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At least 793 records · Page 44Linked to original sources
PubMed1999

Incorporation of MAL, an integral protein element of the machinery for the glycolipid and cholesterol-mediated apical pathway of transport, into artificial membranes requires neither of these lipid species.

The MAL proteolipid, an integral membrane protein with selective residence in glycolipid- and cholesterol-enriched membrane (GEM) microdomains, has recently been identified as being an element of the integral protein machinery necessary for apical transport in MDCK cells. With the use of a recombinant baculovirus, we have expressed and purified polyhistidine-tagged MAL to determine whether MAL has special lipid requirements for becoming incorporated into membranes. In contrast with caveolin-1, a component of GEMs that requires cholesterol for its integration into artificial membranes, MAL incorporation took place with dimyristoylphosphatidylcholine as the only lipid component. The presence of cholesterol, sphingomyelin, or galactocerebrosides did not affect the efficiency of this process. These results indicated that MAL is compatible with membranes containing either only phospholipids or also glycolipids and cholesterol and are consistent with the reported requirement of a sorting event for the specific targeting of MAL to GEM microdomains.

Animals↗
PubMed1995

Retinoic acid induces changes in Xenopus embryo glycolipid pattern.

Retinoic acid (RA), known for its important role in cellular differentiation, may cause a modification of glycolipid distribution characterized by a shift from globoserie towards latto- and ganglio-series. In the present paper, we have investigated the modifications of the lipidic pattern after exogenous RA treatment of Xenopus embryos. We have noticed a decrease in neutral glycolipids with a parallel increase in gangliosides; the content of sulfatides does not seem to be modified. Beside the shift toward ganglio-serie, we have also observed a redistribution inside this class of lipids. In particular, following RA treatment, the relative distribution of GD1b and GT1b increases while that of GM3 decreases.

Animals↗
PubMed1995

Glycolipid patterns during Xenopus embryo development.

Glycolipid patterns have been studied during the first six days of Xenopus embryo development. Glycolipid contents showed a sharp increase more evident after the third day of development. Glucosylceramide and sulphatide are not only the most represented species, but also those which exhibit a statistically significant percentage change during early development. Among gangliosides, GD3 is the most represented specie. Two polysialylated gangliosides with not yet established structures are also present.

Ammonia↗
PubMed1984

Cerebral and visceral organ gangliosides and related glycolipids in gm1-gangliosidosis type 1, type 2 and chronic type.

Biochemical analyses of the samples of GM1-gangliosidosis Type 1, Type 2, and Chronic type at autopsy showed that GM1 and asialo-GM1 are markedly increased in the whole cerebral tissues of patients with Type 1 and Type 2, but mainly in the basal ganglia including caudate nucleus and putamen in the Chronic Type as already reported by Kobayashi and Suzuki in 1981. On the other hand, the finding that the Type 1 visceral organs contained unusual glycolipids rather than gangliosides was contrasted to those of Type 2 which seemed less abnormal. The unusual glycolipids included particularly fucolipid I and II consisting of glucose:galactose:N-acetylglucosamine:fucose (1:2:1:1) and (1:3:2:2), respectively. The chemical structure of oligosaccharide moiety of fucolipid I may be identical with Lacto-N-fucopentaose II or Lacto-N-fucopentaose III. The fucolipid II may be proposed to be Lacto-N-difucooctanose.

Brain Chemistry↗
PubMed1993

Carbohydrate antigen expression in murine embryonic stem cells and embryos. II. Sialylated antigens and glycolipid analysis.

A mouse embryonic stem (ES) cell line E14 and early mouse embryos were stained with a panel of 15 monoclonal antibodies recognizing sialylated or potentially sialylated carbohydrate determinants. Sialyl Le-x and sialyl Le-a were detected on the pre-implantation embryo from the 8-cell stage, and sialyl Le-a weakly on undifferentiated ES cells. Changes in cell surface carbohydrates occurred after induction of ES cell differentiation with retinoic acid (RA) and dibutyryl cAMP. Qualitative analysis of the neutral glycolipids of untreated and RA-treated ES cells using high-performance thin-layer chromatography (HPTLC) revealed few differences between the two types of culture. The major gangliosides in both cultures were indicative of an active 'a' ganglioside synthesis pathway. GD3, a precursor of the 'b' synthesis pathway, previously reported to be characteristic of embryonal carcinoma (EC) cells, was absent. RA-induced differentiation caused a shift in the spectrum to more complex gangliosides. Application of fast atom bombardment mass spectrometry (FAB-MS) to permethylated derivatives of individual bands permitted partial characterization of an unusual sialylated glycolipid and a rare ganglioside with the suggested structure of GalNAc-GD1a.

