Molecular Approach to the Study of Neural Function and Differentiation

  • M. M. Portier
  • B. Croizat
  • F. Berthelot
  • B. Edde
  • D. Paulin
  • F. Gros


Neurobiology constitutes one of the most challenging aspects of cellular and development biology due to the complexity of the central nervous system and to the diversity of the behavioral patterns among evolved eukaryotic organisms.


Neuroblastoma Cell Neurite Outgrowth Mature Neuron Neural Function Serum Withdrawal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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  1. 1).
    His, W. (1889). Arch. Anat. Entwicklungsgeschichte, p. 49 cited in “Histogenes of the Central Nervous System” (1967), Jan Langman.Google Scholar
  2. 2).
    Hardesty, J. (1904). Ann. J. Anat. 3, 229. Cited in “Histogenesis of the Central Nervous System” (1957), Jan LangmanCrossRefGoogle Scholar
  3. 3).
    Mirsky, R. (1980). Cell-type-specific markers in nervous system cultures. TINS, 3, No. 8, 190.Google Scholar
  4. 4).
    Zipser, B. and McKay, R. (1981). Monoclonal antibodies specific for identifiable leech neurons. In: Monoclonal Antibodies to Neural Antigens, (eds. R. McKay, M.C. Raff, L. Reichardt) Vol. 2, p. 91. Cold Spring Harbor Reports in Neurosciences, Cold Spring Harbor, N.Y.Google Scholar
  5. 5).
    Barnstable, C.J. (1980). Monoclonal antibodies which recognize different cell types in the rat retina. Nature, 286, 23.CrossRefGoogle Scholar
  6. 6).
    Barnstable, C.J. (1981). Developmental studies of rat retina cells using cell-type-specific monoclonal antibodies. In: Monoclonal Antibodies to Neural Antigens, op. cit. p. 219.Google Scholar
  7. 7).
    Trisler, G.D., Schneider, M.D., and Nirenberg, M. (1981). A topographic gradient of molecules in retina can be used to identify neuron position. Proc. Natl. Acad. Sci. USA, 78, 2145.PubMedCrossRefGoogle Scholar
  8. 8).
    Zipser, B. and Mckay, R. (1981). Monoclonal antibodies distinguish identifiable neurons in the leech. Nature, 289, 549.PubMedCrossRefGoogle Scholar
  9. 9).
    Stent, G.S. and Weisblat, D.A. (1982). The development of a simple nervous system. Sci: Amer. 241, No. 1, 135.Google Scholar
  10. 10).
    Matthew, W.D., Reichardt, L.F. and Tsavaler, L. (1981). Monoclonal antibodies to synaptic membranes and vesicles. In: Monoclonal Antibodies to Neural Antigens, op. cit. p. 163.Google Scholar
  11. 11).
    De Blas, A.L., Busis, N.A. and Nirenberg, M. (1981). Monoclonal antibodies to synaptosomal membrane molecules. In: Monoclonal Antibodies to Neural Antigens, op. cit. p. 181.Google Scholar
  12. 12).
    Schwartz, J.H. (1981). Chemical basis of synaptic transmission In: Principles of Neural sciences, p. 107.Google Scholar
  13. 13).
    Snyder, S.H. (1980) Brain peptides as neurotransmitters. Science, 209, 976.PubMedCrossRefGoogle Scholar
  14. 14).
    Acher, R. (1981). Evolution of neuropeptides. TINS 4, No. 9, 225.Google Scholar
  15. 15).
    Nakanishi, A., Inove, A., Kita, T., Nakamura, M., Chang, A., Cohen, S., and Numa, S. (1979). Nucleotide sequence of cloned cDNA for bovine corticotropin — β lipotropin precursor. Nature, 278, 423.PubMedCrossRefGoogle Scholar
  16. 16).
    Comb, M., Seeburg, P.H., Adelman, J., Eiden, L. and Herbert, E. (1982). Primary structure of the human Met and Leu enkephalin precursor and its mRNA. Nature, 295, 663.PubMedCrossRefGoogle Scholar
  17. 17).
    Shine, J., Fettes, I., Lan, N.C.Y., Robert, J.L. and Baxter, J.D. (1980). Expression of cloned β-endorphin gene sequences by Escherichia coli Nature, 285, 456.PubMedCrossRefGoogle Scholar
  18. 18).
    Giraudat, J., Devillers-Thiery, A., Rougeon, F., Auffray, C. and Changeux, J.P. (1982). Identification of a cDNA clone coding for the acetylcholine binding subunit of torpedo marmorata acetylcholine receptor. EMBO Journal, in pressGoogle Scholar
  19. 19).
    Mallet, J., personal communicationsGoogle Scholar
  20. 20).
    Augusti-Tocco, G. and Sato, G. (1969). Establishment of functional clonal lines of neuron from mouse neuroblastoma. Proc. Natl. Acad. Sci. USA, 64, 311.PubMedCrossRefGoogle Scholar
  21. 20a).
    Schubert, D., Humphreys, S., Baroni, C. and Cohn, M. (1969). In vitro differentiation of a mouse neuroblastoma. Proc. Natl. Acad. Sci. USA., 64, 316.PubMedCrossRefGoogle Scholar
  22. 20b).
    For a general review cf. De Laat, S.W. and Van Der Saag, P.T. (1982). The plasma membrane as a regulatory site in growth and differentiation of neuroblastoma cells. Ixy. International Review of Cytology, 74, 1.PubMedCrossRefGoogle Scholar
  23. 21).
    Stallcup, N.B. and Cohn, M. (1979). Cell-specific antisera as reagents for studying the nervous system. Tins,Google Scholar
  24. 22).
    Nelson, P., Clifford, C. and Nirenberg, M. (1976). Synapse formation between clonal neuroblastoma x glioma hybrid cells and striated muscle cells. Proc. Natl. Acad. Sci. USA., 76, 123.CrossRefGoogle Scholar
  25. 23).
    Minna, J., Glazer, D. and Nirenberg, M. (1972). Genetic dissection of neural properties using somatic cell hybrids. Nature New Biol. 235, 225.PubMedGoogle Scholar
  26. 24).
    Greene, L.A. and Shooter, E.M. (1980). Ann. Review. Neurosci. 3, 353.CrossRefGoogle Scholar
  27. 25).
    De Vitry, F. (1977). Growth and differentiation of a primitive nervous cell line after in vivo transplantation into syngeneic mice. Nature, 267, 48.PubMedCrossRefGoogle Scholar
  28. 26).
    Roberts, J.L., Philipps, M.A., Rosa, P.A. and Herbert, E. (1978). Steps involved in the processing of common precursor forms of adrenocorticotropin and endorphin in cultures of mouse pituitary cells. Biochemistry, 17, 3619.CrossRefGoogle Scholar
  29. 27).
    Amano, T., Richelson, E. and Nirenberg, M. (1972). Neurotransmitter synthesis by neuroblastoma clones. Proc. Natl. Acad. Sci. USA, 60, 258.CrossRefGoogle Scholar
  30. 28).
    Legault-Demare, L., Zeitoun, