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PubMed1988

A novel tumor-associated, developmentally regulated glycolipid antigen defined by monoclonal antibody ACFH-18.

A mouse IgM monoclonal antibody, ACFH-18, was established after immunization of mice with the human gastric cancer cell line MKN74. The antibody reacts strongly with gastrointestinal carcinoma and showed a clear dependence on the degree of differentiation of gastric cancer cells. The antibody defines a series of glycolipid species with extremely slow TLC mobility present in both acidic and neutral glycolipid fractions of the extract from gastrointestinal adenocarcinoma and the original MKN74 cells. Isolation and structural study of the active glycolipids present in the acidic and neutral fractions and comparison of the antibody reactivity with glycolipids having related structures revealed a novel specificity. The minimum requirement for the maximal reactivity of ACFH-18 was identified as VII3Fuc-nLc10 (Structure A below and Fig. 8 in text). Since the antibody did not react with III3Fuc-nLc6 (Structure B below), which shares the same terminal sequence as VII3Fuc-nLc10, and since it cross-reacted with VII3Fuc-nLc8 (Z1 glycolipid) and VII3Fuc,V3-Fuc,III3Fuc-nLc8 (Z3 glycolipid), antibody ACFH-18 is capable of recognizing a fucosyl residue plus an internal repeating N-acetyllactosamine proximal to ceramide, as indicated by lines in Fig. 8 (Structures A, B, and E-G). (Formula: see text).

Animals↗
PubMed1986

Sialylated glycolipid antigens on human leukemic cell lines.

Many granulocyte-specific mouse monoclonal antibodies recognize the carbohydrate sequence 3-fucosyllactosamine, Ga 1 beta 1-4[Fuc alpha 1-3]GlcNAc, which occurs in cell-surface glycolipids and glycoproteins. In general, these antibodies bind to blast cells from most patients with acute myeloblastic leukemia, but not to those with acute lymphocytic leukemia. Neuraminidase treatment, however, increases exposure of this antigen on both myeloid and lymphoid cells. In the present study, the glycolipids from 13 lymphoid and nonlymphoid human cell lines were examined for the presence of unsialylated and sialylated 3-fucosyllactosamine sequences using a thin-layer chromatography immunostaining method. Nine of the cell lines were also tested by indirect immunofluorescence both before and after neuraminidase treatment. None of the six B-cell and T-cell lines had detectable neutral or sialylated glycolipid antigen. In contrast, six out of seven and five out of seven nonlymphoid cell lines had neutral and sialylated glycolipid antigens, respectively. These results agreed, in general, with those found by indirect immunofluorescence. They also represent the first direct demonstration of these sialylated glycolipids on human leukemic cells. Thus, in some cases increased antibody binding to neuraminidase-treated cells can be explained by the presence of sialylated glycolipid antigen.

Antibodies, Monoclonal↗
PubMed1984

Analysis of the major antigenic determinants of the characteristic phenolic glycolipid from Mycobacterium leprae.

Antibodies to the major phenolic glycolipid purified from Mycobacterium leprae have been demonstrated previously in sera of leprosy but not tuberculosis patients using an ELISA. The major antigenic determinants on this molecule were investigated using antisera raised in rabbits to the purified glycolipid and with a pool of sera from human lepromatous leprosy patients. A small, but significant cross-reaction was observed with the glycolipids from M. bovis and M. kansasii, which contain the phenolphthiocerol dimycocerosate part of the molecule but have different sugars, and also with a semi-synthetic 'attenuation indicator lipid' which shares the phenolphthiocerol but has no sugars. There was however no cross-reaction with phthiocerol dimycocerosate. The disaccharide, corresponding to the two terminal sugars of the M. leprae glycolipid has been chemically synthesized and shown to inhibit the reaction between glycolipid and antibody in the ELISA. The cross-reactivity observed with the M. bovis and M. kansasii glycolipids was not inhibited by the synthetic disaccharide. These findings suggest that the cross-reactivity is associated with the phenol ring and implies the disaccharide may be a unique antigenic determinant of M. leprae.

Animals↗
PubMed1984

Effects of sodium butyrate, dimethyl sulfoxide, and retinoic acid on glycolipids of human rectal adenocarcinoma cells.