Animals↗
PubMed1993

Prosaposin deficiency: further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease.

Sphingolipid activator protein (SAP) deficiency, previously described in two sibs and shown to be caused by the absence of the common saposin precursor (prosaposin), was further characterized by biochemical lipid and enzyme studies and by ultrastructural analysis. The 20-week-old fetal sib had increased concentrations of neutral glycolipids, including mono-, di-, tri- and tetrahexosylceramide, in liver, kidney and cultured skin fibroblasts compared with the controls. Glucosylceramide and lactosylceramide were particularly elevated. The kidney of the affected fetus showed additional increases in the concentration of sulphatide, galactosylceramide and digalactosylceramide. Free ceramide was stored in the liver and kidney, and GM3 and GM2 gangliosides were elevated in the liver, but not the brain, of the fetus. Phospholipids, however, were normal in the affected fetus. In the liver biopsy of the propositus, who later died at 16 weeks of age, only a few lipids could be studied. Glucosylceramide, dihexosylceramide and ceramide were elevated in agreement with our previous study. Enzyme studies were undertaken using detergent-free liposomal substrate preparations and fibroblast extracts. The sibs' beta-glucocerebrosidase and beta-galactocerebrosidase activities were clearly reduced, but their sphingomyelinase activities were normal. The normal activity of the latter enzyme and the almost normal tissue concentration of sphingomyelin in prosaposin deficiency suggest that the prosaposin-derived SAPs are not required for sphingomyelinase activity in vivo. In keeping with the biochemical findings, skin biopsies from the sibs showed massive lysosomal storage with a vesicular and membranous ultrastructure. The function of SAPs in sphingolipid degradation and the role of SAPs for enzyme activity in vitro are discussed. In addition, the similarity in neutral glycolipid accumulations in Niemann-Pick disease type C and in prosaposin deficiency are noted. The phenotype of the prosaposin deficient sibs resembled acute neuronopathic (type 2) Gaucher disease more than Farber disease in several aspects, but their genotype was unique.

Brain Chemistry↗
PubMed1980

[Lipid-protein interactions: mechanisms of enzymatic glycolipid catabolism and their genetic restrictive escapes].

Investigations of the genetic basis of ganglioside catabolism have led to the characterisation of two types of lipid-enzyme interaction: a) Breakdown of membrane-bound glycolipids as far as catalysed by membrane-bound enzymes is regulated by the membrane itself. b) The degradation of micelle-forming glycolipids by water-soluble lysosomal enzymes is facilitated by cofactors known as activator proteins. A genetic defect in an activator protein can be just as fatal as the lack of the enzyme itself.

Animals↗
PubMed1987

Pilin independent binding of Neisseria gonorrhoeae to immobilized glycolipids.

The adherence process in pathogenesis involves the attachment of bacteria to structures present on eukaryotic cell surfaces. To investigate components necessary for this interaction, we have characterized the binding of N. gonorrhoeae to eukaryotic glycolipids immobilized on thin layer chromatograms. The gonococci specifically bind to a subset of glycolipids consisting of lactosylceramide, gangliotriosylceramide, and gangliotetraosylceramide. This binding was identified in both piliated and nonpiliated cells, and is postulated to be mediated by a nonpilin lectin-like adhesin protein.

Bacterial Adhesion↗
PubMed1990

Axonal regulation of Schwann cell glycolipid biosynthesis.

Schwann cell biosynthesis of glycolipids was studied by in vitro incorporation of [3H]galactose into neonatal rat sciatic nerves before and after endoneurial explant culture and in culture of purified Schwann cells. In neonatal nerves prior to culture, [3H]galactose was actively incorporated into galactocerebrosides (GalCe), monogalactosyl diacylglycerol (MGDG), and the sulfatides (Su). In contrast, the incorporation of [3H]galactose into MGDG, GalCe, and Su was nearly undetected in endoneurial explants after 4 days in vitro (div). Instead, there was increased 3H-labeling of glucocerebrosides (GlcCe) and its homologues, with tetrahexosylceramides (GL-4) being a major product, which continued through 8 div. This shift in glycolipid biosynthesis was further demonstrated in the purified Schwann cell cultures. These observations, together with our early findings in the permanent transection paradigm support a direct role of axons in specifying Schwann cell biosynthesis of the GalCe, MGDG, and Su and that the absence of this Schwann cell-axon interaction results in the phenotypic expression of glucocerebroside homologues by the Schwann cell.

Animals↗
PubMed1994

Expression and biological functions of sulfoglucuronyl glycolipids (SGGLs) in the nervous system--a review.

