Zusammenfassung
Im Verlauf der Evolution, die zu einer ständig wachsenden Komplexität der Organismen führte, entwickelten sich eine Reihe von Mechanismen, die es ermöglichten, rasch auf Umwelteinflüsse zu reagieren und selbst zu agieren. Von diesen kommen dem zentralen und peripheren Nervensystem (ZNS bzw. PNS) die größte Bedeutung zu wegen der Möglichkeit, Informationen zwischen entfernten Nervenzellen (Neuronen) und Erfolgsorganen über Axone mit hoher Geschwindigkeit zu übertragen. Neben den Neuronen entwickelte sich die Neuroglia, ein Stützgewebe für die Neuronen, zu dem die Astroglia und die Oligodendroglia zählen. Ein entscheidender Sprung in der Evolution bestand in der Entwicklung eines elektrischen Isoliersystems der Nervenfasern in Form der Myelinscheide, die von den Oligodendrocyten gebildet wird. Die Geschwindigkeit der Erregungsleitung ist proportional dem Durchmesser des Axons im Falle der nackten Axone. In myelinisierten Axonen hingegen verläuft diese in Abhängigkeit von der Ausprägung der Myelinscheide mehr als 1OOmal schneller als in Abwesenheit des Myelins, d. h. der Querschnitt eines Axons kann für die gleiche Leistung erheblich reduziert werden. Neben der Erhöhung der Erregungsleitungsgeschwindigkeit ermöglicht die Myelinisierung die Unterbringung einer vielfachen Zahl von Axonen. Das wiederum macht die äußerst kompakte Struktur des Zentralnervensystems möglich. Wären die Axone der Bahnen des Rückenmarks z.B. nicht myelinisiert, so müßten letztere zu Erfüllung der gleichen Leistung einen Durchmesser einer mehrere hundert Jahre alten Eiche besitzen oder der Sehnerv, Nervus opticus,statt 2 bis 4 mm einen Durchmesser von 10 bis 15 cm aufweisen.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Literatur
Arquini, M., Roder, J., Chia, L. S., Down, J., Wilkinson, D., Bayley, H., Braun, P., Dunn, R. (1987) Molecular cloning and primary structure of myelin-associated glycoprotein, Proc. Natl Acad. Sci USA 84, 600–604.
Barbarese, E., Braun, P.E., Carson, F.H. (1977) Identification of pre-large and presmall basic proteins in mouse myelin and their structural relationship to large and small basic proteins, Proc. Natl. Acad. Sci USA 74, 3360–3364.
Billings-Gagliardi, S., Adcock, L.H., Wolf, M.K. (1980) Hypomyelinated mutant mice: description of jp(msd) and comparison with jp and qk on their present genetic backgrounds, Brain Res. 194, 325–328.
Boison, D., Stoffel, W. (1989) Myelin-deficient rat: a point mutation in Exon III (A → C, Thr → Pro) of the myelin proteolipid protein causes dysmyelination and oligodendrocyte death, Embo J. 8, 3295–3302.
Boué, J., Oberlé, I., Heilig, R., Mandel, J. L., Moser, A., Moser, H., Larsen, W., Dumez, Y., Boué, A. (1985) First trimester prenatal diagnosis of adrenoleukodystrophy by determination of very long chain fatty acid levels and by linkage analysis to a DNA probe, Hum. Genet 69, 272–274.
Braun, P.E. (1984) in: Myelin, ed. Morell, P (Plenum Press, New York), pp. 97–106.
Campagnoni, C. W, Carey, G.D., Campagnoni, A.T. (1978) Synthesis of myelin basic protein in the developing mouse brain. Arch. Biochem. Biophys. 190, 118–125.
Carnegie, P.R. (1971) Amino acid sequence of the encephalitogenic protein of human myelin, Biochem. J. 123, 57–67.
Carson, J. H., Nielson, M. L., Barbarese, E. (1983) Developmental regulation of myelin basic expression in mouse brain. Dev. Biol 96, 485–492.
Chen, E. J., Seeburg, P. H. (1985) Supercoil sequencing: a fast and simple method for sequencing plasmid DNA, DNA 4, 165–170.
