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PubMed1990

Synthesis, spectral properties and enzymatic hydrolysis of fluorescent derivatives of cerebroside sulfate containing long-wavelength-emission probes.

Fluorescent derivatives of cerebroside sulfate (sulfogalactosyl ceramide, sulfatide) containing long-wavelength-emission fluorophores were synthesized. For this purpose a procedure was developed for preparing a cerebroside 3-sulfate derivative with an amino group on the terminal carbon atom of its fatty acyl residue. The latter compound has been used to prepare cerebroside 3-sulfate, coupled to lissamine-rhodamine, fluoresceine, eosine and NBD. The spectroscopic properties of these compounds, in different solvent systems and when incorporated into micelles of a non-ionic detergent or liposomes of a phospholipid, are reported. Incubation of these respective sulfatides with a human leukocyte preparation, resulted in the formation of the corresponding fluorescent cerebrosides.

Cerebroside-Sulfatase↗
PubMed1982

Cerebroside sulfotransferase in rat gastric mucosa.

1. Cerebroside sulfotransferase activity was demonstrated in rat gastric mucosa. This enzyme preparation catalyzes the transfer of sulfate group from 3'-phosphoadenosine-5'-phosphosulfate to added cerebroside and lactosylceramide. 2. Psychosine also serves as an acceptor for sulfate group. 3. Both hydroxy-fatty acid and non-hydroxy-fatty acid containing cerebrosides are equally sulfated. However, this enzyme is inactive toward glucosylceramide. 4. The optimum pH is around 6.0. The reaction is stimulated by the addition of 0.4-0.9% of Triton X-100. 5. The presence of 2-4 mM ATP moderately stimulates the reaction, but is inhibitory when the concentration exceeds 6 mM. 6. EDTA has no effect. 7. Both Mg2+ and Ca2+ stimulate at lower concentrations (less than 16 mM), but inhibit at higher concentrations (greater than 20 mM). Mn2+, however, is a strong inhibitor even at 8 mM concentration. 8. The apparent Km for cerebroside is 0.04 mM, while that for 3'-phosphoadenosine-5'-phosphosulfate is 0.45 microM.

Animals↗
PubMed1980

Molecular conformations of cerebrosides in bilayers determined by Raman spectroscopy.

Vibrational Raman spectra of the solid and gel phases of bovine brain cerebrosides and the component fractions, kerasin and phrenosin, provide conformational information for these glycosphingolipids in bilayer systems. The carbon-carbon stretching mode profiles (1,150-1,000 cm-1) indicate that at 22 degrees C the alkyl chains assume an almost all-trans arrangement. These spectral data, combined with those from the C-H stretching region (3,050-2,800 cm-1), show that phrenosin forms the most highly ordered polycrystalline solid and kerasin the most ordered gel phase. The conformation of the unsaturated, 24-carbon acyl chains is monitored independently by a skeletal stretching mode at 1,112 cm-1. The alkyl chains in the kerasin and phrenosin gels are sufficiently extended to allow interdigitation of the 24-carbon acyl chains across the midplane of the bilayer. The amide I vibrational mode occurs at a lower frequency in solid phrenosin than kerasin, a shift consistent with stronger hydrogen bounding. This band is broadened and shifted to higher frequencies, however, in the phrenosin gel phase. In both the solid and gel phases natural cerebroside exhibits a composite amide I mode. The disruptive effects on cerebroside chain packing and headgroup orientation arising from mixing with dimyristoyl phosphatidylcholine are examined. Vibrational data for cerebroside are also compared to those for ceramide, sphingosine, and distearoyl phosphatidylcholine structures. Spectral interpretations are discussed in terms of calorimetric and X-ray structural data.

Animals↗
PubMed1986

Factors affecting surface expression of glycolipids: influence of lipid environment and ceramide composition on antibody recognition of cerebroside sulfate in liposomes.

