Revisão Revisado por pares

Recent Advances in Studies on Genes for Myelin Proteins

1991; Wiley; Volume: 33; Issue: 3 Linguagem: Inglês

10.1111/j.1440-169x.1991.00181.x

ISSN

1440-169X

Autores

Kazuhiro Ikenaka, Hideyuki Okano, Tomohiro Tamura, Katsuhiko Mikoshiba,

Tópico(s)

Endoplasmic Reticulum Stress and Disease

Resumo

Development, Growth & DifferentiationVolume 33, Issue 3 p. 181-192 Free Access Recent Advances in Studies on Genes for Myelin Proteins (myelin basic protein/myelin proteolipid protein/myelin associated glycoprotein/P0 protein/P2 protein) Kazuhiro Ikenaka, Kazuhiro Ikenaka Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan.Search for more papers by this authorHideyuki Okano, Hideyuki Okano Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan.Search for more papers by this authorTaka-aki Tamura, Taka-aki Tamura Division of Behavior and Neurobiology, Department of Biological Regulation, National Institute for Basic Biology, Okazaki, Aichi 444, Japan.Search for more papers by this authorKatsuhiko Mikoshiba, Corresponding Author Katsuhiko Mikoshiba Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan. Division of Behavior and Neurobiology, Department of Biological Regulation, National Institute for Basic Biology, Okazaki, Aichi 444, Japan.All correspondence should be addressed to K. MikoshibaSearch for more papers by this author Kazuhiro Ikenaka, Kazuhiro Ikenaka Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan.Search for more papers by this authorHideyuki Okano, Hideyuki Okano Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan.Search for more papers by this authorTaka-aki Tamura, Taka-aki Tamura Division of Behavior and Neurobiology, Department of Biological Regulation, National Institute for Basic Biology, Okazaki, Aichi 444, Japan.Search for more papers by this authorKatsuhiko Mikoshiba, Corresponding Author Katsuhiko Mikoshiba Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan. Division of Behavior and Neurobiology, Department of Biological Regulation, National Institute for Basic Biology, Okazaki, Aichi 444, Japan.All correspondence should be addressed to K. MikoshibaSearch for more papers by this author First published: June 1991 https://doi.org/10.1111/j.1440-169X.1991.00181.xCitations: 11AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 Akowitz, A. A., E. Barbarese, K. Scheld and J. H. Carson, 1987. Structure and expression of myelin basic protein gene sequences in the MLD mutant mouse: Reiteration and rearrangement of the MBP gene. Genetic, 116, 447– 464. 2 Amur, S. G., G. Shanker, J. M. Cochran, H. S. Ved and J. E. Pieringer, 1986. Correlation between inhibition of myelin basic protein (arginine) methyltransferase by sinefungin and lack of compact myelin formation in cultures of cerebral cells from embryonic mice. J. Neurosci. Res., 16, 367– 376. 3 Aoyama, A., T. Tamura and K. Mikoshiba, 1990. Regulation of brain-specific transcription of the mouse myelin basic protein gene: Function of the NFl-binding site in the distal promoter. Biochem. Biophys. Res. Commun., 167, 648– 653. 4 Arquint, M., J. Rober, L.-S. Chia, J. Down, D. Wilkinson, H. Bayley, P. Braun and R. Dunn, 1987. Molecular cloning and primary structure of myelin-associated glycoprotein. Proc. Natl. Acad. Sci. USA, 84, 600– 604. 5 Bartlett, W. P., P. E. Knapp and R. P. Skoff, 1988. Glial conditioned medium enables jimpy oligodendrocytes to express properties of normal oligodendrocytes; Production of myelin antigens and membranes. Glia, 1, 253– 259. 6 Barton, D. E., M. Arquint, J. Roder, R. Dunn and U. Francke 1987. The myelin-associated glycoprotein gene: Mapping to human chromosome 19 and mouse chromosome 7 and expression in quivering mice. Genomics, 1, 107– 112. 7 Beraducci, A., A. C. Peterson and A. J. Aguayo, 1981. Oligodendrocyte mosaicism in the CNS of jimpy normal mouse chimaeras. Neurology, 31, 118. 