Skip to main content
SpringerLink
Log in

Expression of myelin-specific proteins during development of normal and hypomyelinatedParalytic tremor mutant rabbits

I. Studies on the brain homogenates

  • Original Articles
  • Published:
Molecular and Chemical Neuropathology

Abstract

The paralytic tremor (pt) rabbit is an X-linked recessive mutant characterized by hypomyelination of the CNS. The onset of myelin mutants’ neurological symptoms typically occurs about the tenth postnatal day. A partial recovery is often observed; thus, the life-span of affected animals is almost normal and they can breed successfully. Mutants presenting this phenotype were chosen for our study. Because proteins can serve as excellent markers for the myelin formation process, we examined the developmental expression of several important myelin proteins (PLP/DM-20, MBP, CNP, MAG, and MOG) in bothpt mutant and control rabbit brain homogenates.

Expression of the investigated proteins occurs in rabbits as follows: CNP and MAG are already present at the early postnatal stage; PLP/DM-20 and MBP appear about the 10th postnatal day; MOG, expressed last, has been detected on the 28th postnatal day. Whereas the MBP, CNP, MAG, and MOG content is only slightly reduced in maturept mutant brain homogenates (80–90% of control values), the amount of PLP corresponds to approximately 30–40% of that present in controls. Expression of all of the examined proteins is substantially retarded in maturing brains, which leads to the conclusion that besides severe PLP deficiency, retardation of oligodendrocyte maturation is another probable feature ofpt mutation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

PLP:

Proteolipid protein

MBP:

myelin basic protein

CNP:

2′3′-cyclic nucleotide 3′-phosphohydrolase protein

MAG:

myelin associated glycoprotein

MOG:

and myelin/oligodendrocyte glycoprotein

References

  • Amiguet P., Gardinier M. V., Zanetta J.-M., and Matthieu J.-M. (1992) Purification and partial structural and functional characterization of mouse myelin/oligodendrocyte glycoprotein.J. Neurochem. 58, 1676–1682.

    Article  PubMed  CAS  Google Scholar 

  • Brady R. O., and Quarles R. H. (1988) Developmental and pathophysiological aspects of the myelin associated glycoprotein.Cell. Mol. Neurobiol. 8, 139–148.

    Article  PubMed  CAS  Google Scholar 

  • Braun P. E., Bambric L. L., Edwards A. M., and Bernier L. (1990) 2′, 3′ cyclic nucleotide 3′-phosphodiesterase has characteristic of cytoskeletal proteins. A hypothesis for its function.Ann. N.Y. Acad. Sci. 605, 55–65.

    Article  PubMed  CAS  Google Scholar 

  • Brunner C., Lassman H., Waehneldt T. V., Matthieu J.-M., and Linington C. (1989) Differential ultrastructural localization of myelin basic protein, myelin/oligodendroglial glycoprotein, and 2′, 3′-cyclic nucleotide 3′-phosphodiesterase in the CNS of adult rats.J. Neurochem. 52, 296–304.

    Article  PubMed  CAS  Google Scholar 

  • Burger D., Perruisseau, G., Simon M., and Steck A. J. (1992) Comparison of the N-linked oligosaccharide structures of the two major human myelin glycoproteins MAG and Po: Assessment and relative occurrence of oligosaccharide structure by serial lectin affinity chromatography of14C-glycolipides.J. Neurochem. 58, 845–853.

    Article  PubMed  CAS  Google Scholar 

  • Burger D., Steck A. J., Bernard C. C. A., Kerlero de Rosbo N. (1993) Human myelin oligodendrocyte glycoprotein: a new member of the L2/HNH-1 family.J. Neurochem. 61, 1822–1827.

    Article  PubMed  CAS  Google Scholar 

  • De Vellis J. (1990) Developmental and hormonal regulation of gene expression in oligodendrocytes.Ann. NY Acad. Sci. 605, 81–89.

