed to exogenous GM1 were transfected with GPI-YFP cDNA. The distribution of GPI-YFP fusion protein expressed at the plasma membrane was studied using the membrane-impermeable cross-linking agent bis(sulfosuccinimidyl)suberate. Results indicate that GPI-YFP forms clusters at the surface of cells expressing GM3, or cells depleted of glycolipids, or transfected cells expressing mainly GD3 and GT3, or GM1 and GD1a, or mostly GM2, or highly expressing GM1. However, no significant changes in membrane microdomains of GPI-YFP were detected in the different glycolipid environments provided by the membranes of the cell lines under study. On the other hand, wild type CHO-K1 cells exposed to 100 microm GM1 before cross-linking with bis(sulfosuccinimidyl)suberate showed a dramatic reduction in the amount of GPI-YFP clusters. These findings clearly indicate that manipulating the glycolipid content of the cellular membrane, just by changing the ganglioside biosynthetic activity of the cell, did not significantly affect the association of GPI-YFP on the cell surface of CHO-K1 cells. The effect of exogenous GM1 gangliosides on GPI-YFP plasma membrane distribution might be a consequence of the ganglioside level reached in plasma membrane and/or the effect of particular ganglioside species (micelles) that lead to membrane architecture and/or dynamic modifications.

Animals↗
PubMed2002

Botulinum neurotoxin A activity is dependent upon the presence of specific gangliosides in neuroblastoma cells expressing synaptotagmin I.

Botulinum neurotoxin A (BoNT/A) is the deadliest of all known biological substances. Although its toxicity makes BoNT/A a biological warfare threat, its biologic activity makes it an increasingly useful therapeutic agent for the treatment of muscular disorders. However, almost 200 years after its discovery, the neuronal cell components required for the activity of this deadly toxin have not been unequivocally identified. In this work, neuroblastoma cells expressing synaptotagmin I, a protein shown to be bound by BoNT/A, were used to determine whether specific gangliosides were necessary for BoNT/A activity as measured by synaptosomal-associated protein of 25 kDa (SNAP-25) cleavage. Ganglioside GT1b was found to support BoNT/A activity significantly more effectively than GD1a, which was far more effective than GM1 when added to ganglioside-deficient murine cholinergic Neuro 2a or to human adrenergic SK-N-SH neuroblastoma cells. Whereas both cell lines expressed synaptotagmin I, SNAP-25 cleavage was not observed in the absence of complex gangliosides. These results indicate that 1) gangliosides are required for BoNT/A activity, 2) synaptotagmin I in the absence of gangliosides does not support BoNT/A activity, and 3) Neuro 2a cells are an efficient model system for studying the biological activity of BoNT/A.

Animals↗
PubMed2004

Gangliosides act as co-receptors for Salmonella enteritidis FliC and promote FliC induction of human beta-defensin-2 expression in Caco-2 cells.

Antimicrobial peptides such as defensins are crucial for host defense at mucosal surfaces. We reported previously that Salmonella enteritidis flagellin (FliC) induced human beta-defensin-2 (hBD-2) mRNA expression in Caco-2 cells via NF-kappaB activation (Ogushi, K., Wada, A., Niidome, T., Mori, N., Oishi, K., Nagatake, T., Takahashi, A., Asakura, H., Makino, S., Hojo, H., Nakahara, Y., Ohsaki, M., Hatakeyama, T., Aoyagi, H., Kurazono, H., Moss, J., and Hirayama, T. (2001) J. Biol. Chem. 276, 30521-30526). In this study, we examined the role of ganglioside as co-receptors with Toll-like receptor 5 (TLR5) on FliC induction of hBD-2 expression in Caco-2 cells. Exogenous gangliosides suppressed FliC induction of hBD-2 promoter activity and binding of FliC to Caco-2 cells. Incorporation of exogenous ganglioside GD1a into Caco-2 cell membranes increased the effect of FliC on hBD-2 promoter activity. In support of a role for endogenous gangliosides, incubation of Caco-2 cells with dl-threo-2-hexadecanoylamino-3-morpholino-1-phenylpropanol, a glucosylceramide synthase inhibitor, reduced FliC induction of hBD-2 promoter activity. GD1a-loaded CHO-K1-expressing TLR5 cells had a higher potential for hBD-2 induction following FliC stimulation than GD1a-loaded CHO-K1 cells not expressing TLR5. FliC increased phosphorylation of mitogen-activated protein kinase, p38, and ERK1/2. Exogenous gangliosides GD1a, GD1b, and GT1b each suppressed FliC induction of p38 and ERK1/2 phosphorylation. Furthermore, FliC did not enhance luciferase activity in Caco-2 cells transfected with a plasmid containing a mutated activator protein 1-binding site. These results suggest that gangliosides act as co-receptors with TLR5 for FliC and promote hBD-2 expression via mitogen-activated protein kinase.