The reactivity of the acidic glycolipid cerebroside sulfate (CBS) with antibody was studied as a function of its lipid environment in vesicles and of its ceramide composition. The lipid environment was varied by using phosphatidylcholine of varying chain length with cholesterol in a phosphatidylcholine:cholesterol:cerebroside sulfate molar ratio to glycolipid of 1:0.75:0.1. The ceramide structure of CBS was varied by using synthetic forms containing palmitic acid, lignoceric acid, or the corresponding alpha-hydroxy fatty acids. Reactivity with antibody was determined by measuring complement-mediated lysis of the vesicles containing a spin-label marker, tempocholine chloride. The data were analyzed by a theoretical model which gives relative values for the dissociation constant and concentration of antibodies within the antiserum which are able to bind to the glycolipid. If the phosphatidylcholine chain length was increased, increasing the bilayer thickness, only a small population of high-affinity antibodies were able to bind to cerebroside sulfate, suggesting decreased surface exposure of the glycosyl head group. A larger population of lower affinity antibodies were able to bind to it in a shorter chain length phosphatidylcholine environment. However, if the chain length of the cerebroside sulfate was increased, it could be recognized by more antibodies of lower affinity than the short chain length form, suggesting that an increase in chain length of the glycolipid increased surface exposure. Hydroxylation of the fatty acid inhibited antibody binding; only a smaller population of higher affinity antibodies was able to bind to the hydroxy fatty acid forms.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1996

New bioactive cerebrosides from Arisaema amurense.

From Arisaema amurense, four new cerebrosides were isolated along with a known cerebroside. The new cerebrosides were characterized as 1-O-beta-D-glucopyranosyl- (2S,3R,4E,8Z)-2-[(2(R)- hydroxyicosanoyl)amido]-4,8-octadecadiene-1,3-diol (1), 1-O-beta-D- glucopyranosyl-(2S,3R,4E,8Z)- 2-[(2-hydroxyoctadecanoyl)amido]-4,8-octadecadiene-1,3-diol (2), 1-O-beta-D- glucopyranosyl- (2S,3R,4E,8E)-2-[(2-hydroxyicosanoyl)amido]-4,8-oct adecadiene-1,3-diol (4), and 1-O-beta-D- glucopyranosyl-(2S,3R,4E,8E)-2-[(2-hydroxyoctadecanoyl )amido]-4,8- octadecadiene-1,3-diol (5), respectively. These cerebrosides displayed significant antihepatotoxic activity.

Animals↗
PubMed2002

Existence of cerebroside in Saccharomyces kluyveri and its related species.

Sphingolipids are ubiquitous compounds derived from ceramide that consist of a sphingoid long-chain base with a 2-amino group amide linked to fatty acid and are present in the membranes of many organisms. As a principal sphingolipid, Saccharomyces cerevisiae contains a free ceramide and its inositol-phosphorylated derivatives (acidic types) but not a neutral glycosylated ceramide, glucosylceramide (cerebroside), which usually appears in eukaryotic cells. When 31 strains accepted in the genera Saccharomyces, Torulaspora, Zygosaccharomyces, and Kluyveromyces were analyzed for sphingolipids, cerebrosides were found in S. kluyveri, Z. cidri, Z. fermentati, K. lactis, K. thermotolerans, and K. waltii. The cerebrosides of S. kluyveri and K. lactis included 9-methyl 4-trans, 8-trans-sphingadienine and its putative metabolic intermediates. A unique characteristic of S. kluyveri was the presence of a trihydroxy sphingoid base, which rarely occurs in fungal cerebrosides. A polymerase chain reaction with primers targeted to the glucosylceramide synthase gene of other microorganisms amplified the fragments of the expected size from S. kluyveri and K. lactis and further extended to the adjacent regions. The presumed protein of S. kluyveri had 54.4% similarity to that of K. lactis, higher than the glucosylceramide synthases from Candida albicans, Pichia pastoris, and other organisms. From these observations, the divergence of S. kluyveri from the lineage of K. lactis in their evolution is discussed.