In the present study, we have examined the neutral glycolipids, gangliosides, and sulfoglycolipids of human rectal adenocarcinoma (HRT-18) cells and the alterations produced by the differentiating agents, sodium butyrate, dimethyl sulfoxide, and retinoic acid. Thin-layer chromatography of neutral glycolipids showed that HRT-18 cells contained mono- and diglycosylceramides. Cells treated with differentiating agents had additional glycolipids which comigrated with tri- and tetraglycosylceramides. Labeling of neutral glycolipids with [3H]galactose showed that HRT-18 cells also contain glycosylceramides larger than diglycosylceramides which also were altered by treatment with differentiating agents. In studies of acidic glycolipids, GM3, the major ganglioside in untreated cells, was reduced in cells treated with retinoic acid but not in cells treated with other agents. Upon labeling with radioactive galactose, changes were seen only in the minor ganglioside components of treated cells. Differentiating agents also altered the patterns of sulfogalactolipids and fucolipids in HRT-18 cells. In the case of fucolipids, 2 new bands were observed in the cells treated with dimethyl sulfoxide and retinoic acid. The changes brought about by differentiating agents may identify glycolipids involved in the process of tumorigenicity.

Adenocarcinoma↗
PubMed1982

Neutral glycolipid antigens as developmental markers of mouse teratocarcinoma and early embryos: an immunologic and chemical analysis.

Purified rabbit antibodies to neutral glycolipids were analyzed for their binding to mouse embryonal carcinoma cells (ECC) and preimplantation mouse embryos. Antibodies to globotetraosylceramide first bind to 2 to 4-cell embryos and reach a peak of staining intensity with morulae, whereas anti-Forssman antibodies first bind to late morulae and then, most intensely, to early blastocysts. We compared the binding of a monoclonal anti-Forssman antibody with that of rabbit anti-Forssman antibodies and show that although they react similarly with ECC, they do not do so with morulae: The monoclonal antibody stained weakly and unevenly, whereas the rabbit antiserum produced a uniformly bright immunofluorescent staining. Chemical analyses revealed that globotetraosylceramide is the most abundant glycolipid of F9 ECC and that there is poor correlation between the concentration of individual glycolipids in these cells and their reactivity with antibodies to glycolipid molecules. Interestingly, the 2 Forssman antibody-reactive glycolipids of F9 ECC differ in their mobility on TLC plates from the classical Forssman antigen extracted from sheep red blood cells. This illustrates the potential problems in extrapolating from the coincident binding properties of an anti-glycolipid antibody to the chemical structure or abundance of an antigen in different cell types.

Animals↗
PubMed1982

Structures of branched blood group A-active glycosphingolipids in human erythrocytes and polymorphism of A- and H-glycolipids in A1 and A2 subgroups.

The structures of two branched variants of blood group A-active glycolipid, Ac and Ad (Hakomori, S., Stellner, K., and Watanabe, K. (1972) Biochem. Biophys. Res. Commun. 49, 1061-1068), isolated from human type A-erythrocytes, were elucidated. The intact glycolipids and fragments produced by treatment with endo-beta-galactosidase from Escherichia freundii (Fukuda, M. N., and Matsumura, G. (1976) J. Biol. Chem. 251, 6218-6225) were analyzed by methylation. In addition, a specific limited enzyme digestion of Ad-glycolipid was made by incorporating the glycolipid into liposomes before endo-beta-galactosidase digestion. The method preferentially hydrolyzed one of the side chains carrying an A-determinant leaving a core which was recovered from the liposomes. The Ac- and Ad- glycolipids have two branched carbohydrate chains with 12 and 14 sugar residues, respectively, and both have two A-determinants as shown below. (formula see text). The structures of A- and H-active variants isolated from subgroups A1 and A2 have been compared. The results indicate that A variants from A1 or A2 erythrocytes have identical structures, and that H-variants isolated from A2 erythrocytes are identical to those isolated from O erythrocytes. Thus, there is no qualitative structural difference in A-active glycolipids between A1 and A2 erythrocytes.

ABO Blood-Group System↗
PubMed1982

A new glycolipid antigen isolated from human erythrocyte membranes reacting with antibodies directed to globo-N-tetraosylceramide (globoside).