Animals↗
PubMed1986

Potential ganglioside antigens associated with human gliomas.

Gangliosides in human gliomas were investigated and found to have an altered composition and concentration as compared to normal grey and white matter of brain. The major gangliosides GM1, GD1a, and GT1b were markedly reduced in the tumour tissue and in contrast there was an increase of gangliosides GM3 and GD3, which often appeared as the dominating ones. Moreover, the tumours contained gangliosides, both mono- and oligosialylated, which could not be detected in the normal brain. The concentration of gangliosides, 0.7 +/- 0.4 mumol sialic acid/g, was significantly lower as compared to normal brain grey (p less than 0.001) and white matter (p less than 0.01), which contained 3.5 +/- 0.3 and 1.2 +/- 0.3 mumol sialic acid/g respectively. The tumour tissue concentration of phospholipids was 14 +/- 8 and of cholesterol 19 +/- 12 mumol/g. The appearance in glioma tissue of gangliosides that are not found in normal brain tissue suggests that these are tumour associated and might serve as surface antigens detectable by specific monoclonal antibodies.

Adult↗
PubMed1988

A role for gangliosides in astroglial cell differentiation in vitro.

Rat cerebral astroglial cells in culture display specific morphological and biochemical behaviors in response to exogenously added gangliosides. To examine a potential function for endogenous gangliosides in the processes of astroglial cell differentiation, we have used the B subunit of cholera toxin as a ganglioside-specific probe. The B subunit, which is multivalent and binds specifically to GM1 ganglioside on the cell surface, induced a classical star-shaped (stellate) morphology in the astroglial cells and inhibited DNA synthesis in a dose-dependent manner. The morphological response was massive and complete within 2 h, with an ED50 of 0.8 nM, and appeared to depend on the direct interaction of the B subunit with GM1 on the cell surface. A B subunit-evoked inhibition of DNA synthesis and cell division (ED50 = 0.2 nM) was observed when the cells were stimulated with defined mitogens, such as epidermal growth factor and basic fibroblast growth factor. Maximal inhibition approached 80% within 24 h. The effects of the B subunit were unrelated to increases in cAMP. These observations, taken together with previous studies, demonstrate that both endogenously occurring plasma membrane gangliosides and exogenously supplied gangliosides can influence the differentiative state (as judged by morphological and growth behaviors) of astroglial cells in vitro.

Animals↗
PubMed1993

Specific suppression of major histocompatibility complex class I and class II genes in astrocytes by brain-enriched gangliosides.

The effect of brain-enriched gangliosides on constitutive and cytokine-inducible expression of major histocompatibility complex (MHC) class I and II genes in cultured astrocytes was studied. Before treatment with gangliosides, astrocytes expressed constitutive MHC class I but not class II molecules, however, the expression of both MHC class I and II cell surface molecules on astrocytes was induced to high levels by interferon gamma (IFN-gamma). Constitutive and IFN-gamma-inducible expression of MHC class I and II molecules was suppressed by treatment of astrocytes with exogenous bovine brain gangliosides in a dose-dependent manner. Constitutive and induced MHC class I and II mRNA levels were also suppressed by gangliosides, indicating control through transcriptional mechanisms. This was consistent with the ability of gangliosides to suppress the binding activity of transcription factors, especially NF-kappa B-like binding activity, important for the expression of both MHC class I and II genes. These studies may be important for understanding mechanisms of central nervous system (CNS)-specific regulation of major histocompatibility molecules in neuroectodermal cells and the role of gangliosides in regulating MHC-restricted antiviral and autoimmune responses within the CNS.