Amino Acid Sequence↗
PubMed1974

Cerebroside antibody inhibits sulfatide synthesis and myelination and demyelinates in cord tissue cultures.

Antiserum to cerebroside was prepared in rabbits by injection of cerebroside together with bovine serum albumin in complete Freund's adjuvant. When applied to cultures of embryo mouse spinal cord at explantation, this antiserum inhibited sulfatide synthesis and myelination; when applied to myelinated cultures it inhibited sulfatide synthesis and produced demyelination. Complement fixation assays also show antibody to cerebroside in serums from rabbits with experimental allergic encephalomyelitis induced by injection of whole white matter. Absorption of such serum with cerebroside abolishes the inhibiting and demyelinating activities.

Animals↗
PubMed1990

Heterosis for brain cerebroside synthesis in mice.

The (C57BL/6J X DBA/2J) F1 or B6D2F1 hybrid mice are known to exhibit a transitory hypermyelinating activity compared with their parental strains B6 and D2. These mice exhibit an elevated accumulation of cerebrosides in the brain which can be explained by an increase in their synthesis. Analysis of the two major cerebroside species indicated that the elevated content of total cerebrosides in the cerebellum and cerebrum of B6D2F1, as well as D2B6F1 hybrids, reflected an increased accumulation of the hydroxylated species. The UDP-galactose:ceramide galactosyltransferase (CgalT) activities in B6, D2 and hybrid mice were studied using as substrates alpha-hydroxy fatty acid (HFA)-containing ceramides or normal fatty acid (NFA)-containing ceramides (HFA- and NFA-CgalT activities, respectively). Both CgalT activities were found to be about 2 times higher in the cerebellum than in the cerebrum for all the strains studied. Before 20 days of age, the HFA-CgalT activities in B6D2F1, D2B6F1 and D2 mice were higher than in B6. However, at 20 days, there was no difference between B6 and D2 while the HFA-CgalT activity in the hybrids remained about 20% higher than in the parental strains. In contrast, no strain differences could be detected for the NFA-CgalT activity at all ages. The data suggest that the increased synthesis of brain cerebrosides in the B6D2F1 and D2B6F1 strains of mice could be largely accounted for by an increased HFA-CgalT activity.

Animals↗
PubMed1976

The activator of cerebroside sulphatase. Lysosomal localization.

1) An activator protein necessary for the enzymic hydrolysis of cerebroside sulphate could be partially purified from unfractionated rat liver. This activator, which is similar to that of human origin, proved to be a heat-stable, non-dialyzable, low molecular weight protein with an isoelectric point of 4.1. Its activity could be destroyed by pronase. 2) For elucidation of the subcellular localization of the activator, rat liver was fractionated by differential centrifugation. The intracellular distribution of the cerebroside sulphatase activator was compared to the distribution patterns of marker enzymes for different cell organelles and found to coincide with the lysosomal arylsulphatase, thus indicating a lysosomal localization. 3) This was confirmed using highly purified secondary, i.e. iron-loaded, lysosomes. After disruption by osmotic shock, these organelles hydrolyzed cerebroside sulphate when incubations were performed under physiological conditions with endogenous as well as exogenous sulphatase A as enzyme. 4) After subfractionation of the disrupted secondary lysosomes into membrane and lysosol fractions by high speed centrifugation, it was found that the activator protein was exclusively associated with the lysosol, whereas the acid hydrolases were distributed differently between the two fractions. 5) The lysosol was further fractionated by semi-preparative electrophoresis on polyacrylamide gels. Two protein fractions were obtained: a high molecular weight fraction, containing the activator-free acid hydrolases, and a low molecular weight fraction, containing the enzyme-free activator of cerebroside sulphatase. 6) The significance of these findings for the hydrolysis of sphingolipids in the lysosomes is discussed.

Animals↗
PubMed1980

Effect of nicotinic acid on the concentration of cerebroside in rat brain.

