Characteristic Constituents of Glycolipids from Frog Brain and Sciatic Nerve

Saito, Shintaro; Tamai, Yoichi

doi:10.1111/j.1471-4159.1983.tb04802.x

Cited by 18 publications

(12 citation statements)

References 32 publications

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“…Lipid Composition. Our data are in close agreement with previous investigations on myelin lipids in elasmobranch, teleost (including garfish), and amphibian (Hofteig et al, 1981;Saito and Tamai, 1983;Biirgisser et al, 1986). Overall, unlike the findings with myelin proteins, there were no apparent phylogenetic trends.…”

Section: Comparison With Previous Phylogenetic Studies: Biochemistrysupporting

confidence: 93%

Myelin Membrane Structure and Composition Correlated: A Phylogenetic Study

Kirschner

Inouye

Ganser

et al. 1989

Journal of Neurochemistry

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We have correlated myelin membrane structure with biochemical composition in the CNS and PNS of a phylogenetic series of animals, including elasmobranchs, teleosts, amphibians, and mammals. X-ray diffraction patterns were recorded from freshly dissected, unfixed tissue and used to determine the thicknesses of the liquid bilayer and the widths of the spaces between membranes at their cytoplasmic and extracellular appositions. The lipid and protein compositions of myelinated tissue from selected animals were determined by TLC and sodium dodecyl sulfate-polyacrylamide gel electrophoresis/immunoblotting, respectively. We found that (1) there were considerable differences in lipid (particularly glycolipid) composition, but no apparent phylogenetic trends; (2) the lipid composition did not seem to affect either the bilayer thickness, which was relatively constant, or the membrane separation; (3) the CNS of elasmobranch and teleost and the PNS of all four classes contained polypeptides that were recognized by antibodies against myelin P0 glycoprotein; (4) antibodies against proteolipid protein (PLP) were recognized only by amphibian and mammalian CNS; (5) wide extracellular spaces (ranging from 36 to 48 A) always correlated with the presence of P0-immunoreactive protein; (6) the narrowest extracellular spaces (approximately 31 A) were observed only in PLP-containing myelin; (7) the cytoplasmic space in PLP-containing myelin (approximately 31 A) averaged approximately 5 A less than that in P0-containing myelin; (8) even narrower cytoplasmic spaces (approximately 24 A) were measured when both P0 and 11-13-kilodalton basic protein were detected; (9) proteins immunoreactive to antibodies against myelin P2 basic protein were present in elasmobranch and teleost CNS and/or PNS, and in mammalian PNS, but not in amphibian tissues; and (10) among mammalian PNS myelins, the major difference in structure was a variation in membrane separation at the cytoplasmic apposition. These findings demonstrate which features of myelin structure have remained constant and which have become specifically altered as myelin composition changed during evolutionary development.

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Section: Comparison With Previous Phylogenetic Studies: Biochemistrysupporting

confidence: 93%

Myelin Membrane Structure and Composition Correlated: A Phylogenetic Study

Kirschner

Inouye

Ganser

et al. 1989

Journal of Neurochemistry

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“…The total lipids were extracted and glycolipids were isolated essentially as described previously (Saito and Tamai. 1983;Tamai et al, 1986).…”

Section: Lipid Analysismentioning

confidence: 99%

“…The contents ofglycolipids (Saito and Tamai, 1983), cholesterol (Allah et al, 1974), and phospholipids (Tamai et al, 1974) in a stock solution of total lipids were determined as described. respectively.…”

Section: Lipid Analysismentioning

confidence: 99%

“…Previously, it was reported that the concentration of glycolipids fluctuated during the metamorphosis of Xenopiis tadpoles and increased as the frogs matured, although the composition remained rather unchanged throughout the metamorphosis (Okamura and Kishimoto, 1983). Our previous study showed that glycosphingolipids in frog nerve tissues consist of characteristic molecular species that have not been found in higher vertebrates (Saito and Tamai, 1983).…”

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confidence: 94%

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Metamorphic Changes in Glycolipids and Myelin Proteins and 2′,3′‐Cyclic Nucleotide 3′‐Phosphohydrolase in Bullfrog and Axolotl Brains

Tamai

Kojima

Saito

et al. 1993

Journal of Neurochemistry

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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 approximately 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.

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“…Myelin lipid composition has been examined in elasmobranch, teleost (including garfish), amphibian and mammal (e.g., Hofteig et aI., 1981;Saito & Tarnai, 1983;Biirgisser et aI., 1986;Kirschner et aI., 1989). Myelin lipid composition has been examined in elasmobranch, teleost (including garfish), amphibian and mammal (e.g., Hofteig et aI., 1981;Saito & Tarnai, 1983;Biirgisser et aI., 1986;Kirschner et aI., 1989).…”

Section: -----------------------------------------------------------mentioning

confidence: 99%

Cellular and Molecular Biology of Myelination

1990

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© Springer-Verlag Berlin Heidelberg 1990 Softeover reprint of the hardcover 1st edition 1990 2131/3140-543210-Printed on acid-free-paper PREFACEThe process of myelination is one of the key events during nervous system development and represent the ultimate step of cellular differentiation by which proper neuronal function is attained. Knowledge of the biochemistry and cell biology of the myelin-forming glia has advanced rapidly in recent years. This progress was to a large extent conveyed by the concerted application of new experimental tools, including improved cell culture systems, availability of specific immunological probes and the powerful development of recombinant DNA technology and cell transfection. The multidisciplinary aspects of glial cell biology and myelination were comprehensively dicussed by leading neuroscientist from Europe, Israel, USA and Canada at a NATO Advanced Research Workshop held at Monastery Ohrbeck, near Osnabruck, August 28 -September 2,1989.The meeting concentrated on the following major topics:A detailed characterization of the different steps of oligodendroglial differentiation ranging from a bipotential precurser to the actively myelinating oligodendrocyte was given. Subsequently the regenerative potential of mature oligodendrocytes after experimental lesioning was discussed and most recent progress made in the field of glial cell transplantation was reported.Furthermore the role of specific growth factors and their receptors for glial cell proliferation and differentiation were evaluated in detail. Special emphasis was given to the involvement of proteinkinases A and C in the underlying transmembrane signalling events. New avenues of glial cell biology were pursued by means of genetically manipulated cells. In a subsequent session recent developments in the field of myelin membrane biochemistry were discussed.Another topic of major interest was related to the molecular structure and regulation of genes coding for myelin proteins. Detailed information was given as regards the structure of myelin basic protein and proteolipid protein genes as well as the chain of events underlying myelin gene expression in the peripheral nervous system. VIThe rather remote location of the meeting place and its intimate setting provided an appropriate frame for fruitful discussions and a stimulating exchange of ideas in a friendly and harmonious atmosphere. We hope that these positive experiences are reflected in the contents of this book.The papers presented at the conference are combined m the present volume.The editors are very grateful to the participants for their cooperative efforts.

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Characteristic Constituents of Glycolipids from Frog Brain and Sciatic Nerve

Cited by 18 publications

References 32 publications

Myelin Membrane Structure and Composition Correlated: A Phylogenetic Study

Myelin Membrane Structure and Composition Correlated: A Phylogenetic Study

Metamorphic Changes in Glycolipids and Myelin Proteins and 2′,3′‐Cyclic Nucleotide 3′‐Phosphohydrolase in Bullfrog and Axolotl Brains

Cellular and Molecular Biology of Myelination

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