Lactosylceramides (bovine brain)
目录号 : GC44026Lactosylceramide (LacCer) is an endogenous bioactive sphingolipid.
Sample solution is provided at 25 µL, 10mM.
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- Purity: >98.00%
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Lactosylceramide (LacCer) is an endogenous bioactive sphingolipid. It is expressed on the plasma membrane of human phagocytes and mediates phagocytosis, chemotaxis, and superoxide generation. LacCer forms membrane microdomains with Lyn kinase and the αi subunits of inhibitory G protein-coupled receptors, suggesting a role in cell signaling. Elevated LacCer levels in kidney cortex homogenates and urine are directly correlated with hyperglycemia, insulin resistance, and obesity in db/db transgenic diabetic mice. It promotes recruitment of CNS-infiltrating monocytes and microglia and enhances neurodegeneration in mice with chronic experimental autoimmune encephalomyelitis (EAE), a model of multiple sclerosis (MS). Increased levels of LacCer in atherosclerotic plaques are correlated with increased levels of the pro-inflammatory cytokines IL-6, monocyte chemoattractant protein-1 (MCP-1), and macrophage inflammatory protein 1β (MIP-1β), as well as lipids and macrophages. LacCer is also upregulated during the secretory phase of the menstrual cycle. This product is a mixture of LacCers isolated from bovine brain with variable N-acyl chain lengths.
Cas No. | SDF | ||
Canonical SMILES | O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]2[C@@H](CO)O[C@@H](OC[C@@H]([C@H](O)/C=C/CCCCCCCCCCCCC)NC(CCCCCCCCCCCCCCCCC)=O)[C@H](O)[C@H]2O | ||
分子式 | C48H91NO13 (for stearoyl) | 分子量 | 890.2 |
溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
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Shipping Condition | 评估样品解决方案:配备蓝冰进行发货。所有其他可用尺寸:配备RT,或根据请求配备蓝冰。 |
制备储备液 | |||
1 mg | 5 mg | 10 mg | |
1 mM | 1.1233 mL | 5.6167 mL | 11.2334 mL |
5 mM | 0.2247 mL | 1.1233 mL | 2.2467 mL |
10 mM | 0.1123 mL | 0.5617 mL | 1.1233 mL |
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给药剂量 | mg/kg | 动物平均体重 | g | 每只动物给药体积 | ul | 动物数量 | 只 | |||
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% DMSO % % Tween 80 % saline | ||||||||||
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工作液浓度: mg/ml;
DMSO母液配制方法: mg 药物溶于 μL DMSO溶液(母液浓度 mg/mL,
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1. 首先保证母液是澄清的;
2.
一定要按照顺序依次将溶剂加入,进行下一步操作之前必须保证上一步操作得到的是澄清的溶液,可采用涡旋、超声或水浴加热等物理方法助溶。
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Gangliosides and sialosylglycoproteins in coated vesicles from bovine brain
Biochem J 1985 Feb 1;225(3):713-21.PMID:2858201DOI:10.1042/bj2250713.
The content of gangliosides and sialosylglycoproteins was investigated in a coated-vesicle-enriched fraction prepared from bovine brain by the method of Pearse [(1975) J. Mol. Biol. 97, 93-98] and further purified by g.p.c. (glass-permeation chromatography) [Pfeffer & Kelly (1981) J. Cell Biol. 91, 385-391]. From morphological criteria and from the analysis of the polypeptide pattern on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis the coated-vesicle fraction (CV-fraction) appeared more than 95% pure. The ganglioside-NeuAc (N-acetylneuraminate), glycoprotein-NeuAc, phospholipid and cholesterol contents of CV-fraction were compared with those of bovine brain synaptic plasma membranes (SPM). The cholesterol to phospholipid molar ratio was 0.47 +/- 0.07 in CV-fraction and 1.06 +/- 0.08 in SPM. The ganglioside-NeuAc and glycoprotein-NeuAc to phospholipid molar ratios were 0.047 and 0.020 respectively in CV-fraction and 0.039 and 0.016 respectively in SPM. The (Na+ + K+)-dependent ATPase activity sensitive to ouabain (in mumol of Pi/h per nmol of phospholipid) was 1.04 in CV-fraction and 0.63 in SPM; the ratio between this activity and the activity resistant to ouabain was 2 in CV-fraction and 1.4 in SPM. A t.l.c. analysis of the ganglioside fractions showed that most of the ganglioside species present in SPM were present in CV-fraction. In a rat brain coated-vesicle preparation not subjected to g.p.c., the activities [as sugar-radioactivity (c.p.m.) transferred/h per mumol of phospholipid] of the enzymes CMP-NeuAc:sialosyl-lactosylceramide (GM3) sialosyl-, UDP-Gal:N-acetylgalactosaminyl(sialosyl)lactosylceramide (GM2) galactosyl- and UDP-GalNAc:sialosyl-lactosylceramide (GM3) N-acetylgalactosaminyl-transferases, which were considered Golgi-apparatus markers, were about 19, 16 and 10% respectively of those determined in rat brain neuronal perikaryon-enriched fractions. Taken together, the results indicate that most of the major gangliosides are constituents of coated vesicles.