The effect of nicotinic acid on the changes of rat brain cerebroside levels has been studied during brain development. There is a gradual increase in the concentration of cerebroside from 12 days of age to adult level at approximately 47 days of age. However, the concentration of cerebroside was significantly lower in brain of rat fed the nicotinic acid-deficient diet. Therefore, nicotinic acid may play an important role in cerebroside synthesis in brain of developing rat.

Age Factors↗
PubMed1972

A method for fractionation of cerebrosides into classes with different fatty acid compositions.

A method is described for the separation of beef brain cerebrosides into three fractions containing different classes of fatty acids: nonhydroxy (I), unsaturated nonhydroxy (II), and hydroxy fatty acid cerebrosides (III). The procedure consists of benzoylation of either crude or purified cerebrosides, followed by column chromatographic separation of benzoylated derivatives containing nonhydroxy acids from those containing hydroxy fatty acids. The benzoyl groups are removed by sodium methoxide-catalyzed transesterification; from the reaction mixtures, fractions I and III precipitate. The fraction II present in mother liquor of I was shown to contain mainly short-chain and unsaturated nonhydroxy fatty acid cerebrosides. The fatty acid composition of each fraction was obtained by gas-liquid chromatography.

Acylation↗
PubMed1968

Changes in the fatty acid composition of cerebrosides and sulfatides of human nervous tissue with age.

Sphingogalactolipids (galactocerebrosides and sulfatides) have been isolated in almost quantitative yields from normal human nervous tissue (mostly brain) at different ages and their fatty acid compositions have been determined by gas-liquid chromatography. The ratio of hydroxy acids to normal acids increased slightly during myelination and then remained rather constant; in adults the ratio for cerebrosides was about 2, and for sulfatides, 0.6-0.8. In adult nervous tissue the two predominant fatty acids of cerebrosides and sulfatides were the C(24) monounsaturated and 2-hydroxy saturated acids. The infant brain galactolipids had (compared with child and adult) a lower percentage of C(22)-C(26) fatty acids and a much lower percentage of monoenoic acids, both of normal and hydroxy acids. Low activities of fatty acid elongation and desaturation systems during myelination are inferred. Fatty acid changes with age were the same for cerebrosides and sulfatides but occurred later in the sulfatides, which supports the hypothesis that the cerebrosides are precursors of the sulfatides. The adult pattern of fatty acid composition with regard to degree of unsaturation and total percentage of C(22)-C(26) acids was reached as early as at 2 yr of age, but the percentage of odd-numbered (C(23) and C(25)) fatty acids continued to increase up to the age of 10-15 yr. The fatty acid composition of the galactolipids of peripheral nerves differed mainly in its lower percentages of C(25) and C(26) acids and higher percentages of C(22) and C(16) acids. This composition is thus intermediate between those of brain and of extraneural organs.

Adolescent↗
PubMedDate not supplied

[Cerebrosides and sulfocerebrosides in the brain of the macaque Macaca fascicularis].

The content of cerebrosides and sulfocerebrosides has been determined in the whole brain, in the gray and white matter of the cerebral hemispheres of the macaque. Fatty acid composition and long chain bases of these sphingolipids in the whole brain were also investigated. The species studied belongs to the order of higher primates, the family of lower Old World monkeys. In the whole brain, rather high content of both sphingolipids was found, the cerebral white matter being the richer. Cerebrosides with hydroxy acids predominate in the whole brain, in the white and gray matter. Cerebrosides of the whole brain contain mainly palmitic and stearic acids and relatively small amounts of C24 normal fatty acids. In sulfocerebrosides, the proportion of palmitic and stearic acids is lower and that of C24 normal fatty acids--larger, as compared to cerebrosides. In both sphingolipids, the content of saturated hydroxy acids, mainly cerebronic acid, is rather high. Among the long chain bases, only sphingenine and sphinganine were detected the former being predominant. Sphingolipids from the brain of the macaque were compared to these from the human brain.