Animals↗
PubMed1991

Ganglioside-binding proteins in skeletal and cardiac muscle.

Several ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues.

Animals↗
PubMed2000

A strain of human influenza A virus binds to extended but not short gangliosides as assayed by thin-layer chromatography overlay.

A human strain of influenza virus (A, H1N1) was shown to bind in an unexpected way to leukocyte and other gangliosides when compared with avian virus (A, H4N6) as assayed on TLC plates. The human strain bound only to species with about 10 or more sugars, while the avian strain bound to a wide range of gangliosides including the 5-sugar gangliosides. By use of specific lectins, antibodies, and FAB and MALDI-TOF mass spectrometry an attempt was done to preliminary identify the sequences of leukocyte gangliosides recognized by the human strain. The virus binding pattern did not follow binding by VIM-2 monoclonal antibody and was not identical with binding by anti-sialyl Lewis x antibody. There was no binding by the virus of linear NeuAcalpha3- or NeuAcalpha6-containing gangliosides with up to seven monosaccharides per mol of ceramide. Active species were minor NeuAcalpha6-containing molecules with probably repeated HexHexNAc units and fucose branches. This investigation demonstrates marked distinctions in the recognition of gangliosides between avian and human influenza viruses. Our data emphasize the importance of structural factors associated with more distant parts of the binding epitope and the complexity of carbohydrate recognition by human influenza viruses.

Carbohydrate Sequence↗
PubMed1994

Immunohistochemical localization of minor gangliosides in the rat central nervous system.

We previously described the differential distribution of major gangliosides (GM1, GD1a, GD1b, GT1b and GQ1b) in adult rat brain detected by specific antibodies (Kotani, M., Kawashima, I., Ozawa, I., Terashima, T. and Tai, T. Glycobiology, 3, 137-146, 1993). We report here the distribution of minor gangliosides in the adult rat brain by an immunofluorescence technique with mouse monoclonal antibodies (MAbs). Ten MAbs (GMR6, GMB28, GMR11, GMR19, GMR2, GMR7, GGR51, AMR10, NGR54 and NGR53) that specifically recognize GM3, GM2, GT1a, GD3, O-Acdisialoganglioside, GD2, GM1b, GM4, IV3NeuAc alpha-nLc4Cer and IV6NeuAc alpha-nLc4Cer, respectively, were used. Our study revealed that there is a cell type-specific expression of minor gangliosides, as well as major gangliosides, in the rat brain. In the cerebellar cortex, GM3 was expressed intensely in the white matter and slightly in the granular layer. GD3 was present in both the granular layer and the white matter, but not in the Purkinje cell layer or in the molecular layer. An O-Ac-disialoganglioside, which was suggested to be O-Ac-LD1, was detected exclusively in both the molecular layer and Purkinje cell layer. The presence of GD2 was restricted to the granular layer. GM4 was associated with some astrocytes, but not with myelin or oligodendrocytes. GM2, GT1a, GM1b, IV3NeuAc alpha-nLc4Cer and IV6NeuAc alpha-nLc4Cer gangliosides were not clearly detected in the cerebellar cortex. In other regions, such as cerebral cortex, hippocampal formation and spinal cord, the expression of the gangliosides was also highly localized to a specific cell type and layer.

Animals↗
PubMed1995

Expression of new KDN-gangliosides in rainbow trout testis during spermatogenesis and their structural identification.