Dautigny, A., Alliel, P. M., d’auriol, L., Pham-Dinh, D., Nussbaum, J. L., Galibert, F., Jollès, P. (1985) Molecular cloning and nucleotide sequence of a cDNA clone coding for rat brain myelin proteolipid, FEBS Letters 188, 33–36
Dautigny, A., Mattei, M. G., Morello, D., Alliel, P. M., Pham-Dinh, D., Amar, L., Arnaud, D., Simon, D., Mattei, J. F., Guenet, J. L., Jollès, P., Avner, P. (1986) The structural gene coding for myelin-associated proteolipid protein is mutated in jimpy mice, Nature 321, 867–869.
de Ferra, F., Engh, H., Hudson, L., Kamholz, J., Puckett, C, Molineaux, S., Lazzarini, R. A. (1985) Alternative splicing accounts for the four forms of myelin basic protein. Cell 43, 721–727
Drummond, R. J., Dean, G. (1980) J. Neurochem. 35, 1155–1165.
Dunkley, P.R., Carnegie, P.R. (1974) Amino acid sequence of the smaller basic protein from rat myelin, Biochem. J. 141, 243–255.
Eylar, E., Brostoff, S.W., Hashim, G., Coccam, J., Burnett, P. (1971) Basic A1 protein of the myelin membrane. The complete amino acid sequence, J. BioL Chem. 246, 5770–5784.
Folch, J., Lees, M. (1951) A simple method for the isolation and purification of total lipids from animal tissues, J. Biol Chem. 191, 807–817.
Gardiner, M. V., Macklin, W. B., Diniak, A. J., Deininger, P. L. (1986) Characterisation of myelin proteolipid mRNAs in normal and jimpy mice, Mol Cell Biol 6, 3755–3762.
Gartler, S. M., Riggs, A. D. (1983) Mammalian X chromosome inactivation, Ann. Rev. Genet 17, 155–190.
Gilbert, W. (1985) Genesis-in-pieces revisited, Science 228, 823–824.
Gubler, U., Hoffman, B.J. (1983) A simple and very efficient method for generating cDNA libraries, Gene 25, 263–269.
Heinrich, P. (1986) Guidelines for quick and simple plasmid sequencing (Boehringer Mannheim GmbH, Mannheim).
Hogan, E. L., Greenfield, S. (1984) in: Myelin, ed. Morell, P. (Plenum Press, New York).
Hudson, L. D., Bendt, J. A., Puckett, C, Kozak, C. A., Lazzarini, R. A. (1987) Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse, Proc. Natl. Acad. Sci. USA 84, 1454–1458.
Hudson, L.D., Berndt, J. A., Puckett, C., Kozak, C. A., Lazzarini, R. A. (1987) Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse, Proc. Natl. Acad. Sci. USA 84, 1454–1458.
Huxley, A. F., Stämpfli, R. (1949) Evidence for saltatory conduction in peripheral myelinated nerve fibers, J. Physiol. 108, 315.
Igarashi, N., Schaumburg, H., Power, J., Kishimoto, Y., Kolodemy, E., Suzuki, K. (1976) Fatty acid abnormality in adrenoleukodystrophy, J. Neurochem. 26, 851–860.
Kamholz, J., de Ferra, F., Puckett, C., Lazzarini, R. A. (1986) Identification of three forms of human myelin basic protein by cDNA cloning, Proc, Natl. Acad. Sci. USA 83, 4962–4966.
Kerner, A. L., Carson, J. H. (1984) Effect of the jimpy mutation on expression of myelin proteins in heterozygous and hemizygous mouse brain, J. Neurochem. 43, 1706–1715.
Koeppen, A. H., Ronca, N. A., Greenfield, E. A., Hans, M.B. (1987) Defective biosynthesis of proteolipid protein in Pelizaeus-Merzbacher disease, Ann. Neurol. 21, 159–170.
Lyon, M. F. (1961) Gene action in the X chromosome of the mouse (Mus musculus L.), Nature 190, 372–373.
