Glycolipids
Glycosphingolipids
Chromatography, Thin Layer
Globosides
Sulfoglycosphingolipids
Carbohydrate Sequence
Gangliosides
Cerebrosides
Lactosylceramides
Forssman Antigen
Galactolipids
Galactosylceramides
Carbohydrates
Glucosylceramides
Spectrometry, Mass, Fast Atom Bombardment
Trihexosylceramides
ABO Blood-Group System
Chromatography, Gas
Fatty Acids
Blood Group Antigens
Glycoconjugates
Galactose
Lewis Blood-Group System
Oligosaccharides
G(M1) Ganglioside
Galactosyltransferases
Molecular Sequence Data
Mass Spectrometry
Membrane Lipids
Antigens, CD1d
Magnetic Resonance Spectroscopy
G(M3) Ganglioside
Antigens, CD1
Sialic Acids
Antigens, CD15
Ceramides
G(M2) Ganglioside
Monosaccharides
P Blood-Group System
Sphingomonas
Phospholipids
Glycosylphosphatidylinositols
Mycobacterium marinum
Natural Killer T-Cells
Gas Chromatography-Mass Spectrometry
I Blood-Group System
Lipids
Galactose Oxidase
Gangliosidoses
Glycosyltransferases
Sulfuric Acids
Mannose
Halobacteriaceae
N-Acetylneuraminic Acid
Neutral Glycosphingolipids
Molecular Structure
Glyceryl Ethers
Sphingolipids
Phosphatidylinositols
Glycoproteins
Fucosyltransferases
Chromatography, High Pressure Liquid
Lectins
Ustilaginales
Chemistry
Sialyltransferases
Chemical Phenomena
Acholeplasma laidlawii
Cord Factors
Erythrocytes
Glycosides
Adhesins, Escherichia coli
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Hemadsorption Inhibition Tests
Methylation
Cell Wall
Chloroform
A genetic model of substrate deprivation therapy for a glycosphingolipid storage disorder. (1/2592)
Inherited defects in the degradation of glycosphingolipids (GSLs) cause a group of severe diseases known as GSL storage disorders. There are currently no effective treatments for the majority of these disorders. We have explored a new treatment paradigm, substrate deprivation therapy, by constructing a genetic model in mice. Sandhoff's disease mice, which abnormally accumulate GSLs, were bred with mice that were blocked in their synthesis of GSLs. The mice with simultaneous defects in GSL synthesis and degradation no longer accumulated GSLs, had improved neurologic function, and had a much longer life span. However, these mice eventually developed a late-onset neurologic disease because of accumulation of another class of substrate, oligosaccharides. The results support the validity of the substrate deprivation therapy and also highlight some limitations. (+info)Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL. (2/2592)
T cell receptor (TCR) recognition of nonpeptidic and modified peptide antigens has been recently uncovered but is still poorly understood. Immunization with an H-2Kb-restricted glycopeptide RGY8-6H-Gal2 generates a population of cytotoxic T cells that express both alpha/beta TCR, specific for glycopeptide, and gamma/delta TCR, specific for the disaccharide, even on glycolipids. The crystal structure of Kb/RGY8-6H-Gal2 now demonstrates that the peptide and H-2Kb structures are unaffected by the peptide glycosylation, but the central region of the putative TCR binding site is dominated by the extensive exposure of the tethered carbohydrate. These features of the Kb/RGY8-6H-Gal2 structure are consistent with the individual ligand binding preferences identified for the alpha/beta and gamma/delta TCRs and thus explain the generation of a carbohydrate-specific T cell response. (+info)Cryptosporidium parvum sporozoite pellicle antigen recognized by a neutralizing monoclonal antibody is a beta-mannosylated glycolipid. (3/2592)
The protozoan parasite Cryptosporidium parvum is an important cause of diarrhea in humans, calves, and other mammals worldwide. No approved vaccines or parasite-specific drugs are currently available for the control of cryptosporidiosis. To effectively immunize against C. parvum, identification and characterization of protective antigens are required. We previously identified CPS-500, a conserved, neutralization-sensitive antigen of C. parvum sporozoites and merozoites defined by monoclonal antibody 18.44. In the present study, the biochemical characteristics and subcellular location of CPS-500 were determined. CPS-500 was chloroform extractable and eluted with acetone and methanol in silicic acid chromatography, consistent with being a polar glycolipid. Following chloroform extraction and silicic acid chromatography, CPS-500 was isolated by high-pressure liquid chromatography for glycosyl analysis, which indicated the presence of mannose and inositol. To identify which component of CPS-500 comprised the neutralization-sensitive epitope recognized by 18.44, the ability of the monoclonal antibody to bind CPS-500 treated with proteases, or with alpha- or beta-glycosidases, was