The developmental expression of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid-containing glycosphingolipids (KDN-gangliosides) in rainbow trout testis during spermatogenesis was studied using a monoclonal antibody, mAb.kdn3G, which recognizes the KDN alpha 2-->3Gal beta 1-->epitope. A major KDN-ganglioside found in mature sperm, (KDN)GM3, KDN alpha 2-->3Gal beta 1-->4Glc beta 1-->Cer (where Cer is ceramide), was expressed in testis throughout all stages of its maturation. On the contrary, four new KDN-gangliosides which were reactive with mAb.kdn3G were not detected in mature sperm, although they were identified in immature testis and expressed during spermatogenesis. The structures of these KDN-gangliosides were established by chemical, enzymatic and immunochemical methods as: (i) (KDN)GD1a, KDN alpha 2-->3Gal beta 1-->3GalNAc beta 1-->4(KDN alpha 2-->3)Gal beta 1-->4Glc beta 1-->Cer; (ii) (KDN, Neu5Ac)GD1a, KDN alpha 2-->3Gal beta 1-->3GalNAc beta 1-->4(Neu5Ac alpha 2-->3)Gal beta 1-->4Glc beta 1-->Cer and Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc beta 1-->4(KDN alpha 2-->3)Gal beta 1-->4Glc beta 1-->Cer; (iii) (KDN) GD1 alpha, KDN alpha 2-->3Gal beta 1-->3(KDN alpha 2-->6)GalNAc beta 1-->4Gal beta 1-->4Glc beta 1-->Cer; and (iv) (KDN,Neu5Ac)GD1 alpha, KDN alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc beta 1-->4Gal beta 1-->4Glc beta 1-->Cer. (KDN)GD1a and (KDN,Neu5Ac)GD1a first appeared at an early stage of spermatogenesis, but (KDN)GD1 alpha and (KDN,Neu5Ac)GD1 alpha were not expressed until 2 months prior to spermiation. While (KDN)GM3 was previously shown to contain only 4-sphingenine (d18:1) acylated with a C16:0 fatty acid, the new KDN-gangliosides discovered in this study were composed of 4-hydroxysphinganine (t18:0) or 4-sphingenine (d18:1), and were acylated with a C24:1 or C16:0 fatty acid. A possible function of these KDN-gangliosides is suggested.

Acylation↗
PubMed1995

Detection in human blood platelets of sialyl Lewis X gangliosides, potential ligands for CD62 and other selectins.

Activated platelets are known to express P-selectin, a lectin-like adhesion receptor (CD62), through which they bind to sialyl Lewis X (sLex) ligands displayed on the membranes of leukocytes. To determine whether direct platelet-platelet interactions via P-selectin/sLex interactions are also possible, we have examined the ganglioside extract of human blood platelets for the presence of sLex ligands. Using the sensitive method of high-performance thin-layer chromatography (HPTLC)-immunostaining with the monoclonal antibody (mAb) CSLEX or with sialidase followed by mAbs MC480 or PM81, eight sLex bands were demonstrated at Rf 0.01, 0.03, 0.05, 0.06, 0.08, 0.10, 0.14 and 0.21 in the solvent 45:55:10 chloroform-methanol-aqueous 0.02% CaCl2. The sensitivity of all eight bands to sialidase or endoglycoceramidase confirmed that they were gangliosides. Comparison of the HPTLC mobilities and densities of platelet bands with those from five other human tissues (granulocytes, monoblasts, kidney, aortic endothelium and erythrocytes) in three different solvents revealed three major bands associated with platelets: 3 (Rf0.03), 6 (0.08) and 14 (0.21). Platelet bands were demonstrated not to have resulted from granulocyte contamination. Partial purification of platelet sLex gangliosides by high-performance liquid chromatography and their reaction with 14 oligosaccharide-specific mAbs (FH4, FH5, LM112-161, LM119-181, A5, 1B2, BR55-2, BE2, ES4, MC631, MH04, SH34, P001 and MC813-70) revealed that band 6 is a multifucosylated neolacto ganglioside and band 14 is a branched, disialo neolacto fucoganglioside. Platelet band 3 combined the features of both bands 6 and 14, and reacted differently than granulocyte band 3. These partial structures resemble gangliosides associated with adhesion in other cell systems. It is concluded that platelets express tissue-specific sLex gangliosides (sLex ligands). Thus, it is possible that platelet-platelet binding may be mediated at least partially through P-selectin/sLex interactions, especially after platelet activation.