Sulfoglucuronyl carbohydrate linked to neolactotetraose reacts with HNK-1 antibody. The HNK-1 carbohydrate epitope is found in two major glycolipids, several glycoproteins and in some proteoglycans of the nervous system. Most of the HNK-1 reactive glycoproteins so far identified are neural cell adhesion molecules and/or are involved in cell-cell interactions. HNK-1 carbohydrate is highly immunogenic. Several HNK-1-like antibodies, including IgM of some patients with plasma cell abnormalities and having peripheral neuropathy, have been described. This article summarizes published work mainly on sulfoglucuronyl glycolipids, SGGLs and covers: structural requirements of the carbohydrate epitope for binding to HNK-1 and human antibodies, expression of the lipids in various neural areas, stage and region specific developmental expression in CNS and PNS, immunocytochemical localization, loss of expression in Purkinje cell abnormality murine mutations, biosynthetic regulation of expression by a single enzyme N-acetylglucosaminyl transferase, identification of receptor-like carbohydrate binding neural proteins (lectins), and perceived role of the carbohydrate in physiological functions. The latter includes role in: pathogenesis of certain peripheral neuropathies, in migration of neural crest cells, as a ligand in cell-cell adhesion/interaction and as a promoter of neurite outgrowth for motor neurons. Multiple expression of HNK-1 carbohydrate in several molecules and in various neural cell types at specific stages of nervous system development has puzzled investigators as to its specific biological function, but this may also suggest its importance in multiple systems during cell differentiation and migration processes.

Animals↗
PubMed1994

Role of basal lamina in Schwann cell glycolipid biosynthesis.

Schwann cells that are deprived of axonal contact switch their glycolipid metabolic pathway from primarily galactocerebroside (GalCe) synthesis to the formation of glucocerebroside (GlcCe) and its homologs. The removal of axonal influence has a dual effect on Schwann cell phenotype; they lose the ability to assemble both myelin and basement membrane. To determine whether a loss of basement membrane directly affects glycolipid expression, we have examined lipid biosynthesis in Schwann cells which were allowed to interact with axons of dorsal root ganglion neurons but which were deprived of the ability to assemble basal lamina. These Schwann cells resemble those from myelinating nerve in that they synthesize a large amount of galactohydroxycerebroside. This suggests that axon contact, even in the absence of basement membrane, is sufficient to induce the GalCe metabolic pathway.

Animals↗
PubMed1980

ABO(H) blood group antigens of the human erythrocyte membrane: contribution of glycoprotein and glycolipid.

Formaldehyde-fixed human erythrocytes were extracted with sodium dodecyl sulfate and with three other solvent systems, at least two of which are known to remove glycolipids quantitatively. The extracted cells possessed the ability to absorb the ABO blood group-specific antibody at about one-third the level of unextracted cells. Treatment of fresh cells with pronase also reduced the ability of the cells to absorb the antibody, further supporting the presence of ABO blood group active glycoprotein in the membrane. Trypsinization of red cells, while removing PAS-1 and partly PAS-2, did not lead to any decrease in the activity. Papainization also did not diminish the activity, although PAS-1, PAS-2, and PAS-3 were removed from the cells. Thus, both glycolipid and glycoprotein contribute to ABO antigens of erythrocytes. Also, none of the three major glycoproteins of the membrane bears this activity.

ABO Blood-Group System↗
PubMed1995

Oligodendrocyte development in PLP "pt" mutant rabbits: glycolipid antigens and PLP gene expression.

Paralytic tremor (pt), a hereditary neurological disorder of rabbits is a recessive, X-linked point mutation of the gene for proteolipid protein (PLP) biosynthesis. This mutation results in substitution of histidine by glutamine in the PLP molecule and produces severe hypomyelination. In the present study, we investigated the developmental expression of myelin-oligodendrocyte-specific glycolipid markers by means of ELISA assay. While immunoreactivity with antibodies recognising proligodendroblast (POA) antigen was unchanged, only minute amounts of the other glycolipid markers characteristic for more advanced stages of OLs maturation, such as 04 and 01 antigens, were expressed in pt brain. The degree of down-regulation was similar to that for MBP. Concomitantly, the level of in situ expression of the mutated PLP gene mRNA in glial cells of 14 day old pt brain was found to be as high as in age-matched controls. Northern blot analysis of developmental PLP gene expression showed a significant deficit of this message in pt brain, but only at more advanced developmental stages. However, aside from changes in myelin structure, no changes in glial cell number or morphology were evident by light microscopic examination of pt mutants. In contrast, electron microscopy revealed substantial abnormalities in pt oligodendrocyte cytoarchitecture, indicating functional impairment of intracellular transport and utilisation of myelin constituents. Thus, only POA expression is positively correlated with the unchanged content of OLs in pt brain, whereas decreases of 04 and 01 antigens, together with MBP immunoreactivity, are indicators of the degree of hypomyelination. Furthermore, oligodendrocyte differentiation appears to proceed normally in pt mutant brain up to the stage of PLP gene expression. Then, due to intracellular accumulation of this abnormal gene product, synthesis of PLP as well as the other myelin-specific constituents is inhibited by a "feed-back" control mechanism.