8 Boison, D. and W. Stoffel, 1989. Myelin-deficient rat; a point mutation in exon III (A→C, Thr75→Pro) of the myelin proteolipid protein causes dysmyelination and oligodendrocyte death. EMBO J., 8, 3295– 3302. 9 Campagnoni, A. T., M. J. Hunkeler and J. E. Moskaitis, 1987. Translational regulation of myelin basic protein synthesis. J. Neurosci. Res., 17, 102– 110. 10 Campagnoni, A. T. and W. B. Macklin, 1988. Cellular and molecular aspects of myelin protein gene expression. Mol. Neurobiol., 2, 41– 89. 11 Carson, J. H., M. L. Nielson and E. Barbarese, 1983. Development al regulation of myelin basic protein expression in mouse brain. Dev. Biol., 96, 485– 492. 12 Chou, J. and B. Roizman, 1985. Isomerization of Herpes Simplex Virus 1 genome: Identification of the cis-acting and recombination sites within the domain of the a sequence. Cell, 41, 803– 811. 13 Coleman, D. R., G. Kreibich, A. B. Frey and D. D. Sabatini, 1982. Synthesis and incorporation of myelin polypeptides into CNS myelin. J. Cell Biol., 95, 598– 608. 14 Cullen, B. R., P. T. Lomedico and G. Ju, 1984. Transcriptional interference in avian retroviruses-implications for the promoter insertion model of leukemogenesis. Nature, 307, 241– 245. 15 Dautigny A. M.-G, Mattei, D. Morello, P. M. Alliel, D. Pham-Dinh, D. Pham-Dinh L. Amar, D. Arnaud, D. Simon, J.-F. Mattei, J.-L. Guenet, P. Jollés and P. Avner, 1986. The structural gene coding for myelin-associated proteolipid protein is mutated in jimpy mice. Nature, 321, 867– 869. 16 de Ferra, F., H. Engh, L. Hudson, J. Kamholz, C. Puckett, S. Molineaux and R. A. Lazzarini, 1985. Alternative splicing accounts for the four forms of myelin basic protein. Cell, 43, 721– 727. 17 Diel. H.-J., M. Schaich, R.-M. Budzinski and W. Stoffel 1986. Individual exons encode the integral membrane domains of human myelin proteolipid protein. Proc. Natl. Acad. Sci. USA, 83, 9807– 9811. 18 Doolittle, D. P., N. Baumann and G. Chernoff, 1981. Allelism of two myelin deficiency mutations in the mouse. J. Hered., 72, 285. 19 Doolittle, D. P. and K. M. Schweikart, 1977. Myelin deficient, a new neurological mutant in the mouse. J. Hered., 68, 331– 332. 20 Dupouey, P., C. Jacque, J. M. Bourre, F. Cesselin, H. Priat and N. Baumann, 1979. Immunochemical studies of the basic protein in Shiverer mouse devoid of major dense line of myelin. Neurosci. Lett., 12, 113– 118. 21 D'Eustachio, P., D. R. Colman and J. L. Salzer, 1988. Chromosomal location of the mouse gene that encodes the myelin-associated glycoproteins. J. Neurochem. 50, 589– 593. 22 D'Urso, D., P. J. Brophy, S. M. Staugaitis, C. S. Gillespie, A. B. Frey, J. G. Stempak and D. R. Colman, 1990. Protein zero of peripheral nerve myelin: Biosynthesis, membrane insertion, and evidence for homotypic interaction. Neuron, 2, 449– 460. 23 Edwards, A. M., M. Arquint, P. E. Braun, J. C. Roder, F. J. Dunn, T. Pawson and J. C. Bell, 1988. Myelin-associated glycoprotein, a cell adhesion molecule of oligodendrocytes, is phosphorylated in brain. Mol. Cell. Biol., 8, 2655– 2658. 24 Edwards, A. M., P. E. Braun, J. C. Bell, 1989. Phosphorylation of myelin-associated glycoprotein in vivo and in vitro occurs only in the cytoplasmic domain of the large isoform. J. Neurochem., 52, 317– 320. 25 Emerman, M. and H. M. Temin, 1984. Genes with promoters in retrovirus vectors can be independently suppressed by an epigenetic mechanism. Cell, 39, 459– 467. 26 Fahrig, T., C. Landa, P. Pesheva, K. Kühn and M. Schachner, 1987. Characterization of binding properties of the myelin-associated glycoprotein to extracellular matrix constituents. EMBO J., 6, 2875– 2883. 27 Filbin, M. T., F. S. Walsh, B. D. Trapp, J. A. Pizzey and G. I. Tennekoon, 1990. Role of myelin P0 protein as a homophilic adhesion molecule. Nature, 344, 871– 872. 28 Folch, J. and M. Lees, 1951. Proteolipids, a new type of tissue lipoproteins. J. Biol. Chem. 191, 807– 817. 29 Frail, D. E. and P. E. Braun, 1984. Two developmentally regulated messenger RNAs differing in their coding region may exist for the myelin-associated glycoprotein. J. Biol. Chem., 259, 14857– 14862. 