Blood Platelets↗
PubMed2002

Preferential binding of the anticancer drug rViscumin (recombinant mistletoe lectin) to terminally alpha2-6-sialylated neolacto-series gangliosides.

Production of biochemically defined recombinant mistletoe lectin was achieved by cloning and separate expression of the single catalytically active A-chain and the B-chain with carbohydrate binding properties in Escherichia coli, yielding an active heterodimeric protein named rViscumin (Eck et al. [1999] Eur. J. Biochem., 265, 788-797). Employing solid phase binding assays, rViscumin was shown to preferentially bind to terminally alpha2-6-sialylated neolacto-series gangliosides IV(6)Neu5Ac-nLc4Cer, VI(6)Neu5Ac-nLc6Cer, and VIII(6)Neu5Ac-nLc8Cer isolated from human granulocytes. Only marginal binding of rViscumin to galactose-terminated neutral GSLs was determined, whereas reinvestigation of ricin specificity demonstrated this lectin as a galactose-binding protein. Human promyelotic HL-60 cells exhibited an IC(50) value (half maximum cytotoxicity) of 1.16 pM and human bladder carcinoma 5637 cells of 12.1 pM rViscumin; CHO-K1 cells were resistant to rViscumin treatment up to a concentration of 5.26 nM tested. Quantification of the predominant receptor ganglioside IV(6)Neu5Ac-nLc4Cer by means of a specific anti-Neu5Acalpha2-6Galbeta1-4GlcNAc-R antibody revealed 3.68 x 10(6) and 1.54 x 10(6) receptor molecules per HL-60 and 5637 cell, respectively; CHO-K1 cells were negative, lacking alpha2-6-sialylated gangliosides. The data imply a direct correlation of rViscumin cytotoxicity and the expression of receptor ganglioside. Moreover, CHO-K1 cells were rendered susceptible toward rViscumin cytotoxicity after exogenous application of human granulocyte gangliosides. Thus, (1) rViscumin has to be considered as a sialic acid-specific rather than a galactose-specific type II ribosome-inactivating protein, and (2) neolacto-series gangliosides with Neu5Acalpha2-6Galbeta1-4GlcNAc-terminus are true functional and physiologically relevant rViscumin receptors.

Animals↗
PubMed2000

Alleviation of neuronal ganglioside storage does not improve the clinical course of the Niemann-Pick C disease mouse.

Niemann-Pick disease Type C (NP-C) is a progressive neurodegenerative disorder caused by mutations in the NPC1 gene and characterized by intracellular accumulation of cholesterol and sphingo-lipids. The major neuronal storage material in NP-C consists of gangliosides and other glycolipids, raising the possibility that the accumulation of these lipids may participate in the neurodegenerative process. To determine if ganglioside accumulation is a crucial factor in neuropathogenesis, we bred NP-C model mice with mice carrying a targeted mutation in GalNAcT, the gene encoding the beta-1-4GalNAc transferase responsible for the synthesis of GM2 and complex gangliosides. Unlike the NP-C model mice, these double mutant mice did not exhibit central nervous system (CNS) accumulation of gangliosides GM2 or of glycolipids GA1 and GA2. Histological analysis revealed that the characteristic neuronal storage pathology of NP-C disease was substantially reduced in the double mutant mice. By contrast, visceral pathology was similar in the NP-C and double mutant mice. Most notably, the clinical phenotype of the double mutant mice, in the absence of CNS ganglioside accumulation and associated neuronal pathology, did not improve. The results demonstrate that complex ganglioside storage, while responsible for much of the neuronal pathology, does not significantly influence the clinical phenotype of the NP-C model.

Animals↗
PubMed1979

Studies on the glycosphingolipids of the starfish, Asterina pectinifera. III. Isolation and structural studies of two novel gangliosides containing internal sialic acid residues.