Matthieu, J.M., Roach, J.M., Omlin, F.X., Rauboldt, I., Almanzan, G., Braun, P.E. (1986) Myelin instability and oligodendrocyte metabolism in myelin-deficient mutant mice, J Cell. Biol. 103, 2673–2682.
McLauchlan, J., Gaffney, D., Whitton, J. L., Clements, J. B. (1985) The consensus sequence YGTGTTYY located downstream from the AATAAA signal is required for efficient formation of mRNA 3′-termmi, Nucl. Acids Res. 13, 1347–1368.
Meier, A., MacPike, A.D. (1970) A neurological mutation (msd) of the mouse causing a deficiency of myelin synthesis, Exp. Brain Res. 10, 512–528.
Milner, R.J., Lai, C, Nave, K. A., Lenoir, D., Ogata, J., SutcliffE, J. G. (1985) Nucleotide sequences of two mRNAs for rat brain myelin proteolipid protein. Cell 42, 931–939.
Morello, D., Dautigny, A., Pham-Dinh, D., Jollès, P. (1986) Myelin proteolipid protein (PLP and DM-20) transcripts are deleted in jimpy mutant mice, EMBO J. 5, 3489–3493.
Martenson, R. E., Deisler, G. E., Kies, M. W., McKneally, S. S., Shapira, R., Kibler, R. F. (1972) Differences between the two myelin basic proteins of the rat central nervous system, Biochim. Biophys. Acta 263, 193–203.
Nave, L. A., Kai, C, Bloom, F.E., Milner, R.J. (1986) Jimpy mutant mouse: a 74 base deletion in the mRNA for myelin proteolipid protein and evidence for a primary defect in RNA splicing, Proc. Natl. Acad. Sci. USA 84, 1454–1458.
Neuhäuser, G. (1979) in: Handbook of Clinical Neurology, eds. Vinken, PJ., Bryott, C. W. (North Holland Publishing Company, Amsterdam), Vol. 42, pp. 498–500.
Norgard, M. v., Tocci, M.J., Monahan, J.J. (1980) On the cloning of eukaryotic total poly (A)+ RNA populations in Escherichia coli, J. Biol. Chem. 255, 7665–7672.
Norton, W.T., Poduslo, S. E. (1973) Myelination in rat brain: changes in myelin composition during brain myelination, J. Neurochem. 21, 759–773.
Norton, W.T., Crammer, W. (1984) in: Myelin, ed Morell, P (Plenum Press, New York) pp. 147–195.
Oberlé, I., Drayna, D., Camerino, G., White, R., Mandel, J. L. (1985) The telomeric region of the human X chromosome long arm: Presence of a highly polymorphic DNA marker and analyis of recombination frequency, Proc. Natl. Acad. Sci. USA 82, 2824–2828.
Oshiro, Y, Eylar, E. H. (1970) Allergic encephalomyelitis: preparation of the encephalitogenic basic protein from bovine brain. Arch. Biochem. Biophys. 138, 392–396
Popko, B., Puckett, C, Lai, E., Shine, H.D., Readhead, C, Takahashi, N., Hunt, S.W., Sidman, R.L., Hood, L. (1987) Myelin deficient mice: expression of myelin basic protein and generation of mice with varying levek of myelin, Cell 48, 713–721.
Ranvier, M. L. (1878) Leçons sur l’Histologie du Systeme nerveux (Librarie F. Savy, Paris).
Readhead, C, Popko, B., Takahashi, N., Shine, H.D., Saavedra, R., Sidman, R.L., Hood, L. (1987) Expression of a myelin basic protein gene in transgenic shiverer mice: correction of the dysmyeli nating phenotype. Cell 48, 703–712.
Reddy, E.P, Sandberg-Wollheim, M., Mettus, R. V., Ray, P.E., De Freitas, E., Koprowski, H. (1989) Amplification and molecular cloning of HTL V-1 sequences from DNA of multiple sclerosis patients. Science 243, 529.
Roach, A., Takahashi, N., Pravtcheva, D., Ruddie, F., Hood, L. (1985) Chromosomal mapping of mouse myelin basic protein gene and structure and transcription of the partially deleted gene in shiverer mutant mice, Cell 42, 149–155.
