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  • 1
    Electronic Resource
    Electronic Resource
    Metamorphic Changes in Glycolipids and Myelin Proteins and 2′,3′-Cyclic Nucleotide 3′-Phosphohydrolase in Bullfrog and Axolotl Brains (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 60 (1993), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The metamorphic changes in levels of glycolipids and myelin proteins and 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNP) in the brains of bullfrog tadpoles, adult frogs, and axolotls were investigated, with particular emphasis on myelin maturation. The concentrations of cerebroside. sulfatide, and galactosyldiacylglycerol gradually increased from the onset of prometamorphosis throughout the active metamorphic period and then greatly increased after metamorphosis was completed. The ratio of glucocerebroside to galactocerebroside increased greatly in the prometamorphic period and then rapidly decreased to the frog level during the climax period. The fatty acid compositions of cerebroside and sulfatide showed a developmental change, with 24:1 being more predominant in the later metamorphic stage. The proportion of hydroxy fatty acids increased up to the onset of the prometamorphic stage and thereafter remained constant at ∼ 50% of the total. The CNP activity remained unchanged throughout metamorphosis at 60% that in frog myelin and increased in the adult frog. The composition of tadpole myelin proteins remained constant during metamorphosis, with large basic protein being the most abundant, and in the frog, proteolipid protein and large basic protein were present in comparable amounts. The two adult forms of axolotl, i.e., the neotenous and metamorphosed forms, exhibited almost identical myelin constituents, and CNP activity in the neotenous form amounted to one-fifth that in the bullfrog. These results indicate that active biosynthesis of myelin marker components occurs as metamorphosis proceeds, but more pronounced changes of myelin components occur after metamorphosis is completed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb13412.x
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  • 2
    Electronic Resource
    Electronic Resource
    A Comparative Study of 2′,3′-Cyclic-Nucleotide 3′-Phosphodiesterase in Vertebrates: cDNA Cloning and Amino Acid Sequences for Chicken and Bullfrog Enzymes (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: In mammalian brain, two 2′,3′-cyclic-nucleotide 3′-phosphodiesterase (EC 3.1.4.37) isoforms, CNP1 and CNP2, are translated, respectively, from the two mRNAs, which have been transcribed and processed by alternative use of the two transcription start points and by differential splicing. In the present study, the cDNAs encoding chicken CNP2 and bullfrog CNP1, respectively, were isolated, and the amino acid sequences of chicken CNP2 and bullfrog CNP1 were deduced. Western blot analysis showed that chicken brain contains a major CNP2-type protein together with a minor unidentified isoform, and bullfrog brain contains only a CNP1-type protein. All available amino acid sequences of vertebrate 2′,3′-cyclic-nucleotide 3′-phosphodiesterases were aligned and compared. Three conserved motif sequences were noted: (a) an ATP-binding site near the amino terminus, (b) an isoprenylation site at the carboxyl terminus, and (c) a probable catalytic site resembling the active site of β-ketoacyl synthase (EC 2.3.1.41). The second and the third motifs are conserved also in goldfish RICH (regeneration-induced 2′,3′-cyclic-nucleotide 3′-phosphodiesterase homologue), which has been shown recently to have 2′,3′-cyclic-nucleotide 3′-phosphodiesterase activity. The third motif (probably catalytic site) was assigned for the first time in the present report.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69041335.x
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  • 3
    Electronic Resource
    Electronic Resource
    Biosynthesis of a blood group H1 antigen by α1,2-fucosyltransferase in PC12 cells (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 445-452 
    Details
    ISSN: 1573-4986