Two gangliosides, provisionally named Gangliosides 1 and 2 in previous studies, were isolated from starfish, Asterina pectinifera by silicic acid, DEAE-Sephadex, and Iatrobeads column chromatography procedures, and preparative thin-layer chromatography, and their structures were established. On the basis of the results of partial acid hydrolysis, methylation and oxidation with chromium trioxide, Gangliosides 1 and 2 were proposed to be Ara p beta(1 leads to 6)Gal p beta(1 leads to 4)8-O-MeNeuGc(2 leads to 3)Gal p beta(1 leads to 4)Glc p beta(1 leads to 1)-ceramide and Ara p beta(1 leads to 6)Gal p beta(1 leads to 4)NeuGc(2 leads to 3)Gal p beta(1 leads to 4)Glc p beta(1 leads to 1)-ceramide, respectively. The ceramide moieties of both gangliosides had similar phytosphingosine and 2-hydroxy fatty acid compositions, and both gangliosides were structurally related to the previously described Ganglioside 3.

Animals↗
PubMed1984

Ganglioside composition of chromaffin granule membrane in bovine adrenal medulla.

The ganglioside composition of chromaffin granule membranes of bovine adrenal medulla was investigated. Two major gangliosides, which accounted for over 95% of total gangliosides, were characterized as GM3 (NeuAc) and GM3 (NeuGc) by thin layer chromatography (TLC) and gas-liquid chromatography (GLC). Chromaffin granule membranes contained a relatively higher concentration of gangliosides than the membranes of other subcellular organelles; three times higher than microsomal membranes and seven times higher than mitochondrial membranes. This high concentration of ganglioside in chromaffin granule membranes could contribute to the high concentration of gangliosides in the adrenal medulla as compared to other extraneural tissues.

Adrenal Medulla↗
PubMedDate not supplied

Serum total gangliosides and TA90-IC levels: novel immunologic markers in colorectal cancer.

BACKGROUND: Because of the challenge in defining prognostic markers predictive of recurrence or progression, carcinoembryonic antigen (CEA) remains the most frequently used marker in colorectal cancer, despite its low sensitivity. We hypothesized that TA90-IC status and serum ganglioside levels might be useful markers and might be of prognostic significance in colorectal cancer. METHODS: Serum samples from 68 patients undergoing surgical treatment for histologically proven colorectal cancer were analyzed for the presence of CEA, serum gangliosides, and TA90-IC. Forty-one patients had node-negative disease, whereas 27 patients had limited metastatic disease. The intent was curative resection, even for patients with metastatic disease. Cryopreserved serum specimens were analyzed in a blinded fashion for total serum ganglioside levels (by an assay that detects lipid-associated sialic acids), for CEA, and for TA90-IC (by a murine monoclonal antibody-based enzyme-linked immunosorbent assay). A positive value for TA90-IC levels was defined as an optical density (OD) of more than 0.410 at 405 nm. RESULTS: Serum ganglioside levels were elevated more frequently than CEA concentrations (84% vs 44%). The combination of serum ganglioside and CEA values was more sensitive (88%) than CEA value alone (44%) in identifying patients with early-stage colorectal cancer. TA90-IC levels were elevated more frequently than CEA concentrations (56% vs 32%). The combination of TA90-IC and CEA values was more sensitive (72%) than CEA value alone (32%) in identifying patients with advanced-stage colorectal cancer. At an enzyme-linked immunosorbent assay cutoff level of 0.410, 15 (56%) patients had positive TA90-IC values. Fourteen patients alive with residual disease had a median OD TA90-IC level of 0.879, and only three patients had levels below the OD cutoff value of 0.410. Thirteen patients with no evidence of disease had a median level of 0.277, and only four patients had OD levels > or = 0.410. TA90-IC was significantly higher in the alive with residual disease patients than those rendered no evidence of disease (P = 0.02). CONCLUSIONS: We speculate that a multiple-marker analysis that combines CEA values with serum ganglioside and TA90-IC values may be more sensitive than CEA value alone for detecting colorectal cancer. The potential prognostic significance of TA90-IC status in advanced disease warrants further investigation.

Adult↗