determined. Monoclonal antibody 18.44 did not bind antigen treated with beta-D-mannosidase but did bind antigen treated with alpha-D-mannosidase, other alpha- or beta-glycosidases, or a panel of proteases. These data indicated that the target epitope was dependent on terminal beta-D-mannopyranosyl residues. By immunoelectron microscopy, 18.44 binding was localized to the pellicle and an intracytoplasmic tubulovesicular network in sporozoites. Monoclonal antibody 18.44 also bound to antigen deposited and released onto substrate over the course travelled by gliding sporozoites and merozoites. Surface localization, adhesion and release during locomotion, and neutralization sensitivity suggest that CPS-500 may be involved in motility and invasion processes of the infective zoite stages. (+info)Gas-liquid chromatography of the heptafluorobutyrate derivatives of the O-methyl-glycosides on capillary columns: a method for the quantitative determination of the monosaccharide composition of glycoproteins and glycolipids. (4/2592)
We have developed a method involving the formation of hepta-fluorobutyrate derivatives of O-methyl-glycosides liberated from glycoproteins and glycolipids following methanolysis. The stable derivatives of the most common monosaccharides of these glycoconjugates (Ara, Rha, Xyl, Fuc, Gal, Man, Glc, GlcNAc, GalNAc, Neu5Ac, KDN) can be separated and quantitatively and reproducibly determined with a high degree of sensitivity level (down to 25 pmol) in the presence of lysine as an internal standard. The GlcNAc residue bound to Asn in N-glycans is quantitatively recovered as two peaks. The latter were easily distinguished from the other GlcNAc residues of N-glycans, thus allowing a considerable improvement of the data on structure of N-glycans obtained from a single carbohydrate analysis. The most common contaminants present in buffers commonly used for the isolation of soluble or membrane-bound glycoproteins (SDS, Triton X-100, DOC, TRIS, glycine, and polyacrylamide or salts, as well as monosaccharide constituents of proteoglycans or degradation products of nucleic acids) do not interfere with these determinations. A carbohydrate analysis of glycoproteins isolated from a SDS/PAGE gel or from PDVF membranes can be performed on microgram amounts without significant interferences. Since fatty acid methyl esters and sphingosine derivatives are separated from the monosaccharide peaks, the complete composition of gangliosides can be achieved in a single step starting from less than 1 microg of the initial compound purified by preparative Silicagel TLC. Using electron impact ionization mass spectrometry, reporter ions for the different classes of O-methyl-glycosides (pentoses, deoxy-hexoses, hexoses, hexosamines, uronic acids, sialic acid, and KDN) allow the identification of these compounds in very complex mixtures. The mass of each compound can be determined in the chemical ionization mode and detection of positive or negative ions. This method presents a considerable improvement compared to those using TMS derivatives. Indeed the heptafluorobutyrate derivatives are stable, and acylation of amino groups is complete. Moreover, there is no interference with contaminants and the separation between fatty acid methyl-esters and O-methyl glycosides is achieved. (+info)Formation of lipid-linked sugar compounds in Halobacterium salinarium. Presumed intermediates in glycoprotein synthesis. (5/2592)
The ability of bacitracin to inhibit the growth of Halobacterium salinarium suggested that glycosylation of the major envelope component, a high molecular weight glycoprotein, might occur via a pathway involving lipid intermediates. This report demonstrates that the cells have enzymatic activities for formation of lipid-linked sugar compounds having the expected properties of such intermediates. Whole cell homogenate catalyzed the transfer of sugar from UDP-glucose, GDP-mannose, and UDP-N-acetyglucosamine to endogenous lipid acceptors. Two lipid products were formed from UDP-glucose, two from GDP-mannose, and one from UDP-N-acetylglucosamine. Characterization of the partially purified lipids by ion exchange chromatography, thin layer chromatography, and mild acid and base hydrolysis showed the major product in each case to have the properties expected for polyisoprenyl phosphoglucose, polyisoprenyl phosphomannose, and polyisoprenyl pyrophospho-N-acetylglucosamine. Estimates of chain length by thin layer chromatography indicate that the lipid has 11 to 12 isoprene identity as a C55-60-polyisoprenyl pyrophospho-N-acetylglucosamine. The N-acetylglucosamine transferase, present in cell envelope preparations, was partially characterized. The enzyme was found to be extremely halophilic, specifically requiring a high concentration of KCl. Optimum activity was obtained at 4 m KCl and partial substitution of K+ by Na+ resulted in a decrease in activity. (+info)Isolation and characterization of two mouse L cell lines resistant to the toxic lectin ricin. (6/2592)