Two glycolipid fractions were separated by high performance liquid chromatography from human erythrocyte membranes and which were reactive with antibodies to globo-N-tetraosylceramide (globoside). The reactivity to the antibody was abolished by treatment with endo-beta-galactosidase of Escherichia freundii which specifically hydrolyzes lacto-N-glycosyl series glycolipids, but does not hydrolyze globo series glycolipids. One of the fractions was isolated by repeated high performance liquid chromatography, and its structure was determined by direct probe mass spectrometry, methylation analysis, and by degradation with exo- and endoglycosidases as follows: GalNAc beta 1 leads to 3Gal beta 1 leads to 4GLcNAc beta 1 leads to 3 Gal beta 1 leads to 4Glc beta 1 leads to 1ceramide. The carbohydrate structure was identical with the asialo core of "G3-ganglioside" (IV3NeuAc2 leads to 3GalNAcLcnOs4Cer) (Watanabe, K., and Hakomori, S. (1979) Biochemistry 14,5502-5504), but the ceramide moiety of this glycolipid was characterized by having C22 and C24 fatty acids in a striking contrast to that G3-ganglioside was characterized by the predominance of C14 fatty acid. Since globoside was previously identified as blood group P antigen (Marcus, D. M., Kundu, S. K., and Suzuki, A. (1981) Semin. Hematol. 18, 63-71), and both globoside and this glycolipid possess the common terminal structure GalNAc beta 1 leads to 3Gal, this glycolipid may represent the second blood group P antigen belonging to the lacto series.

Antibodies↗
PubMed1981

Stimulation of glycolipid synthesis and exchange by human serum high density lipoprotein-3 in human fibroblasts and leukocytes.

Upon exposure to either human skin fibroblasts or human circulating leukocytes, the composition of human serum high density lipoprotein-3 (HDL3) was modified by the apparent loss of apolipoprotein A-II and a 2- to 4-fold increase in glycosphingolipid content. Exposure of HDL3 to leukocytes produced an increase in the content of lactosylceramide, which is the major glycolipid in leukocytes, whereas exposure of HDL3 to human skin fibroblasts produced predominantly an increase in trihexosylceramide, which is the major glycolipid in fibroblasts. Other protein components of HDL3 (such as apolipoprotein A-I) were unaffected and there were no major changes in either neutral lipid or phospholipid composition. The increase in glycosphingolipid content of both cells and reisolated HDL3 particles was HDL3 concentration-dependent up to a concentration of 1 mg/ml and appeared to be the result of a stimulation of cellular glycolipid synthesis by HDL3 and subsequent transfer to HDL3 in the medium. A similar stimulation could not be produced by either low density lipoprotein or lipoprotein-deficient human serum. The coaddition of HDL3 and lipoprotein-deficient serum reduced both the loss of apolipoprotein A-II and the change in HDL3 glycolipid content, but not the increase in cellular glycolipid content, suggesting that modification of the apolipoprotein A-II peptide may enhance the ability of HDL3 to acquire new glycolipid from cells.

Cells, Cultured↗
PubMed1980

Adaptation of mass spectrometry for the analysis of tumor antigens as applied to blood group glycolipids of a human gastric carcinoma.

Total neutral (nonacidic) glycolipid fractions have been isolated from a gastric adenocarcinoma and the surrounding normal gastric tissue removed at laparotomy of a Blood Group B human individual. Each glycolipid mixture was fractionated by silicic acid column chromatography into ten different partly purified glycolipid fractions. These fractions were analyzed by thin-layer chromatography and tested for Blood Group A and B activity. Blood group B activity was found in several fractions from both tumor and normal tissue. Two of the tumor glycolipid fractions reacted with some batches of commercial anti-A antisera, but other antisera tested did not react. No such Blood Group A reactivity was found in the fractions from the normal gastric tissue. The two Blood Group A-active tumor glycolipid fractions were methylated and methylated-reduced, and these two derivatives were analyzed by mass spectrometry. It was shown that these two fractions were mixtures of glycosphingolipids with five to nine sugars. The dominating glycosphingolipids were blood group Leb and B-like hexaglycosylceramides, a B-similar heptaglycosylceramide with an additional fucose, an H-like heptaglycosylceramide, and a Leb-like octaglycosylceramide. Evidence for small amounts of a Blood Group A-similar heptaglycosylceramide with an additional fucose was also found. The finding of a Blood Group A-similar glycolipid in a fraction which reacts with some anti-A antisera is the first chemical evidence for a heterolog blood group antigen in human cancer which has previously been found by histoimmunological techniques. The clinical significance of this finding is discussed in relation to diagnostic procedures and immunotherapy.