De-N-acetyllactotriaosylceramide as a novel cationic glycosphingolipid of bovine brain white matter: isolation and characterization
Biochemistry 2005 Jul 12;44(27):9555-62.PMID:15996110DOI:10.1021/bi0504411.
A novel cationic lipid was separated from bovine brain white matter by a series of chromatographies on carboxymethyl-Sephadex and silica gel in chloroform and methanol. Its structure was identified unambiguously as de-N-acetyllactotriaosylceramide (deNAcLc(3)Cer) by mass spectrometry and (1)H NMR. The natural occurrence of this glycolipid in white matter extract was detected by immunostaining of thin-layer chromatography with monoclonal antibody 5F5, which is directed to deNAcLc(3)Cer and recognizes the terminal beta-glucosaminyl (GlcNH(2)) residue, having a free NH(2) group. A de-N-acetylase capable of hydrolyzing the N-acetyl group of Lc(3)Cer was detected in bovine brain extract using N-[(14)C]acetyl-labeled Lc(3)Cer as a substrate. The biogenesis and possible functional significance of deNAcLc(3)Cer are discussed.
Intermembrane phospholipid fluxes catalyzed by bovine brain phospholipid exchange protein
Biochim Biophys Acta 1981 Apr 23;664(1):22-32.PMID:7236697DOI:10.1016/0005-2760(81)90025-4.
bovine brain phospholipid exchange protein catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between two populations of single bilayer vesicles. The inclusion of lactosylceramide in one of the vesicle populations and the ability to precipitate those vesicles in the presence of Ricinus communis agglutinin assures the quantitative separation of donor and acceptor vesicles following incubation with exchange protein. When both vesicle populations contain phosphatidylinositol and phosphatidylcholine and transfers are monitored in both directions, the flux of phosphatidylinositol (or phosphatidylcholine) in the forward direction equals that in the reverse. When one of the vesicle populations initially lacks phosphatidylinositol, a net unidirectional transfer of that phospholipid occurs. Concurrently, a compensatory flux of phosphatidylcholine takes place in the opposite direction, such that the bidirectional fluxes of total phospholipid are equal. A net transfer of phosphatidylcholine is also demonstrated. A mechanism of true molecular exchange between vesicles, rather than net transfer, is proposed for the bovine brain phospholipid exchange protein.
Specificity of galactosylceramidase activation by phosphatidylserine
Biochim Biophys Acta 1980 Aug 11;619(2):396-402.PMID:6773584DOI:10.1016/0005-2760(80)90087-9.
bovine brain phosphatidylserine effectively activates human brain galactosylceramidase (Hanada, E. and Suzuki, K. (1979) Biochim. Biophys. Acta 575, 410-420). Its effect on the other beta-galactosidase (Gm1-ganglioside beta-galactosidase) in human tissues, genetically distinct from galactosylceramidase, was examined. When partially purified human brain beta-galactosidase preparations, pure with respect to each other, were used as the enzyme source and when lactosylceramide, a common glycosphingolipid substrate for both beta-galactosidases, was used as the substrate, phosphatidylserine activated only hydrolysis of lactosylceramide by galactosylceramidase but not by GM1-ganglioside beta-galactosidase. With either galactosylceramide or lactosylceramide as substrate, and with phosphatidylserine as the activator, diagnosis of globoid cell leukodystrophy was possible using whole homogenates of cultured fibroblasts. Since 80-90% of lactosylceramide-cleaving activity in normal fibroblasts is due to GM1-ganglioside beta-galactosidase and since fibroblasts of globoid cell leukodystrophy patients are genetically deficient in galactosylceramidase but normal in GM1-ganglioside beta-galactosidase, these rsults are also consistent with specific activation of galactosylceramidase by phosphatidylserine.
Purification and properties of GM1 ganglioside beta-galactosidases from bovine brain
J Biochem 1986 Sep;100(3):707-15.PMID:3096983DOI:10.1093/oxfordjournals.jbchem.a121763.
Two GM1-beta-galactosidases, beta-galactosidases I, and II, have been highly purified from bovine brain by procedures including acetone and butanol treatments, and chromatographies on Con A-Sepharose, PATG-Sepharose, and Sephadex G-200. beta-Galactosidase I was purified 30,000-fold and beta-galactosidase II 19,000-fold. Both enzymes appeared to be homogeneous, as judged from the results of polyacrylamide disc gel electrophoresis. Enzyme I had a molecular weight of 600,000-700,000 and enzyme II one of 68,000, as determined on gel filtration. On sodium dodecyl sulfate polyacrylamide slab gel electrophoresis under denaturing conditions, enzyme II gave a single band with a molecular weight of 62,000, while enzyme I gave two minor bands with molecular weights of 32,000 and 20,000 in addition to the major band at 62,000. Both enzymes liberated the terminal galactose from GM1 ganglioside and lactosylceramide but not from galactosylceramide. Enzyme I showed a pH optimum of 4.0 and was heat stable, while enzyme II showed a pH optimum of 5.0 and lost 50% of its activity in 15 min at 45 degrees C. Enzyme I showed a pI of 4.2 and enzyme II one of 5.9.