Two variant mouse L cell lines (termed CL 3 and CL 6) have been selected for resistant to ricin, a galactose-binding lectin with potent cytotoxic activity. The resistant lines exhibit a 50 to 70% decrease in ricin binding and a 300- to 500-fold increase in resistance to the toxic effects of ricin. Crude membrane preparations of CL 3 cells have increased sialic acid content (200% of control), while the galactose, mannose, and hexosamine content is within normal limits. Both the glycoproteins and glycolipids of CL 3 cells have increased sialic acid, with the GM3:lactosylceramide ratios for parent L and CL 3 cells being 0.29 and 1.5, respectively. In contrast, the membranes of CL 6 cells have a decrease in sialic acid, galactose, and hexosamine content with mannose being normal. Both cell lines have specific alterations in glycosyltransferase activities which can account for the observed membrane sugar changes. CL 3 cells have increased CMP-sialic acid:glycoprotein sialyltransferase and GM3 synthetase activities, while CL 6 cells have decrease UDP-GlcNAc:glycoproteinN-acetylglucosaminyltransferase and DPU-galactose:glycoprotein galactosyltransferase activities. The increased sialic acid content of CL 3 cells serves to mask ricin binding sites, since neuraminidase treatment of this cell line restores ricin binding to essentially normal levels. However, the fact that neuraminidase-treated CL 3 cells are still 45-fold resistant to ricin indicates that either a special class of productive ricin binding sites is not being exposed or that the cell line has a second mechanism for ricin resistance. (+info)Participation of a trisaccharide-lipid in glycosylation of oviduct membrane glycoproteins. (7/2592)
Preincubation of a hen oviduct membrane preparation with UDP-Nactyl[14C]glucosamine and bacitracin, followed by incubation with GDP-mannose, leads to formation of a chloroform/methanol (2/1)-extractable glycolipid. Treatment of the lipid with mild acid results in the release of a trisaccharide shown to have the structure beta-mannosyl-N-acetylglucosamineyl-N-acetylglucosamine. Incubation of purified trisaccharide-lipid with oviduct membranes in the presence of sodium deoxycholate, Mn2+, and GDP-mannose leads to formation of a labeled glycoprotein with an apparent molecular weight of 25,000... (+info)A fluorescence resonance energy transfer approach for monitoring protein-mediated glycolipid transfer between vesicle membranes. (8/2592)
A lipid transfer protein, purified from bovine brain (23.7 kDa, 208 amino acids) and specific for glycolipids, has been used to develop a fluorescence resonance energy transfer assay (anthrylvinyl-labeled lipids; energy donors and perylenoyl-labeled lipids; energy acceptors) for monitoring the transfer of lipids between membranes. Small unilamellar vesicles composed of 1 mol% anthrylvinyl-galactosylceramide, 1.5 mol% perylenoyl-triglyceride, and 97.5% 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC) served as donor membranes. Acceptor membranes were 100% POPC vesicles. Addition of glycolipid transfer protein to mixtures of donor and acceptor vesicles resulted in increasing emission intensity of anthrylvinyl-galactosylceramide and decreasing emission intensity of the nontransferable perylenoyl-triglyceride as a function of time. The behavior was consistent with anthrylvinyl-galactosylceramide being transferred from donor to acceptor vesicles. The anthrylvinyl and perylenoyl energy transfer pair offers advantages over frequently used energy transfer pairs such as NBD and rhodamine. The anthrylvinyl emission overlaps effectively the perylenoyl excitation spectrum and the fluorescence parameters of the anthrylvinyl fluorophore are nearly independent of the medium polarity. The nonpolar fluorophores are localized in the hydrophobic region of the bilayer thus producing minimal disturbance of the bilayer polar region. Our results indicate that this method is suitable for assay of lipid transfer proteins including mechanistic studies of transfer protein function. (+info)There are several types of gangliosidoses, including:
1. GM1 gangliosidosis: This is the most common form of the disorder, affecting approximately 1 in 100,000 individuals worldwide. It is caused by a deficiency of the enzyme beta-galactosidase A, which results in the accumulation of GM1 ganglioside in cells.