ABO Blood-Group System↗
PubMedDate not supplied

[The glycolipid composition of Francisella tularensis strains with different degrees of attenuation].

The glycolipid composition of F. tularensis strains was investigated by silica gel thin-layer chromatography. Vaccine strains in contrast to virulent ones lacked glycolipid 8, possessed new glycolipid 8-a and a higher level of glycolipid 7. Low immunogenic strains had a decreased content of glycolipids, while avirulent non-immunogenic strain (15-a) nearly completely lost them. Thus, the glycolipid composition is associated with the level of attenuation, virulence and immunogenicity of F. tularensis.

Bacterial Vaccines↗
PubMed1996

Aglycone modulation of glycolipid receptor function.

The aglycone has been largely ignored in consideration of glycoconjugate function. Evidence is reviewed which suggests that the role of the lipid in glycolipid carbohydrate function may be particularly significant. The lipid moiety can promote or reduce carbohydrate exposure of membrane glycolipids. Theoretical calculation has indicated that the plane of the plasma membrane can restrict the permitted conformations of a given glycolipid oligosaccharide. Thus the lipid moiety may influence the relative conformation of such carbohydrate sequences. Evidence of ceramide regulation of glycolipid function can be found in studies of enzyme substrate specificity, antiglycolipid recognition and bacterial/host cell interactions. Studies of verotoxin binding to its glycolipid receptor globotriaosyl ceramide indicate that modulation of receptor function by glycolipid fatty acid content plays an important role in in vitro binding assays, cell cytotoxicity and intracellular routing.

Receptors, Cell Surface↗
PubMed1985

Properties of a specific glycolipid transfer protein from bovine brain.

A transfer protein specific for glycolipids has been isolated from bovine brain. As judged by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis, the protein is 68% pure and has a molecular weight of 20 000. Three different assays were employed to study the protein's specificity and glycolipid binding properties. The protein transferred several different neutral glycosphingolipids and ganglioside GM1 equally well, but failed to accelerate phosphatidylcholine or sphingomyelin intervesicular movement. The protein's ability to interact with glycolipids was strongly influenced by the physical properties of the matrix phospholipid in which the glycolipids reside. Both the phase state of the phospholipid matrix and bilayer curvature affected glycolipid intervesicular transfer rates. Protein binding to phospholipid vesicles containing either tritium-labeled or pyrene-labeled glucosylceramide could not be demonstrated by density gradient centrifugation or fluorescence energy transfer measurements, respectively. A specific association of the transfer protein for pyrene-labeled glucosylceramide was found when the fluorescence emission of the pyrene excimer-to-monomer ratio was measured suggesting that a portion of the fluorescent glycolipid was being sequestered from the phospholipid vesicles and was binding to the freely soluble protein.

Animals↗
PubMed1998

The role of globo-series glycolipids in neuronal cell differentiation--a review.

Alterations in glycolipid composition as well as glycosyltransferase activities during cellular differentiation and growth have been well documented. However, the underlying mechanisms for the regulation of glycolipid expression remain obscure. One of the major obstacles has been the lack of a well defined model system for studying these phenomena. We have chosen PC12 pheochromocytoma cells as a model because (a) the properties of these cells have been well characterized, and (b) they respond to nerve growth factor (NGF) by differentiating into sympathetic-like neurons and are amenable to well-controlled experimentation. Thus, PC12 cells represent a suitable model for studying changes in glycolipid metabolism in relation to cellular differentiation. We have previously shown that subcloned PC12 cells accumulate a unique series of globo-series neutral glycolipids which are not expressed in parental PC12 cells. This unusual change in glycolipid distribution is accompanied by changes in the activities of specific glycosyltransferases involved in their synthesis and is correlated with neuritogenesis and/or cellular differentiation in this cell line. We have further demonstrated that changes in the glycosyltransferase activities may be modulated by the phosphorylation states of the cells via protein kinase systems. We conclude that these unique globo-series glycolipids may play a functional role in the initiation and/or maintenance of neurite outgrowth in PC12 cells.