Animals↗
PubMed1980

Human brain cerebroside beta-galactosidase: deficiency of transgalactosidic activity in Krabbe's disease.

Under experimental conditions optimal for the assay of D-galactosyl-N-acylsphingosine galactohydrolase (EC 3.2.1.46) activity, homogenates of neurologically normal human brain tissue could transfer galactose from galactosyl ceramide (gal-cer), lactosyl ceramide (lac-cer), 4-methylumbelliferyl-beta-galactoside (4-MU-gal), or p-nitrophenyl-beta-galactoside (PNP-gal) to [1-14C]oleoyl sphingosine, but homogenates of brain tissue from patients with Krabbe's disease lacked this ability. The rate of hydrolysis of ganglioside GM1 and, to a lesser extent, of PNP-gal by homogenates of Krabbe's brain tissue was also decreased. Activity of PNP-beta-galactosidase in normal brain tissue, like that of cerebroside beta-galactosidase from the same source, was considerably more heat-stable than the activity of either 4-MU-beta-galactosidase or the predominant GM1 beta-D-galactosidase (EC 3.2.1.23). Lac-cer and GM1, as well as 4-MU-gal and PNP-gal, were competitive inhibitors of human-brain cerebroside beta-galactosidase. These findings confirm the ability of mammalian cerebroside beta-galactosidase to catalyze a transgalactosylation reaction and provide additional information on the substrate specificity of human brain cerebroside beta-galactosidase.

Adolescent↗
PubMed1999

Structure and properties of totally synthetic galacto- and gluco-cerebrosides.

The structural and thermal properties of aqueous dispersions of the totally synthetic cerebrosides, D-erythro-N-palmitoyl galactosyl- and glucosyl-C18-sphingosine (C16:0-GalCer and C16:0-GluCer, respectively) have been studied using differential scanning calorimetry (DSC) and X-ray diffraction. Over the temperature range 0-100 degrees C, both C16:0-GalCer and C16:0-GluCer show complex thermal transitions characteristic of polymorphic behavior of exclusively bilayer phases. On heating, hydrated C16:0-GalCer undergoes an exothermic bilayer-bilayer transition at 59 degrees C to produce a stable bilayer crystal form. X-ray diffraction at 70 degrees C reveals a bilayer structure with an ordered hydrocarbon chain-packing arrangement. This ordered bilayer phase undergoes an endothermic chain-melting transition at 85 degrees C to the bilayer liquid crystalline state. Similar behavior is exhibited by hydrated C16:0-GluCer which undergoes the exothermic transition at 49 degrees C and a chain-melting transition at 87 degrees C. The exothermic transitions observed on heating hydrated C16:0-GalCer and C16:0-GluCer are irreversible and dependent upon previous chain melting, prior cooling rate, and time of incubation at low temperatures. Thus, the structure and properties of totally synthetic C16:0-GalCer and C16:0-GluCer with identical sphingosine (C18:1) and fatty acid (C16:0) chains are quite similar, suggesting that the precise isomeric structure of the linked sugar plays only a minor role in regulating the properties of hydrated cerebrosides. Further, these studies indicate that the complex thermal behavior and bilayer phase formation exhibited by these single-sugar cerebrosides are intrinsic properties and not due to the heterogeneity of the sphingosine base found in natural and partially synthetic cerebrosides.

Calorimetry, Differential Scanning↗
PubMed1978

Evidence for the involvement of cerebroside sulfate in opiate receptor binding: Studies with Azure A and jimpy mutant mice.