Ruddle, F. A. (1971) Linkage analysis in man by somatic cell genetics, Nature 242, 165–169.
Saxe, D. F., Takahashi, N., Hood, L., Simon, M. I. (1985) Localisation of the human myelin basic protein gene (MBP) to region 18q22-qter by in situ hybridisation, Cytogenet Cell. Genet 39, 246–249.
Schaich, M., Budzinski, R.-M., Stoffel, W. (1986) Cloned proteolipid protein and myelin basic protein cDNA, Biol. Chem. Hoppe-Seyler 367, 825–834.
Seitelberger, F. (1979) in Handbook of Clinical Neurology, eds. Vinken, P.J., Bryott, C. W. (North Holland Publishing Company, Amsterdam), Vol. 10, 150–202.
Sorg, B.J. A., Agrawal, D., Agrawal, H.C, Campagnoni, A.T. (1986) Expression of myelin proteolipid protein and basic protein in normal and dysmyelinating mutant mice, J. Neurochem. 46, 379–387.
Sparkes, P.S., Mohandas, T., Heiman, C, Roth, H.J. Klissak, I., Campagnoni, A.T. (1987) Assignment of the myelin basic protein to human chromosome 18q22-qter, Human Genet 75, 147–150.
Stoffel, W, Hillen, H., Giersiefen, H. (1984) Structure and molecular arrangement of proteolipid protein of central nervous system myelin, Proc. Natl. Acad. Sci USA 81, 5012–5016.
Stoner, G.L. (1984) Predicted folding of β-structure in myelin basic protein, J. Neurochem. 43, 433–447.
Streicher, R., Stoffel, W. (1989) The organisation of the human myelin basic protein, Biol. Chem. Hoppe-Seyler 370, 503–510.
Südhof, T.C, Goldstein, J. L., Brown, M. L., Russell, D. H. (1985) The LDL receptor gene: a mosaic of exons shared with different proteins, Science 228, 815–822.
Takahashi, N., Roach, A., Taplow, D.B., Prusiner, S.B., Hood, L. (1985) Cloning and characterization of the myelin basic protein gene from mouse: one gene can encode both 14 kd and 18.5 kd MBPs by alternate use of exons. Cell 42, 139–148.
Virchow, R. (1854) Ueber das ausgebreitete Vorkommen einer dem Nervenmark analogen Substanz in den tierischen Geweben, Virchows Arch. Pathol Anat 6, 562–572.
Waehneldt, T.V., Matthieu, J.M., Jeserich, G. (1986) Appearance of myelin proteins during vertebrate evolution, Neurochem. Int 9, 463–474.
Willard, H. F., Riordan, J. R. (1985) Assignment of the gene for myelin proteolipid protein to the X chromosome: implications for X-linked myelin disorders, Science 230, 940–942.
Wolfgram, F. (1966) A new proteolipid fraction of the nervous system. I. Isolation and amino acid analyses, J. Neurochem. 13, 461–470.
Yakolev, P.I., Lecours, A.-R. (1967) in: Regional development of the brain in early Life, ed. Minkowski, A. (Blackwell Scientific Pub., Oxford), pp. 3–70.
Yanagisawa, K., Duncan, I. D., Hammang, J. P., Quarles, R. H. (1986) Myelin-deficient rat: analysis of myelin proteins, J Neurochem. 47, 1901–1907.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1990 Westdeutscher Verlag GmbH Opladen
About this chapter
Cite this chapter
Stoffel, W. (1990). Essentielle makromolekulare Strukturen für die Funktion der Myelinmembran des Zentralnervensystems. In: Natur-, Ingenieur- und Wirtschaftswissenschaften. VS Verlag für Sozialwissenschaften. https://doi.org/10.1007/978-3-322-85589-3_1
Download citation
DOI: https://doi.org/10.1007/978-3-322-85589-3_1
Publisher Name: VS Verlag für Sozialwissenschaften
Print ISBN: 978-3-531-08376-6
Online ISBN: 978-3-322-85589-3
eBook Packages: Springer Book Archive