30 Frail, D. E. and P. E. Braun, 1985. Abnormal expression of the myelin-associated glycoprotein in the central nervous system of dysmyelinating mutant mice. J. Neurochem., 45, 1071– 1075. 31 Fujita, N., H. Ishiguro, S. Sato, T. Kurihara, R. Kuwano, K. Sakimura, Y. Takahashi and T. Miyatake, 1990. Induction of myelin-associated glycoprotein mRNA in experimental remyelination. Brain Res., 513, 152– 155. 32 Fujita, N., S. Sato, T. Kurihara, T. Inuzuka, Y. Takahashi and T. Miyatake, 1988. Developmentally regulated alternative splicing of brain myelin-associated glycoprotein mRNA is lacking in the quaking mouse. FEBS Lett. 232, 323– 327. 33 Fujita, N., S. Sato, T. Kurihara, R. Kuwano, K. Sakimura, T. Inuzuka, Y. Takahashi and T. Miyatake, 1989. cDNA cloning of mouse myelin-associated glycoprotein: A novel alternative splicing pattern. Biochem. Biophys. Res. Commun., 165, 1162– 1169. 34 Gardinier, M. V., W. B. Macklin, A. J. Diniak, P. L. Deininger, 1986. Characterization of myelin proteolipid mRNAs in normal and jimpy mice. Mol. Cell. Biol. 6, 3755– 3762. 35 Gencic, S., D. Abuelo, M. Ambler and L. D. Hudson, 1989. Pelizaeus-Merzbacher disease: An X-linked neurologic disorder of myelin metabolism with a novel mutation in the gene encoding proteolipid protein. Am. J. Hum. Genet., 45, 435– 442. 36 Hogan, E. L. and S. Greenfield, 1984. Animal models of genetic disorders of myelin. In Myelin, (ed. Morell), pp. 489– 534. Plenum Press, New York . 37 Hudson, L. D., J. A. Berndt, C. Puckett, C. A. Kozak and R. A. Lazzarini, 1987. Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse. Proc. Natl. Acad. Sci. USA, 84, 1454– 1458. 38 Hudson, L. D., C. Puckett, J. Berndt, J. Chan and S. Gencic, 1989. Mutation of the proteolipid protein gene PLP in a human X chromosome-linked myelin disorder. Proc. Nat. Acad. Sci. USA, 86, 8128– 8131. 39 Ikenaka, K., T. Furuichi, Y. Iwasaki, A. Moriguchi, H. Okano and K. Mikoshiba, 1988. Myelin proteolipid protein gene structure and its regulation of expression in normal and jimpy mutant mice. J. Mol. Biol., 199, 587– 596. 40 Inoue, Y., K. Mikoshiba, M. Aoyama, K. Inoue, T. Terashima, T. Nomura and Y. Tsukada, 1986. Alteration of the primary pattern of central myelin in a chimeric environment-study of shivererwild-type chimeras. Devel. Brain Res. 26, 239– 247. 41 Inoue, Y., R. Nakamura, K. Mikoshiba and Y. Tsukada, 1981. Fine structure of the central myelin sheath in the myelin deficient mutant shiverer mouse, with special reference to the pattern of myelin formation by oligodendroglia. Brain Res. 219, 85– 94. 42 Inoue, Y., S. Takahashi, C. Takayama, K. Inoue, H. Okano and K. Mikoshiba, 1988. Central myelin in the first hybrid mice produced by intercrossing homozygotes of shiverer and myelin-deficient mutants. Brain Res., 449, 271– 280. 43 Jacque, C., A. Privat, P. Dupouey, J. M. Bourre, T. Bird and N. Baumann, 1978. Shiverer mouse: a dysmyelinating mutant with absence of major dense line and basic protein in myelin. Proc. Eur. Soc. Neurochem., 1, 131. 44 Johnson, P. W., W. Abramow-Newerly, B. Seilheimer, R. Sadoul, M. B. Tropak, M. Arquint, R. J. Dunn, M. Schachner and J. C. Roder, 1989. Recombinant myelin-associated glycoprotein confers neural adhesion and neurite outgrowth function. Neuron, 3, 377– 385. 45 Jones, T. A., T. Bergfors, J. Sedzik and T. Unge, 1988. The three-dimensional structure of P2 myelin protein. EMBO J., 7, 1597– 1604. 46 Katsuki, M., M. Sato, M. Kimura, M. Yokoyama, K. Kobayashi and T. Nomura, 1988. Conversion of normal behavior to shiverer by myelin basic protein antisense cDNA in transgenic mice. Science, 241, 593– 595. 47 Kenney, S., V. Natarajan, D. Strike, G. Khoury and N. P. Salzman, 1984. JC virus enhancer-promoter active in human brain cells. Science, 226, 1337– 1339. 