The role of cerebroside sulfate in opiate action and binding was studied by examining the effect of decreasing the availability of the glycolipid in vivo on morphine analgetic activity and receptor affinity. Available cerebroside sites were decreased either by injecting Azure A at a dose with selective high affinity for sulfo-lipids, or by using "jimpy" mice, a genetic leukodystropic mutant mouse with a deficiency in brain sulfatides. Injections of Azure A (4.4 MG/KG) intracerebroventricularly produced a 2-fold increase in the AD50 of morphine (tail-flick test) within 2 hr. The genetic mutation also resulted in a decreased sensitivity to morphine; the morphine AD50 was 6- to 11-fold higher in jimpy mice than in their normal littermates. Azure A produced a dose-dependent inhibition of opiate binding to synaptosomal plasma membranes. There was 85% inhibition of [3H]morphine binding with 0.2 micrometer Azure A, and 40% inhibition of [3H]naloxone binding with 5 micrometer Azure A. The inhibition of morphine binding was competitive and was demonstrated to be different from that elicited by Na+. Synaptic membranes from jimpy mice exhibited a decrease in number of binding sites for morphine. Binding of Azure A to cerebroside sulfate, associated with or in the proximity of the receptor sites, was suggested by the fact that in the presence of 0.2 micrometer Azure A, no inhibition of [3H]morphine binding to synaptosomal plasma membranes of jimpy mice could be demonstrated whereas 31% inh-bition was observed in membranes from control littermates. Based on the findings, it is concluded that cerebroside sulfate strategically located may have a role in binding morphine and mediating its effects.

Animals↗
PubMed2000

Disulfide connectivity in cerebroside sulfate activator is not necessary for biological activity or alpha-helical content but is necessary for trypsin resistance and strong ligand binding.

Cerebroside sulfate activator (CSAct) protein is exceptionally resistant to heat denaturation and proteolytic digestion. Although water soluble the protein binds membrane-associated lipids. Its biological role is thought to be to transfer certain lipids between membranes and to facilitate their catabolism in the lysosomes. An example of the latter is the removal of the sulfate group from cerebroside sulfate by arylsulfatase A. The mechanism of lipid sequestration from membranes and presentation of the lipid-protein complex to catabolic enzymes is a crucial aspect of the function of this protein. The widespread occurrence of the protein class of which CSAct is one of the best known members underscores the significance of this protein. The preparation, purification and chemical and biological properties of a stable disulfide blocked derivative of CSAct is described. The pyridoethylated protein was susceptible to tryptic attack and devoid of a significant population of solvent-protected exchange resistant protons. It apparantly formed a CS complex. However, unlike the complex with the native protein, this was not sufficiently stable to remain intact during size exclusion chromatography. The disulfide-blocked protein had a similar CD spectrum as native protein, indicating similar alpha-helical content. Unexpectedly, the activities of disulfide-blocked protein in the arylsulfatse A catalyzed sulfate hydrolysis from cerebroside sulfate were substantial. Hitherto, it had been assumed that the disulfide connectivities were essential for the protein to maintain a correctly folded configuration to bind lipid ligands and potentiate their hydrolysis. Some revision of our thoughts on the importance of the disulfide connectivities in the structure and function of the protein are necessary.

Amino Acid Sequence↗
PubMed1978

The activator of cerebroside-sulphatase. A model of the activation.

The activator of cereboroside-sulphatase (cerebroside-3-sulphate-3-sulphohydrolase, EC 3.1.6.8) is necessary for the enzymic hydrolysis of sulphatides (cerebroside sulphates) at ionic concentrations in the physiological range. The pH optimum of the reaction is 4.5--4.8. Under similar incubation conditions, a complex is formed between activator and sulphatides which is partially inhibited, due to competitive binding in the presence of cerebrosides of phosphatidylserine. Inhibition depends upon the concentration of the lipids and is of the same order of magnitude as the inhibition (by these lipids) of enzymic sulphatide hydrolysis in the presence of activator. Complex formation between activator and sulphatides is reversible since the complex dissociates partially when certain concentrations of phosphatidylserine are added. Moreover, the rate of sulphatide hydrolysis increases with the concentration of the activator.sulphatide complex in the reaction mixture. This indicates that the activator.sulphatide complex is the substrate for the enzyme and a model for this activation is presented.

Cerebroside-Sulfatase↗