2. GM2 gangliosidosis: This form of the disorder is similar to GM1 gangliosidosis but affects a different type of ganglioside, GM2. It is also known as Sandhoff disease and is particularly severe, with most children dying before the age of five.
3. Globoid-cell leukodystrophy: This is a rare form of gangliosidosis that affects the brain and spinal cord, leading to progressive loss of myelin, the fatty insulating substance that surrounds nerve fibers.
4. Metachromatic leukodystrophy: This is another rare form of gangliosidosis caused by a deficiency of the enzyme arylsulfatase A. It can lead to progressive loss of myelin and other symptoms such as vision loss, seizures, and difficulty with movement.
There is currently no cure for gangliosidoses, but various treatments are available to manage their symptoms and slow their progression. These may include enzyme replacement therapy, physical therapy, speech therapy, and medications to control seizures and other symptoms. Early detection and intervention can help improve the outlook for individuals with these disorders, but the long-term prognosis is often poor.
Glycolipid
Glycolipid transfer protein
Glycolipid 3-alpha-mannosyltransferase
Glycolipid 2-alpha-mannosyltransferase
Lipid
Sophorolipid
Lactosylceramide
Monogalactosyldiacylglycerol synthase
Stage specific embryonic antigen 3
Saccharolipid
Lyme disease microbiology
Meiothermus
Group 1 CD1-restricted T cells
Sarah Spiegel (biologist)
GLTP
Cell biology
Jeanne E. Pemberton
Peptidoglycolipid addressing protein
Dacryopinax spathularia
Biological membrane
Gintonin
Glycoside
Niemann-Pick disease, type C
Slime layer
Globotriaosylceramide
Methanofollis
Chemical glycosylation
Mycobacterium
Lecithin
Oligosaccharide
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Glycoproteins9
- Within lysosomes, this enzyme plays a role in the breakdown of complexes of sugar molecules (oligosaccharides) attached to certain proteins (glycoproteins) and fats (glycolipids). (medlineplus.gov)
- Without this enzyme, glycolipids and glycoproteins cannot be completely broken down. (medlineplus.gov)
- Brain cells are particularly sensitive to the buildup of glycolipids and glycoproteins, which can result in cell death. (medlineplus.gov)
- Accumulation of glycolipids and glycoproteins also occurs in other organs such as the liver, spleen, skin, heart, pancreas, and kidneys, contributing to the additional symptoms of fucosidosis. (medlineplus.gov)
- More specifically, the structure of glycan moieties on glycoproteins, glycolipids, and glycoconjugates of infectious pathogens plays an important role in determining the balance between health and disease such as AIDS and its persisting oral manifestations. (nih.gov)
- It is well-known that glycan moieties exert profound functional effects on glycoproteins and glycolipid conjugates as they regulate key biological processes. (nih.gov)
- Elucidating glycan structure, their abundance, and their distribution on glycoproteins, glycolipids, and glycoconjugates of infectious pathogens has the potential to provide us with new strategies for identification of a new class of biomarkers and therapeutic targets in the future. (nih.gov)
- It is also not known how the relative abundance and distribution of glycan moieties on glycoproteins and glycolipids influence oral infections and diseases. (nih.gov)
- The tick bite is thought to produce immunoglobulin E (IgE) antibodies to the carbohydrate galactose-alpha-1.3-galactose (alpha-gal), a carbohydrate moiety in mammalian meat glycoproteins or glycolipids. (medscape.com)
Proteins1
- These techniques are increasingly applied to the study of proteins and other macromolecular species such as oligosaccharides and glycolipids. (nih.gov)
Vesicles3