48 Kimura, M., H. Inoko, M. Katsuki, A. Ando, T. Sato, T. Hirose, H. Takashima, S. Inayama, H. Okano, K. Takamatsu, K. Mikoshiba, Y. Tsukada and I. Watanabe, 1985. Molecular genetic analysis of myelin-deficient mice: shiverer mutant mice show deletion in gene(s) coding for myelin basic protein. J. Neurochem., 44, 692– 696. 49 Kimura, M., M. Katsuki, H. Inoko, A. Ando, T. Sato, T. Hirose, S. Inayama, H. Takashima, K. Takamatsu, K. Mikoshiba, Y. Tsukada and I. Watanabe, 1986. Structure and expression of the myelin basic protein gene in mouse. In The Ninth Taniguchi Symposium on Brain Science: Molecular Genetic in Developmental Neurobiology. (ed. Y. Tsukada), pp. 125– 133. Japan Scientific Societies Press, Tokyo/VNU Science Press BV, Utrecht , The Netherlands . 50 Kimura, M., M. Sato, A. Akatsuka, S. Nozawa-Kimura, R. Takahashi, M. Yokoyama, T. Nomura and M. Katsuki, 1989. Restoration of myelin formation by a single type of myelin basic protein in transgenic shiverer mice. Proc. Natl. Acad. Sci. USA, 86, 5661– 5665. 51 Kirschner, P. and A. L. Ganser, 1980. Compact myelin exists in the absence of myelin basic protein in the shiverer mutant mouse. Nature, 283, 207. 52 Kristensson, K., N. K. Zeller, M. E. Dubois-Dalcoq, and R. A. Lazzarini, 1986. Expression of myelin basic protein gene in the developing rat brain as revealed by in situ hybridization. J. Histochem. Cytochem., 34, 467– 473. 53 Kruse, J., R. Mailhammer, H. Werneke, A. Faissner, I. Sommer, C. Goridis and M. Schachner, 1984. Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1. Nature, 311, 153– 155. 54 Lai, C., M. A. Brow, K.-A. Nave, A. B. Noronha, R. H. Quarles, F. E. Bloom, R. J. Milner and J. G. Sutcliffe, 1987a. Two forms of 1B236/myelin “associated glycoprotein, a cell adhesion molecule for postnatal neural development, are produced by alternative splicing. Proc. Natl. Acad. Sci. USA, 84, 4337– 4341. 55 Lai, C., J. B. Watson, F. E. Bloom, J. G. Sutcliffe, R. J. Milner, 1987b. Neural protein 1B236/myelin-associated glycoprotein (MAG) defines a subgroup of the immunoglobulin superfamily. Immunol. Rev. 100, 129– 151. 56 Leegwater, P. A. J., P. C. Van der Vliet, R. A. W. Rupp, J. Nowock and A. E. Sipeel, 1986. Functional homology between the sequence-specific DNA-binding proteins nuclear factor I from HeLa cells and the TGGCA protein from chicken liver. EMBO J. 5, 381– 386. 57 Lees, M. B. and S. W. Brostoff, 1984. Proteins of myelin. In Myelin (ed. P. Morell), pp. 197– 224 Plenum Press, New York . 58 Lemke, G. and R. Axel, 1985. Isolation and sequence of a cDNA encoding the major structural protein of peripheral myelin. Cell, 40, 501– 508. 59 Lemke, G. and M. Chao, 1988. Axons regulate Schwann cell expression of the major myelin and NGF receptor genes. Development, 102, 499– 504. 60 Lemke, G., E. Lamar and J. Patterson, 1988. Isolation and analysis of the gene encoding peripheral myelin protein zero. Neuron, 1, 73– 83. 61 Macklin, W. B., C. W. Campagnoni, P. L. Deininger, M. V. Gardinier, 1987. Structure and expression of the mouse myelin proteolipid protein gen. J. Neurosci. Res., 18, 383– 394. 62 Macklin, W. B., M. V. Gardinier, K. D. King and K. Kampf, 1987. An AG-GG transition at a splice site in the myelin proteolipid protein gene in jimpy mice results in the removal of an exon. FEBS Letters, 223, 417– 421. 63 Matthieu, J.-M., H. Ginalski, R. L. Friede and S. R. Cohen, 1980b. Low myelin basic protein levels and normal myelin in peripheral nerves of myelin deficient mutant mice (mld). Neuroscience, 5, 2315– 2320. 64 Matthieu, J.-M., H. Ginalski-Winkelmann and C. Jacque, 1981. Similarities and dissimilarities between two myelin deficient mutant mice, Shiverer and mld. Brain Res., 214, 219– 222. 65 Matthieu, J.-M., J.-M. Roch, F. X. Omlin, I. Rambakli, G. Almazan and P. E. Braun, 1986. Myelin instability and oligodendrocyte metabolism in myelin-deficient mutant mice. J. Cell Biol., 103, 2673– 2682. 66 Matthieu, J.