Animals↗
PubMed2004

Carbohydrates act as receptors for the periodontitis-associated bacterium Porphyromonas gingivalis: a study of bacterial binding to glycolipids.

In this study we show for the first time the use of carbohydrate chains on glycolipids as receptors for the periodontitis-associated bacterium Porphyromonas gingivalis. Previous studies have shown that this bacterium has the ability to adhere to and invade the epithelial lining of the dental pocket. Which receptor(s) the adhesin of P. gingivalis exploit in the adhesion to epithelial cells has not been shown. Therefore, the binding preferences of this specific bacterium to structures of carbohydrate origin from more than 120 different acid and nonacid glycolipid fractions were studied. The bacteria were labeled externally with (35)S and used in a chromatogram binding assay. To enable detection of carbohydrate receptor structures for P. gingivalis, the bacterium was exposed to a large number of purified total glycolipid fractions from a variety of organs from different species and different histo-blood groups. P. gingivalis showed a preference for fractions of human and pig origin for adhesion. Both nonacid and acid glycolipids were used by the bacterium, and a preference for shorter sugar chains was noticed. Bacterial binding to human acid glycolipid fractions was mainly obtained in the region of the chromatograms where sulfated carbohydrate chains usually are found. However, the binding pattern to nonacid glycolipid fractions suggests a core chain of lactose bound to the ceramide part as a tentative receptor structure. The carbohydrate binding of the bacterium might act as a first step in the bacterial invasion process of the dental pocket epithelium, subsequently leading to damage to periodontal tissue and tooth loss.

Carbohydrate Metabolism↗
PubMed1991

Human heterophile antibodies recognizing epitopes present on insect glycolipids.

As a consequence of detecting an IgM M-protein (naturally occurring diseased-state monoclonal antibody) immunoreactive to insect acidic glycolipids in a patient with demyelinating peripheral neuropathy, normal human sera were examined for the occurrence of heterophile antibodies directed against carbohydrate epitopes present on glycosphingolipids of Calliphora vicina (Insecta: Diptera). The insect glycolipids can be separated into neutral, zwitterionic, and acidic types, according to whether the oligosaccharide chains consist of neutral monosaccharides only, or carry an additional phospho-ethanolamine side chain and/or a beta-glucuronic acid residue, respectively. Natural antibody activity to these three classes of insect glycosphingolipids was detected in all normal human sera examined. The antibody activities were separated by sequential chromatography on affinity columns of octyl-Sepharose 4B-bound neutral and zwitterionic glycolipids into three populations with differing epitope-type specificities. As expected for heterophile antibodies, they are mainly of the IgM class. Population I recognized epitopes present on the three types of insect glycolipids, i.e., the neutral oligosaccharide chain backbone, the main determinant of which contains a terminal N-acetylhexosamine. Immunoreactivity is separable into at least four subpopulations of differing carbohydrate epitope specificity. Population II recognized epitopes containing phosphoethanolamine in zwitterionic and some acidic insect glycolipids. There are two subpopulations, the majority of which require the free amino group of phosphoethanolamine for immunoreactivity. Population III antibodies showed immunoreactivity to terminal beta-glucuronic acid-containing epitopes present only on acidic insect glycolipids.

Animals↗
PubMed2002

Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis.