- Again wild-type GLTP and W96 GLTP showed similar behavior in the presence of vesicles containing glycolipids. (abo.fi)
- Effect of lectin-induced agglutination on 13 C nuclear magnetic resonance line width in sonicated phospholipid/glycolipid vesicles. (drsears.com)
- Curatolo WC, Yau AO, Small DM, and Sears B. "Lectin-induced agglutination of phospholipid/glycolipid vesicles. (drsears.com)
Phospholipids2
- least phospholipids and glycolipid fractions with values of 8.20 and 2.60 respectively. (who.int)
- Our lecithin is extracted from soy beans and is composed of various phospholipids, glycolipids, carbohydrates and neutral lipids. (cargill.com)
Membranes2
- In this study we have addressed the ability of the glycolipid transfer protein (GLTP) to transfer anthrylvinyl-galactosylceramide at different pH and sodium chloride concentrations, and the ability of three different mutants to transfer the fluorescently labeled galactosylceramide between donor and acceptor model membranes. (abo.fi)
- Taken together, our data show that the W96 is involved not only in the activity of the protein but also in the interaction between the protein and glycolipid containing membranes. (abo.fi)
Antibodies2
Synthesis1
- Design, synthesis, and functional activity of labeled CD1d glycolipid agonists. (ox.ac.uk)
Molecules1
- Invariant natural killer T cells (iNKT cells) are restricted by CD1d molecules and activated upon CD1d-mediated presentation of glycolipids to T cell receptors (TCRs) located on the surface of the cell. (ox.ac.uk)
Exert1
- We postulated that modifying the glycolipid in this way would exert a minimal impact on the TCR-glycolipid-CD1d ternary complex, allowing the labeled molecule to function as a good mimic for the CD1d agonist under investigation. (ox.ac.uk)
Protein3
- Tryptophan fluorescence emission showed a blue shift of the maximal emission wavelength upon interaction of glycolipid containing vesicle with wild-type GLTP and W96 GLTP, while no blue shift was recorded for the protein variants W85 GLTP and W142 GLTR The quantum yield of tryptophan emission was highest for the W96 GLTP protein whereas W85 GLTP, W142 GLTP and wild-type GLTP showed a lower and almost similar quantum yield. (abo.fi)
- At the molecular level this process was mediated by protein binding to membrane surface sulfatides (Sulf), as indicated by the interference of O4 antibody and Sulf with the attachment of OLs or other Sulf + cells, erythrocytes, to TN-R substrates and by direct protein-glycolipid binding studies. (jneurosci.org)
- 8. Carbohydrate-protein interactions between HNK-1-reactive sulfoglucuronyl glycolipids and the proteoglycan lectin domain mediate neuronal cell adhesion and neurite outgrowth. (nih.gov)
Fatty2
- Associations between serum GDF15 and glycolipid metabolism disorder in metabolic associated fatty liver patients]. (bvsalud.org)
- To investigate relationships between serum growth differentiation factor 15 (GDF15) and glycolipid metabolism in patients with metabolic associated fatty liver disease (MAFLD). (bvsalud.org)
Behavior1
- Because the cytokine response profile is governed by the structure of the glycolipid, we sought a method for labeling various glycolipids to study their in vivo behavior. (ox.ac.uk)
Carbohydrate1
- Glycolipids are located on cell membrane surfaces and have a carbohydrate sugar chain attached to them. (thoughtco.com)
Cell2
Activity1
- Wild-type GLTP and W96 GLTP were both able to transfer anthrylvinylgalactosylceramide, but the two variants W85 GLTP and W142 GLTP did not show any glycolipid transfer activity, indicating that the tryptophan in position 96 is crucial for transfer activity. (abo.fi)
Found1
- Richer 2000 Glycolipids (sulfoquinovosyl diacylglycerol) are found in the chloroplast membrane. (drugs.com)