    Article  PubMed  Google Scholar 

  • Domańska-Janik K., Wikiel H., and Strosznajder J. (1986) Brain lipids of myelin deficient rabbit during development.Neurochem. Pathol. 4, 135–145.

    Article  PubMed  Google Scholar 

  • Domańska-Janik K., Gajkowska B., de Nechaud B., and Bourre J. M. (1988) Myelin composition and activities of CNPase and Na+, K+-ATPase in hypomyelinatedpt mutant rabbitJ. Neurochem. 50, 122–130.

    Article  PubMed  Google Scholar 

  • Domanska-Janik K., de Nechaud B., Inomata M., Kawashima S., and Zalewska T. (1992) Calcium-activated neutral protease (CANP) in normal and dysmyelinating paralytic tremor mutant rabbit myelin.Mol. Chem. Neuropathol. 16, 283–288.

    Article  Google Scholar 

  • Duncan I. D. (1990) Dissection of phenotype and genotype of the X-linked myelin mutants.Ann. New York Acad. Sci. 605, 110–121.

    Article  CAS  Google Scholar 

  • Gardinier M. V., Amiguet P., Linington C., and Mathieu, J.-M. (1992) Myelin/oligodendrocyte glycoprotein cDNA analysis reveals a unique member of the immunoglobulin gene superfamily.J. Neurosci. Res. 33, 177–187.

    Article  PubMed  CAS  Google Scholar 

  • Hogan E., and Greenfield S. (1984) Animal models of genetic disorders of myelin, inMyelin (Morell P., ed.), pp. 489–534, Plenum Press, New York.

    Google Scholar 

  • Hudson L. D. (1990) Molecular genetics of X-linked mutants.Ann. N. Y. Acad. Sci. 605, 155–165.

    Article  PubMed  CAS  Google Scholar 

  • Ikenaka K., Kagawa T., and Mikoshiba K. (1992) Selective expression of DM-20, an alternatively spliced myelin proteolipid protein gene product, in developing nervous system and in nonglial cells.J. Neurochem. 58, 2248–2253.

    Article  PubMed  CAS  Google Scholar 

  • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature 227, 680–685.

    Article  PubMed  CAS  Google Scholar 

  • Linington C. and Lassmann H. (1987) Antibody responses in chronic relapsing experimental allergic encephalomyelitis: correlation of serum demyelinating activity with antibody titre to the myelin/oligodendrocyte glycoprotein (MOG).J. Neuroimmunol. 17, 61–69.

    Article  PubMed  CAS  Google Scholar 

  • Linington C., Webb M., and Woodhams P. (1984) A novel myelin-associated glycoprotein defined by a mouse monoclonal antibody.J. Neuroimmunol. 6, 387–396.

    Article  Google Scholar 

  • Lowry O. H., Rosebrough N. J., Farr A. L., and Randall R. J. (1951) Protein measurement with Folin phenol reagent.J. Biol. Chem. 193, 265–275.

    PubMed  CAS  Google Scholar 

  • Macklin W. B., Gardinier M. V., King K. D., and Kampf K. (1987) An AG-AC transition at a splice site in the myelin proteolipid protein gene in jimpy mice results in the removal of an exon.FEBS Lett. 223, 417–421.

    Article  PubMed  CAS  Google Scholar 

  • Macklin W. B., Gardinier M. V., and Obeso Z. O. (1990) Structure and expression of the mouse myelin proteolipid protein gene.Ann. NY Acad. Sci. 605, 183–193.

    Article  PubMed  CAS  Google Scholar 

  • Morell P., Quarles R. H., and Norton W. T. (1989) Formation, structure, and biochemistry of myelin, inBasic Neurochemistry: Molecular, Cellular and Medical Aspects, 4th ed. (Siegel G. J., Agranoff B. W., Albers R. W., and Molinoff P. B., eds.) pp. 109–136, Raven Press, New York.