-M., H. Ginalski, R. L. Friede, S. R. Cohen and D. Doolittle, 1980a. Absence of myelin basic protein and major dense line in CNS myelin of the MLD mutant mouse. Brain Res., 191, 278– 283. 67 Mikoshiba, K., E. Aoki and Y. Tsukada, 1980a. 2′,3′-cyclic nucleotide 3′-phosphohydrolase activity in the central nervous system of a myelin deficient mutant (shiverer). Brain Res., 192, 195– 204. 68 Mikoshiba, K., S. Kohsaka and Y. Tsukada, 1981. Neurochemical and morphological studies on the myelin of peripheral nervous system from shiverer mutant mice: absence of basic proteins common to central nervous system. Brain Res., 204, 455– 460. 69 Mikoshiba, K., K. Nagaike, S. Kohsaka, K. Takamatsu and Y. Tsukada, 1979. Correlation of 2′,3′-cyclic nucleotide 3′-phosphohydrolase activity and the dysmyelination in the nervous system from the shiverer mutant mice. Bull. Jap. Neurochem. Soc., 18, 200– 203. 70 Mikoshiba, K., K. Nagaike and Y. Tsukada, 1980b. Subcellular distribution and developmental change of 2′,3′-cyclic nucleotide 3′-phosphohydrolase in the central nervous system of the myelin-deficient shiverer mutant mice. J. Neurochem., 35, 465– 470. 71 Mikoshiba, K., H. Okano, Y. Inoue, M. Fujishiro, K. Takamatsu, F. Lachapelle, N. Baumann and Y. Tsukada, 1987. Immunohistochemical, biochemical and electron microscopic analysis of myelin formation in the central nervous system of myelin deficient (mld) mutant mice. Dev. Brain Res., 35, 111– 121. 72 Mikoshiba, K., K. Takamatsu and Y. Tsukada, 1983. Peripheral nervous system of shiverer mutant mice: developmental change of myelin components and immunohistochemical demonstration of the absence of MBP and presence of P2 protein. Dev. Brain Res., 7, 71– 79. 73 Mikoshiba, K., M. Yokoyama, Y. Inoue, K. Takamatsu, Y. Tsukada, 1982a. Oligodendrocyte abnormalities in shiverer mouse mutant are determined in primary chimaeras. Nature, 299, 357– 359. 74 Mikoshiba, K., M. Yokoyama, K. Takamatsu, Y. Tsukada, T. Nomura, 1982b. Chimeric analysis of the pathogenesis of dysmyelination of shiverer mutant mice. Presence of patches of MBP-positive and negative sites in white matter indicating the absence of humoral factors for dysmyelination. Dev. Neurosci., 5, 520– 524. 75 Milner, R. J., C. Lai, K.-A. Nave, D. Lenoir, J. Ogata and J. G. Sutcliffe, 1985. Nucleotide sequences of two mRNAs for rat brain myelin proteolipid protein. Cell, 42, 931– 939. 76 Milner, R. J., C. Lai, K.-A. Nave, D. Montag, L. Farber and J. G. Sutcliffe, 1990. Organization of myelin protein genes: Myelin-associated glycoprotein. In Myelination and Dysmyelination, (Eds. I. D. Duncan, R. P. Skoff and D. R. Colman), Annals N. Y. Academy of Science, in press. 77 Miura, M., T. Tamura, A. Aoyama and K. Mikoshiba, 1989. The promotor elements of the mouse myelin basic protein gene function efficiently in NG108-15 neuronal/glial cells. Gene, 75, 31– 38. 78 Molineaux, S. M., H. Engh, F. de Ferra, L. Hudson, R. A. Lazzarini, 1986. Recombination within the myelin basic protein gene created the dysmyelinating shiverer mouse mutant. Proc. Natl. Acad. Sci. USA, 83, 7542– 7546. 79 Morello, D., D. Pham-Dinh and P. Jolles, 1986. Myelin proteolipid protein (PLP and DM-20) transcripts are deleted in jimpy mutant mice. EMBO J., 5, 3489– 3493. 80 Moriguchi, A., K. Ikenaka, T. Furuichi, H. Okano, Y. Iwasaki and Mikoshiba, 1987. The fifth exon of the myelin proteolipid protein-coding gene is not utilized in the brain of jimpy mutant mice. Gene, 55, 333– 337. 81 Nagata, K., R. A. Guggenheimer, T. Enomoto, J. H. Lichy and J. Hurwitz, 1982. Adenovirus DNA replication in vitro: identification of a host factor that stimulates synthesis of the preterminal protein-dCMP complex. Proc. Natl. Acad. Sci. USA, 79, 6438– 6442. 82 Naismith, A. L., E. Hoffman-Chudzik, L.-C. Tsui and J. R. Riordan, 1985. Study of the expression of myelin proteolipid protein (lipophilin) using a cloned complementary DNA. Nucleic Acids Res., 13, 7413– 7425. 