Animals↗
PubMed1992

Glycolipids of a human glioma cell line bearing receptors for platelet-derived growth factor (PDGF).

Glycolipids of U-1242 MG were characterized because results of previous studies showed that exogenous gangliosides, especially GM3, inhibit PDGF-stimulated growth of this human glioma cell line. GM3 and GM2 are the major gangliosides; both separate as doublets with thin-layer chromatography. The major neutral glycolipid is glucocerebroside with nonhydroxy fatty acids, but paragloboside, ceramide dihexoside, globoside, and asialoGM2 (GA2) are also present. The coexistence in U-1242 MG of these gangliosides and the PDGF receptor, whose mitogenic signal is modulated by GM3 in these cells, suggests a possible functional relationship among them with respect to growth regulation.

Chromatography, Thin Layer↗
PubMed1997

A polyketide-synthase-like gene is involved in the synthesis of heterocyst glycolipids in Nostoc punctiforme strain ATCC 29133.

A Tn5-1063-derived mutant of Nostoc punctiforme strain ATCC 29133 was unable to fix N2 in air although it reduced acetylene in the absence of O2. Mutant strain UCD 307 formed cells morphologically similar to heterocysts, but it failed to synthesize the characteristic heterocyst glycolipids. Sequence analysis around the site of insertion revealed an ORF of 3,159 base pairs, termed hglE. hglE putatively encodes a 115.4-kDa protein containing two domains with conserved amino acid sequences identified with acyl transferase and the chain length factor variation of beta-ketoacyl synthase active sites. These active sites are characteristic of polyketide and fatty acid synthases. The N. punctiforme strain 29133 hglE gene is transcribed only under nitrogen-limiting growth conditions. The hglE gene, or similar sequences, was found in all other heterocyst-forming cyanobacteria surveyed and was absent in unicellular Synechococcus sp. strain PCC 7942. Based on these results, we propose that the synthesis of heterocyst glycolipids follows a pathway characteristic of polyketide synthesis and involves similar large, multienzyme complexes.

Amino Acid Sequence↗
PubMed2004

Cell surface display of the chlamydial glycolipid exoantigen (GLXA) demonstrated by antibody-dependent complement-mediated cytotoxicity.

The chlamydial species are Gram-negative bacterial pathogens critical to human health. Their developmental cycle is associated with the formation and release of the broadly conserved glycolipid exoantigen (GLXA), which has been implicated in the chlamydial elementary body-host cell interaction. This study examines the potential surface display of this glycolipid by chlamydiae-infected cells and the ability of the GLXA they secrete to associate with the plasma membranes of uninfected cells, a prerequisite for exerting influence on them. The sequential incubation of anti-GLXA antibody and complement with Chlamydia trachomatis serovar K or C. pneumoniae AR-39-infected HeLa 229 or macrophage cells resulted in significant cellular cytotoxicity, which preceded the formation of mature elementary bodies. For uninfected cells, co-incubation of GLXA, purified from supernatants of either C. trachomatis or C. pneumoniae-infected HeLa 229 cells, followed by the successive addition of mouse anti-GLXA antibody and complement, yielded similar levels of cellular cytotoxicity. Thus, GLXA indeed is displayed on the surface of infected cells and, therefore, if antibody of appropriate specificity were present, this GLXA could serve to target these infected cells for elimination. Furthermore, released GLXA can associate with uninfected cells and therefore would be positioned to influence their behavior, especially in the context of infection.

Antibody Specificity↗
PubMed1991

Isolation and immunological analysis of Trypanosoma cruzi glycolipids.

A water-soluble glycolipidic fraction from Trypanosoma cruzi was isolated using a mixture of hexane and isopropanol. Analysis by SDS-polyacrylamide gel electrophoresis, after staining by silver and Sudan Black B, showed that the fraction contained one band with a relatively high mobility. Its reactivity and specificity with human chagasic sera and T. cruzi infected mouse sera or with sera from patients with several other pathologies was determined by an immunoradiometric assay. The glycolipid-based radioimmunoassay for the detection of T. cruzi antigens provided a sensitive measure of its activity. However, cross-reactivity with several sera from patients with visceral and cutaneous leishmaniasis was detected.

Animals↗