Abstract
A variety of observations call attention to the potential significance of CNP in CNS myelination1–6. Although this protein is not unique to oligodendrocytes, these cells are the only ones to express it in the CNS. CNP is the earliest of all known myelination-related proteins to appear developmentally in oligodendrocytes; it accumulates in the cytoplasm-containing compartments of the myelin sheath, and is absent from compact lamellae4,7. Despite several interesting primary structural domains that are shared by other proteins, including several that are involved in signal transduction2,3,5 and an isoprenylated domain6, CNP is not assignable to any family of known proteins by virtue of overall sequence homology. This and the catalytic potential for hydrolysis of 2′-3′-cyclic nucleotides to yield 2′-nucleotides (a reaction of no known physiological significance for events in the cytosol) have left the problem of a functional role unresolved.
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References
U.S. Vogel and RJ. Thompson, Molecular structure, localization and possible functions of the myelin associated enzyme 2′, 3′-cyclic nucleotide 3′-phosphodiesterase, J. Neurochem. 50: 1667–1677 (1988).
R.J. Thompson, 2′, 3′-cyclic nucleotide 3′-phosphodiesterase and signal transduction in CNS myelin, Biochem. Soc. Trans. 20: 621–626 (1992).
J.J. Sprinkle, 2′, 3′-cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system, CRC Crit. Rev. Neurobiol. 4: 235–301 (1989).
P.E. Braun, D. Sandillon, A. Edwards, J.M. Matthieu, and A. Privat, Immunocytochemical localization by electron microscopy of 2′, 3′-cyclic nucleotide 3-phosphodiesterase in developing oligodendrocytes of normal and mutant brain, J. Neurosci. 8: 3057–3066 (1988).
P.E. Braun, L.L. Bambrick, A.M. Edwards, and L. Berhier, 2′, 3′-cyclic nucleotide 3′-phosphodiesterase has characteristics of cytoskeletal proteins;a hypothesis for its function, Annals N.Y. Acad. Sci. 605: 55–65 (1990).
P.E. Braun, D. De Angelis, W.W. Shtybel, and L. Bernier, Isoprenoid modification permits 2′, 3′-cyclic nucleotide 3′-phosphodiesterase to bind to membranes, J. Neurossci Res. 30: 540–544 (1991).
B.D. Trapp, L. Bernier, S.B. Andrews, and D. Colman, Cellular and subcellular distribution of CNP and its mRNA in the rat CNS, J. Neurochem. 51: 859–868 (1988).
D. Chelsky, N.I. Gutterson, and D.E. Koshland, Jr., A diffusion assay for detection and quantitation of methyl-esterified proteins on polyacrylamide gels, Anal. Biochem. 141: 143–148 (1984).
C. Volker, R.A. Miller, W.R. McCleary, A. Rao, M. Poenie, J.M. Backer, and J.B. Stock, Effect of farnesylcysteine analogs on protein carboxyl methylation and signal transduction, J. Biol. Chem. 266: 21515–21522 (1991).
J. Stock, Balancing effector outputs, Current Biology 1: 154–156 (1991).
J.F. Hancock, A.I. Magee, J.E. Childs, and C.J. Marshall, All ras proteins are polyisoprenylated but only some are palmitoylated, Cell 57: 1167–1177 (1989).
Y. Kuroda, N. Suzuki, and T. Kataoka, The effect of post-translational modifications on the interaction of Ras2 with adenylyl cyclase, Science 259: 683–686 (1993).
P.M. Pereyra, E. Horvath, and P.E. Braun, Triton X-100 extractions of CNS myelin indicate a possible role for the minor myelin proteins in the stability of lamellae, Neurochem. Res. 13: 583–595 (1988).
C.S. Gillespie, R. Wilson, A. Davidson, and PJ. Brophy, Characterization of a cytoskeletal matrix associated with myelin from rat brain, Biochem. J. 260: 689–696 (1989).
R. Wilson and PJ. Brophy, Role for the oligodendrocyte cytoskeleton in myelination, J. Neurosci. Res. 22: 439–448 (1989).
C.A. Dyer and J.A. Benjamins, Organization of oligodendroglial membrane sheets. I. Association of myelin basic protein and CNP with cytoskeleton, J. Neurosci. Res. 24: 201–211 (1989).
R.G. Fenton, H-f. Kung, D.L. Longo, and M.R. Smith, Regulation of intracellular actin polymerization by prenylated cellular proteins, J. Cell Biol. 117: 347–356 (1992).
H.C. Agrawal, T.J., Sprinkle, and D. Agrawal, 2′-3′-cyclic nucleotide 3′-phosphodiesterase in the CNS is fatty acylated by thioester linkage, J. Biol. Chem. 265: 11849–11853 (1990).
B. Kacher, T. Behar, and M. Dubois-Dalcq, The oligodendrocyte cultured without neurons. Cell shape and motility, Cell Tissue Res. 244: 27–38 (1986).
J.F. Hesketh and I.F. Pryme, Interaction between mRNA, ribosomes and the cytoskeleton, Biochem. J. 277: 1–10 (1991).
S.J. Hill and E. Barbarese, Myelin basic protein mRNA is associated with the oligodendrocyte cytoskeleton, Soc. Neurosa. Abs. 18: 272.9 (1992).
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Angelis, D.D., Cox, M., Gao, E., Braun, P.E. (1994). Cellular and Molecular Characteristics of CNP Suggest Regulatory Mechanisms in Myelinogenesis. In: Salvati, S. (eds) A Multidisciplinary Approach to Myelin Diseases II. NATO ASI Series, vol 258. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2435-9_6
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DOI: https://doi.org/10.1007/978-1-4615-2435-9_6
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