Sulfated trehalose glycolipids are among the most characteristic cell wall molecules of virulent strains of Mycobacterium tuberculosis. They comprise a family of trehalose-2-sulfate esters with an array of acyl fatty acids at various positions of the trehalose moiety. Although their structure has been well characterized, most of the enzymes involved in their biosynthesis, such as sulfotransferases, are unknown. It is demonstrated here by metabolic labelling with 35S abundant incorporation into sulfolipids of M. tuberculosis strains, in comparison to Mycobacterium avium, Mycobacterium bovis BCG and Mycobacterium smegmatis. The most abundant sulfolipid, sulfolipid I, is present in virulent strains H37Rv and Erdman, but absent in attenuated H37Ra. Sulfotransferase assays with the donor substrate 3'-phosphoadenosine-5'-[35S]phosphosulfonate and whole cell lysates of H37Ra resulted in the synthesis of four major sulfolipids (I, II, IV and VI). A search for sulfotransferase gene sequences in M. tuberculosis yielded gene Rv1373, a 981 bp gene slightly homologous (24% identity) to eukaryotic aryl-sulfotransferases. Rv1373 was cloned by PCR and expressed as a 39 kDa recombinant his-tagged protein. The recombinant M. tuberculosis aryl-sulfotransferase exhibited activity towards the cerebroside glycolipids glucosyl- and galactosylceramide. No activity was detected with sulfatide (3'-sulfated galactosylceramide), suggesting that sulfation of galactosylceramide may occur at C-3 of the galactose. Treatment of sulfated products with ceramide glycanase resulted in the release of 35S-labelled material showing that sulfation was at the saccharide moiety (galactose or glucose) of the ceramide. Assays with the M. tuberculosis aryl-sulfotransferase and total H37Ra glycolipids showed one major product corresponding to sulfolipid IV. These results demonstrate that Rv1373 encodes a novel glycolipid sulfotransferase with activity towards typical ceramide glycolipids and mycobacterial trehalose glycolipids.

Amino Acid Sequence↗
PubMed2002

[Anti-glycolipid antibodies in the diagnosis of autoimmune neuropathies]

Recent years have seen major progress in our understanding of the clinical pathophysiology of autoimmune neuropathies particularly with the identification and analysis of antibodies to gangliosides and related glycolipids in the serum of patients. Anti-glycolipid antibodies react with epitopes on the carbohydrate region of glycolipid molecules and can be routinely measured by standard immunoassays. In multifocal motor neuropathy, IgM anti-GM1 antibodies that cross react with GD1b and asialo-GM1 are detectable in around 50p. 100 of cases. This condition may clinically resemble certain forms of lower motor neurone disease. IgM anti-GD1b antibodies are found in IgM paraproteinaemic neuropathy characterised by profound sensory ataxia. In the anti-myelin associated glycoprotein (anti-MAG) IgM paraproteinaemic neuropathy, antibodies also react with the acidic glycolipids, sulphated glucuronyl paragloboside and its higher lactosaminyl homologue (SGPG and SGPLG). Thus a variety of chronic syndromes can be defined by their anti-glycolipid antibody profile. In Guillain-Barré syndrome, anti-GM1, GM1b, GD1a and GalNAc-GD1a antibodies are found in patients with acute motor axonal neuropathy (AMAN) and anti-GQ1b IgG antibodies are a very sensitive and specific marker for the Miller Fisher syndrome. Many other anti-glycolipid antibodies are being increasingly identified in other neuropathy subtypes. The article will summarise existing clinical and serological information in this field.

Journal Article↗
PubMed2002

Anti-glycolipid antibodies in the diagnosis of autoimmune neuropathies.

Recent years have seen major progress in our understanding of the clinical pathophysiology of autoimmune neuropathies particularly with the identification and analysis of antibodies to gangliosides and related glycolipids in the serum of patients. Anti-glycolipid antibodies react with epitopes on the carbohydrate region of glycolipid molecules and can be routinely measured by standard immunoassays. In multifocal motor neuropathy, IgM anti-GM1 antibodies that cross react with GD1b and asialo-GM1 are detectable in around 50p. 100 of cases. This condition may clinically resemble certain forms of lower motor neurone disease. IgM anti-GD1b antibodies are found in IgM paraproteinaemic neuropathy characterised by profound sensory ataxia. In the anti-myelin associated glycoprotein (anti-MAG) IgM paraproteinaemic neuropathy, antibodies also react with the acidic glycolipids, sulphated glucuronyl paragloboside and its higher lactosaminyl homologue (SGPG and SGPLG). Thus a variety of chronic syndromes can be defined by their anti-glycolipid antibody profile. In Guillain-Barré syndrome, anti GM1, GM1b, GD1a and GalNAc-GD1a antibodies are found in patients with acute motor axonal neuropathy (AMAN) and anti-GQ1b IgG antibodies are a very sensitive and specific marker for the Miller Fisher syndrome. Many other anti-glycolipid antibodies are being increasingly identified in other neuropathy subtypes. The article will summarise existing clinical and serological information in this field.

Acute Disease↗