    Keywords: α1,2-fucosyltransferase ; blood group H1 ; PC12 cells ; glycosphingolipid ; disaccharide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We have examined the expression of GDP-fucose: glycosphingolipid fucosyltransferase activity in PC12 cells and PC12 sublines in relation to the neuronal differentiation induced by nerve growth factor (NGF) or dexamethasone. Transfer of fucose to paragloboside (nLc4Cer) yielded a product which was determined to be a blood group H1 antigen (Fucα1-2Galβ1-4GlcNAcβ1-3Galβ1-4Glc-Cer) by gas chromatography/mass spectrometry analysis and enzymatic hydrolysis, suggesting that PC12 cells have an α1,2-fucosyltransferase. Lactosylceramide was also fucosylated at a reduced rate. When the differentiation of PC12 cells and PC12 subline cells, PC12D and MR31, was induced by exposure to either NGF or dexamethasone, the fucosyltransferase activity for nLc4Cer was found to decrease in both cell lines, suggesting the association with cell differentiation. This is the first report of the presence of an α1,2-fucosyltransferase in cultured neuronal cell lines which catalyses thein vitro biosynthesis from nLc4Cer of a type-2 chain glycosphingolipid having the blood group H1 determinant. The disaccharides, β-lactose andN-acetyllactosamine, were also fucosylated by PC12 cell enzyme, although the specificity for the carbohydrate structure was different from that for glycosphingolipids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731477
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  • 4
    Electronic Resource
    Electronic Resource
    Three-dimensional structure of a glycosphingolipid having a novel carbohydrate linkage, Gal beta 1-4(Fuc alpha 1-3)Glc beta 1-3Gal beta, determined by theoretical calculations (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 107-113 
    Details
    ISSN: 1573-4986
    Keywords: conformation ; glycosphingolipid ; theoretical calculation ; Cer, ceramide ; Fuc, fucose ; Gal, galactose ; Glc, glucose ; Hex, hexose ; NMR, nuclear magnetic resonance ; ROESY, rotating frame Overhauser effect spectroscopy ; SEGLx, Gal beta 1-4(Fuc alpha 1-3)Glc beta 1-3Gal beta 1-Cer (a glycosphingolipid from S erinacei)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The novel glycosphingolipid, SEGLx (Gal beta 1-4(Fuc alpha 1-3)Glc beta 1-3Gal beta Cer), which was identified by us (Kawakami Y, et al. (1993) J Biochem 114: 677-83), shows a characteristic spectrum on 1H-NMR analysis, in which the anomeric proton resonances of a reducing end galactose and a glucose are split. To elucidate the structural characteristics of SEGLx, we determined its three-dimensional (3D) structure by means of computer simulation, involving such techniques as molecular mechanics (MM2), the semiempirical molecular orbital method (AM1), molecular dynamics (Amber), and computer 3D modelling. With the hypothesis that all OH group(s) of a ceramide participate in intramolecular hydrogen bonds, two kinds of stable conformers, horizontal and right-angled ones, were formed, depending on the ceramide species. The present findings suggest that the chemical species of both the long chain base and fatty acid moieties, mainly the occurrence of OH group(s), affect the chemical shifts of the anomeric proton resonances not only of the reducing terminal galactose but also the penultimate glucose through the formation of intramolecular hydrogen bonds. Computer simulation through theoretical calculation and 3D modelling was shown to be the best means of confirming the results obtained by experimental analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006908020370
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  • 5
    Electronic Resource
    Electronic Resource
    Gene Structure and Amino Acid Sequence of Latimeria chalumnae (Coelacanth) Myelin DM20: Phylogenetic Relation of the Fish (1999)
    Springer
    Neurochemical research 24 (1999), S. 867-873 
    Details
    ISSN: 1573-6903
    Keywords: Latimeria chalumnae ; coelacanth ; proteolipid protein ; DM20 ; phylogenetic relation ; lungfish
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The structure of Latimeria chalumnae (coelacanth) proteolipid protein/DM20 gene excluding exon 1 was determined, and the amino acid sequence of Latimeria DM20 corresponding to exons 2–7 was deduced. The nucleotide sequence of exon 3 suggests that only DM20 isoform is expressed in Latimeria. The structure of proteolipid protein/DM20 gene is well preserved among human, dog, mouse, and Latimeria. Southern blot analysis indicates that Latimeria DM20 gene is a single-copy gene. When the amino acid sequences of DM20 were compared among various species, Latimeria was more similar to tetrapods than other fishes including lungfish, confirming the previous finding by immunoreactivity (Waehneldt and Malotka 1989 J. Neurochem. 52:1941–1943). However, when phylogenetic trees were constructed from the DM20 sequences, lungfish was clearly the closest to tetrapods. Latimeria was situated outside of lungfish by the maximum likelihood method. The apparent similarity of Latimeria DM20 to tetrapod proteolipid protein/DM20 is explained by the slow amino acid substitution rate of Latimeria DM20.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020958014398
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