    Google Scholar 

  • Norton W. T. (1984)Oligodendroglia. Plenum, New York.

    Google Scholar 

  • Osetowska E., and Leszowski F. (1975) Introduction to investigation of hereditary disease of the nervous system onpt rabbit model (in Polish).Neuropathol. Pol. 13, 61–70.

    CAS  Google Scholar 

  • Popot J.-L., Pham-Dinh D. and Dautigny A. (1991) Major myelin proteolipid: the 4-topology.J. Membrane Biol.,120, 233–246.

    Article  CAS  Google Scholar 

  • Pham-Dinh D. Mattei M.-G., Nussbaum J.-L., Roussel G., Pantarotti P., Roeckel N., Mather I. H., Artzt K., Lindhal K. F., and Dautigny A. (1993) Myelin/oligodendrocyte glycoprotein is a member of the immunoglobulin superfamily encoded within the major histocompatibility complex.Proc. Natl. Acad. Sci. USA 90, 7990–7994.

    Article  PubMed  CAS  Google Scholar 

  • Quarles R. H., Johnson D., Brady R. O., and Sternberger N. H. (1981) Preparation and characterization of antisera to the myelin-associated glycoprotein.Neurochem. Res. 6, 115–127.

    Article  Google Scholar 

  • Quarles R. H., Morell P., and McFarlin D. E. (1989) Disease involving myelin, inBasic Neurochemistry: Molecular, Cellular and Medical Aspects, 4th ed. (Siegel G. J., Agranoff B. W., Albers R. W., and Molinoff P. B., eds.), pp. 697–713, Raven, New York.

    Google Scholar 

  • Schachner M. (1989) Families of neural adhesion molecules, inCarbohydrate Recognition in Cellular Function. Ciba Foundation Symposium145, pp. 156–168. Wiley, Chichester.

    Chapter  Google Scholar 

  • Sypecka J., Tosic M., Dolivo M., Domańska-Janik K., and Matthieu J.-M. (1993) Developmental expression of major myelin specific proteins in hypomyelinatedpt mutant rabbitActa Neurobiol. Exp. 53, 281–284.

    CAS  Google Scholar 

  • Taraszewska A. (1984) Pathology of myelin inpt rabbit (in Polish).Neuropatol. Pol. 22, 205–218.

    PubMed  Google Scholar 

  • Taraszewska A. and Zelman I. (1985) Morphometric studies on myelin development inpt rabbit (in Polish).Neuropathol. Pol. 24, 443–454.

    Google Scholar 

  • Taraszewska A. and Zelman I. (1987) Electron microscopic study of glia inpt rabbits during myelination.Neuropathol. Pol. 25, 351–368.

    CAS  Google Scholar 

  • Timsit S. G., Bally-Cuif L., Colman D. R., and Zalc B. (1992) DM-20 mRNA is expressed during the embryonic development of the nervous system of the mouse.J. Neurochem. 58, 1172–1175.

    Article  PubMed  CAS  Google Scholar 

  • Towbin H., Staehelin T., and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proc. Natl. Acad. Sci. USA 76, 4350–4354.

    Article  PubMed  CAS  Google Scholar 

  • Williams A. F., and Barclay A. N. (1988) The immunoglobulin superfamilydomains for cell surface recognition.Annu. Rev. Immunol. 6, 381–405.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Neurochemistry, Medical Research Centre, Polish Academy of Sciences, 3 Dworkowa Str., 00784, Warsaw, Poland

    Joanna Sypecka & Krystyna Domanska-Janik

Authors
  1. Joanna Sypecka
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Krystyna Domanska-Janik
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sypecka, J., Domanska-Janik, K. Expression of myelin-specific proteins during development of normal and hypomyelinatedParalytic tremor mutant rabbits. Molecular and Chemical Neuropathology 26, 53–66 (1995). https://doi.org/10.1007/BF02814941

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02814941

Index Entries

Search

Navigation