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Immunocytochemical demonstration of the transport of myelin proteolipids through the Golgi apparatus

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Summary

Purified antibodies directed against myelin proteolipids were isolated by affinity chromatography of whole serum obtained from rabbits inoculated with myelin. These antibodies were specific for light, medium and dark oligodendrocytes. Astrocytes, neurons and their processes were not reactive.

Immunocytochemical investigations showed that the membranes of the Golgi complex are highly labeled by these antibodies. Diffuse cytoplasmic labeling was only observed on the light and medium oligodendrocytes and was absent from the dark types. Vesicles possessing a punctate staining were detected in the vicinity of the Golgi complex and the oligodendroglial membrane. A discontinuous labeling of the plasmalemma appears to be characteristic of the actively myelinating light and medium oligodendrocytes. In compact myelin sheaths positive immunostaining was only detected at the dense line.

The immunocytochemical localization of the myelin proteolipids in the oligodendrocytes is in accordance with previously published biochemical data.

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References

  • Agrawal HC, Hartman BK, Shearer WT, Kalmbach S, Margolis FL (1977) Purification and immunohistochemical localization of rat brain myelin proteolipid protein. J Neurochem 28:495–508

    Google Scholar 

  • Benjamins JA, Jones M, Morell P (1975) Appearance of newly synthesized protein in myelin of young rats. J Neurochem 24:1117–1122

    Google Scholar 

  • Benjamins JA, Gray M, Morell P (1976) Metabolic relationships between myelin subfractions: entry of proteins. J Neurochem 27:571–575

    Google Scholar 

  • Benjamins JA, Iwata R, Hazlett J (1978) Kinetics of entry of proteins into the myelin membrane. J Neurochem 31:1077–1085

    Google Scholar 

  • Braun PE, Pereyra PM, Greenfield S (1980) Mechanisms of assembly of myelin in mice: a new approach to the problem. In: Baumann N (ed) Neurological mutations affecting myelination, INSERM Symposium 14, Elsevier, Amsterdam, pp 413–421

    Google Scholar 

  • Burghoffer C, Costes C (1980) Separation of chloroplast lamella proteins dissolved in chloral by gel electrophoresis. Anal Biochem 108:335–342

    Google Scholar 

  • Campagnoni AT, Carey GD, Yu YT (1980) In vitro synthesis of the myelin basic proteins: subcellular site of synthesis. J Neurochem 34:677–686

    Google Scholar 

  • Colman DR, Kreibich G, Frey AB, Sabatini DD (1982) Synthesis and incorporation of myelin polypeptides into CNS myelin. J Cell Biol 95:598–608

    Google Scholar 

  • Dautigny A, Alliel PM, Nussbaum JL, Jollès P (1983) Cell-free synthesis of rat brain myelin proteolipids and their identification by immunoprecipitation. Biochem Biophys Res Commun 110:432–437

    Google Scholar 

  • Hartman BK, Agrawal HC, Kalmbach S, Shearer WT (1979) A comparative study of the immunohistochemical localization of basic protein to myelin and oligodendrocytes in rat and chicken brain. J Comp Neurol 188:273–290

    Google Scholar 

  • Hartman BK, Agrawal HC, Agrawal D, Kalmbach S (1982) Development and maturation of central nervous system myelin: comparison of immunohistochemical localization of proteolipid protein and basic protein in myelin and oligodendrocytes. Proc Natl Acad Sci USA 79:4217–4220

    Google Scholar 

  • Jollès J, Nussbaum JL, Jollès P (1983) Enzymic and chemical fragmentation of the apoprotein on the major rat brain myelin proteolipid. Sequence data. Biochim Biophys Acta 742:33–38

    Google Scholar 

  • Lim BS, Salomon JD (1975) Electron microscopic study of freshly fixed and time-delay fixed tissues. In: Proceedings of the 33rd Annual EMSA Meeting, Claitor's Pub. Div., Baton Rouge, USA, p 618

    Google Scholar 

  • Mithen F, Bunge R, Agrawal H (1980) Proteolipid protein antiserum does not affect CNS myelin in rat spinal cord culture. Brain Res 197:477–483

    Google Scholar 

  • Mori S, Leblond CP (1970) Electron microscopic identification of three classes of oligodendrocytes and a preliminary study of their proliferative activity in the corpus callosum of young rats. J Comp Neurol 139:1–30

    Google Scholar 

  • Nussbaum JL, Rouayrenc JF, Mandel P, Jollés J, Jollés P (1974) Isolation and terminal sequence determination of the major rat brain myelin proteolipid P7 apoprotein. Biochem Biophys Res Commun 57:1240–1247

    Google Scholar 

  • Roussel G, Nussbaum JL (1981) Comparative localization of Wolfgram W1 and myelin basic protein in the rat brain during ontogenesis. Histochem J 13:1029–1047

    Google Scholar 

  • Roussel G, Nussbaum JL (1982) Surface labelling of oligodendrocytes with anti-myelin serum in cell cultures from the rat brain. Light- and electron-microscopic immunocytochemical studies. Cell Tissue Res 225:581–594

    Google Scholar 

  • Roussel G, Delaunoy JP, Mandel P, Nussbaum JL (1978) Ultrastructural localization study of two Wolfgram proteins in rat brain tissue. J Neurocytol 7:155–163

    Google Scholar 

  • Schmidt MFG (1982) Acylation of proteins — a new type of modification of membrane glycoproteins. Tr Biochem Sci 7:322–324

    Google Scholar 

  • Sherman G, Folch-Pi J (1970) Rotatory dispersion and circular dichroism of brain “proteolipid” protein. J Neurochem 17:597–605

    Google Scholar 

  • Stoffel W, Hillen H, Schröder W, Deutzmann R (1982) Lipophilin (proteolipid apoprotein) of brain white matter: purification and amino acid sequence studies of the four tryptophan fragments. Hoppe-Seyler's Z Physiol Chem 363:1397–1407

    Google Scholar 

  • Yu YT, Campagnoni AT (1982) In vitro synthesis of the four mouse myelin basic proteins: evidence for the lack of a metabolic relationship. J Neurochem 39:1559–1568

    Google Scholar 

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Nussbaum, J.L., Roussel, G. Immunocytochemical demonstration of the transport of myelin proteolipids through the Golgi apparatus. Cell Tissue Res. 234, 547–559 (1983). https://doi.org/10.1007/BF00218650

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