83 Narayanan, V., E. Barbosa, R. Reed and G. Tenekoon, 1988. Characterization of a cloned cDNA encoding rabbit myelin P2 protein. J. Biol. Chem., 263, 8332– 8337. 84 Nave, K.-A., C. Lai, F. E. Bloom and R. J. Milner, 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, 83, 9264– 9268. 85 Nave, K.-L., F. E. Bloom and R. J. Milner, 1987a. A single nucleotide difference in the gene for myelin proteolipid protein defines the jimpy mutation in mouse. J. Neurochem., 49, 1873– 1877. 86 Nave, K.-L., C. Lai, F. E. Bloom and R. J. Milner, 1987b. Splice site selection in the proteolipid protein (PLP) gene transcript and primary structure of the DM-20 protein of central nervous system myelin. Proc. Natl. Acad. Sci. USA, 84, 5665– 5669. 87 Kitamura, K., Newman, S. L., Campagnoni, C. W., Verdi, J. M., Mohandas, T., Handley, V. W. and Campagnoni, A. T., 1988. Expression of a novel transcript of the myelin basic protein gene. J. Neurochem., 54, 2032– 2041. 88 Newman, S. L., K. Kitamura and A. T. Campagnoni, 1987. Identification of a cDNA coding for a fifth form of myelin basic protein in mouse. Proc. Natl. Acad. Sci. USA, 84, 886– 890. 89 Nowock, J., U. Borgmeyer, W. W. Puschel, R. A. W. Rupp and A. E. Sippel, 1985. The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer. Nucl. Acids Res., 13, 2045– 2061. 90 Nowock, J. and A. E. Sippel, 1982. Specific protein-DNA interaction at four sites flanking the chicken lysozyme gene. Cell, 30, 607– 615. 91 Okano, H., K. Ikenaka and K. Mikoshiba, 1988b. Recombination within the upstream gene of duplicated myelin basic protein genes of myelin deficient (mld) mouse results in the production of antisense RNA. EMBO J., 7, 3407– 3412. 92 Okano, H., M. Miura, A. Moriguchi, K. Ikenaka, Y. Tsukada and K. Mikoshiba, 1987. Inefficient transcription of the myelin basic protein gene possibly causes hypomyelination in myelin-deficient mutant mice. J. Neurochem., 48, 470– 476. 93 Okano, H., T. Tamura, M. Miura, A. Aoyama, K. Ikenaka, M. Oshimura and K. Mikoshiba, 1988a. Gene organization and transcription of duplicated MBP genes of myelin deficient (shimld) mutant mouse. EMBO J., 7, 77– 83. 94 Poltorak, M., R. Sadoul, G. Keilhauer, C. Landa, T. Fahrig and M. Schachner, 1987. Myelin-associated glycoprotein, a member of the L2/HNK-1 family of neural cell adhesion molecules, is involved in neuron-oligodendrocyte and oligodendrocyte-oligodendrocyte interaction. J. Cell Biol., 105, 1893– 1899. 95 Popko, B., C. Puckett and L. E. Hood, 1988. A novel mutation in myelin-deficient mice results in unstable myelin basic protein gene transcripts. Neuron, 1, 221– 225. 96 Popko, B., C. Puckett, E. Lai, H. D. Shine, C. Read-head, N. Takahashi, S. W. Hunt III, R. Sidman and L. E. Hood, 1987. Myelin deficient mice: expression of myelin basic protein and generation of mice with varying levels of myelin. Cell, 48, 713– 721. 97 Privat, A., C. Jacque, J. M. Bourre, P. Dupouey, N. Baumann, 1979. Absence of the major dense line in myelin of the mutant mouse Shiverer. Neurosci. Lett., 12, 107– 112. 98 Puckett, C., L. Hudson, K. Ono, V. Friedrich, J. Benecke, M. Dubois-Dalcq and R. A. Lazzarini, 1987. Myelin-specific proteolipid protein is expressed in myelinating Schwann cells but is not incorporated into myelin sheaths. J. Neurosci. Res., 18, 511– 518. 99 Quarles, R. H., H. R. Barbarash, D. A. Figlewicz, L. J. McIntyre, 1983. Purification and partial characterization of the myelin-associated glycoprotein from adult rat brain. biochim. Biophys. Acta, 757, 140– 143. 100 Quarles, R. H., J. L. Everly and R. O. Brady, 1973. Evidence for the close association of a glycoprotein with myelin. J. Neurochem., 21, 1177– 1191. 101 Quarles, R. H., 1979. Glycoproteins in myelin and myelin-related membranes. In Complex Carbohydrates of Nervous Tissue. (Eds. R. U. Margolis and R. K. Margolis), pp. 209– 233 Plenum Publishing Corp., N. Y. 102 Quarles, R. H., 1984. Myelin-associated glycoprotein in development and disease. Dev. Neurosci., 6, 285– 303. 103 Readhead, C., B. Popko, N. Takahashi, H. D. Shine, R. A. Saavedra, R. L. Sidman and L. Hood, 1987. Expression of myelin basic protein gene in transgenic shiverer mice: correction of the dysmyelinating phenotype. Cell, 48, 703– 712. 104 Roach, A., K. Boylan, S. Horvath, S. B. Prusiner and L. E. Hood, 1983. Characterization of cloned cDNA representing rat myelin basic protein: absence of expression in brain of shiverer mutant mice. Cell, 34, 799– 806. 105 Roach, A., N. Takahashi, D. Pravtcheva, F. Ruddle and L. E. Hood, 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. 106 Roch, J.-M., M. Brown-Luedi, B. J. Cooper, J.-M. Matthieu, 1986. Mice heterozygous for the mld mutation have intermediate levels of myelin basic protein mRNA and its translation products. Mol. Brain Res., 1, 137– 144. 107 Roth, H. J., K. E. Kronquist, N. Kerlero de Rosbo, B. F. Crandall and A. T. Campagnoni, 1987. Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning. J. Neurosci. Res., 17, 321– 328. 108 Ruoslahti, E. and M. D. Piersbacher, 1987. New perspectives in cell adhesion and integrins. Science, 238, 491– 497. 109 Sacchettini, J. C., J. I. Gordon, L. J. Banaszak, 1988. The structure of crystalline Escherichia coli-derived rat intestinal fatty acid-binding protein at 2.5-A resolution. J. Biol. Chem., 263, 5815– 5819. 110 Sakamoto, Y., K. Kitamura, K. Yoshimura, T. Nishijima and K. Uyemura, 1987. Complete amino acid sequence of P0 protein in bovine peripheral nerve myelin. J. Biol. Chem., 262, 4208– 4214. 111 Salzer, J. L., W. P. Holmes and D. R. Colman, 1987. The amino acid sequences of the myelin-associated glycoproteins: Homology to the immunoglobulin gene superfamily. J. Cell Biol., 104, 957– 965. 112 Sato, S., N. Fujita, T. Kurihara, R. Kuwano, K. Sakimura, Y. Takahashi and T. Miyatake, 1989. cDNA cloning and amino acid sequence for human myelin-associated glycoprotein. Biochem. Biophys. Res. Comm., 163, 1473– 1480. 113 Schonk, D., M. Coerwinkel-driessen, I. Dalen, F. Oerlemans, B Smeets, J. Schepens, T. Hulsebos, D. Cockburn, Y. Boyd, M. Davis, W. Rettig, D. Shaw, A. Roses, H. Ropers and B. Wieringa, 1989. Definition of subchromosomal intervals around the myotonic dystrophy gene region at 19q. Genomics, 4, 384– 396. 114 Schwob, V. S., H. B. Clark, D. Agrawal and H. C. Agrawal, 1985. Electron microscopic immunocytochemical localization of myelin proteolipid protein and myelin basic protein to oligodendrocytes in rat brain during myelination. J. Neurochem., 45, 559– 571. 115 Scott, J. M., P. Wilson, J. J. Dinn and D. G. Weir, 1981. Pathogenesis of subacute combined degeneration: a result of methyl group deficiency. Lancet II, 334– 337. 116 Shen, X.-Y., S. Billigs-Gagliardi, R. L. Sidman and M. K. Wolf, 1985. Myelin deficient (shimld) mutant allele: morphological comparison with shiverer (shi) allele on a B6C3 mouse stock. Brain Res., 360, 235– 247. 117 Shiota, C., M. Miura and K. Mikoshiba, 1989. Developmental profile and differential localization of mRNAs of myelin proteins (MBP and PLP) in oligodendrocytes in the brain and in culture by in situ hybridization. Dev. Brain Res., 45, 83– 94. 118 Sidman, R. L., D. S. Conover and J. H. Carson, 1985. Shiverer gene maps near the distal end of chromosome 18 in the house mouse. Cytogent. Cell Genet., 39, 241– 245. 119 Small, J. A., G. A. Scangos, L. Cork, G. Jay and G. Khoury 1986. The early region of human papovavirus JC induces dysmyelination in transgenic mice. Cell, 46, 13– 18. 120 Small, K. H., P. R. Carnegie, R. McD. Anderson, 1981. Cycloleucine-induced vacuolation of myelin is associated with inhibition of protein methylation. Neurosci. Lett., 21, 287– 292. 121 Spagnol, G., M. Williams, J. Srinivasa, J. Golier, D. Bauer, R. V. Lebo and N. Latov, 1989. Molecular cloning of human myelin-associated glycoprotein. J. Neurosci. Res., 24, 137– 142. 122 Sternberger, N. H., R. H. Quarles, Y. Itoyama and H. F. de Webster, 1979. Myelin-associated glycoprotein demonstrated immunocytochemically in myelin and myelin-forming cells of developing rats. Proc. Natl. Acad. Sci. USA, 76, 1510– 1514. 123 Stoffyn, P. and J. Folch, 1971. On the type of linkage binding fatty acids present in brain white matter proteolipid apoprotein. Biochem. Biophys. Res. Commun., 44, 157– 161. 124 Sutcliffe, J. G., R. J. Milner, T. M. Shinnick and F. E. Bloom, 1983. Identifying the products of brain-specific genes with antibodies to chemically synthesized peptides. Cell, 33, 671– 682. 125 Takahashi, N., A. Roach, D. B. Teplow, S. B. Prusiner, L. Hood, 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. 126 Tamura, T., A. Aoyama, T. Inoue, M. Miura, H. Okano and K. Mikoshiba, 1989b. Tissue-specific in vitro transcription from the mouse myelin basic protein promoter. Mol. Cell. Biol., 9, 3122– 3126. 127 Tamura, T., T. Inoue, K. Nagata and K. Mikoshiba, 1988b. Enhancer of human polyoma JC virus contains nuclear factor I-binding sequences; analysis using mouse brain nuclear extracts. Biochem. Biophys. Res. Commun., 157, 419– 425. 128 Tamura, T., M. Miura, K. Ikenaka and K. Mikoshiba, 1988a. Analysis of transcription control elements of the mouse myelin basic protein gene in HeLa cell extracts: demonstration of a strong NFl-binding motif in the upstream region. Nucl. Acds Res., 16, 11441– 11459. 129 Tamura, T., Y. Ohya, M. Miura, A. Aoyama, T. Inoue and K. Mikoshiba, 1989a. Preparation of large amounts of transcription-competent nuclear extracts from mouse brain. Technique, 1, 33– 36. 130 Tennekoon, G., Y. Kishimoto, J. Singy, G. Nonaka, J. M. Bourre, 1980. The differentiation of oligodendrocytes in the rat optic nerve. Dev. Biol., 79, 149– 158. 131 Tosic, M., A. Roach, J.-C. de Rivaz, M. Dolivo and J.-M. Matthieu, 1990. Posttranscriptional events are responsible for low expression of myelin basic protein in myelin deficient mice: Role of natural antisense RNA. EMBO J., 9, 401– 406. 132 Trapp, B. D., S. B. Andrews, C. Cootauco and R. Quales, 1989. The myelin-associated glycoprotein is enriched in multivesicular bodies and periaxonal membranes of actively myelinating oligodendrocytes. J. Cell Biol., 109, 2417– 2426. 133 Trapp, B. D., T. Moench, M. Pulley, E. Barbosal, G. Tennekoon and J. Griffin, 1987. Spatial segregation of mRNA-encoding myelin-specific proteins. Proc. Natl. Acad. Sci. USA, 84, 7773– 7777. 134 Tropak, M. B., P. W. Johnson, R. J. Dunn and J. C. Roder, 1988. Differential splicing of MAG transcripts during CNS and PNS development. Mol. Brain Res., 4, 143– 155. 135 Uyemura, K., M. Suzuki, K. Kitamura, K. Horie, Y. Ogawa, H. Matsuyama, S. Nozaki and I. Muramatsu, 1982. Neuritogenic determinant of bovine P2 protein in peripheral nerve myelin. J. Neurochem. 39, 895– 898. 136 Varmuza, S. L. and J. R. Smiley, 1985. Signals for site-specific cleavage of HSV DNA: Maturation involves two separate cleavage events at sites distal to the recognition sequences. Cell. 41, 793– 802. 137 Weiher, H., K. Monika and P. Gruss, 1983. Multiple point mutations affecting the simian virus 40 enhancer. Science, 219, 626– 631. 138 Willard, H. F. and J. R. Riordan, 1985. Assignment of the gene for myelin proteolipid protein to the X chromosome: implications for X-linked myelin disorders. Science, 230, 940– 942. 139 Yoon, C. H. and E. P. Les, 1957. Quivering, a new first chromosome mutation in mice. J. hered., 48, 176– 180. 140 Zeller, N. K., T. N. Hehar, M. E. Dubois-Dalcq and R. A. Lazzarini, 1985. The timely expression of myelin basic protein gene in cultured rat brain oligodendrocytes is independent of continuous neuronal influences. J. Neurosci., 5, 2955– 2962. 141 Zeller, N. K., M. J. Hunkeler, A. T. Campagnoni, J. Sprague and R. A. Lazzarini, 1984. Characterization of mouse myelin basic protein messenger RNAs with a myelin basic protein cDNA clone. Proc. Natl. Acad. Sci. USA, 81, 18– 22. Citing Literature Volume33, Issue3June 1991Pages 181-192 ReferencesRelatedInformation

Referência(s)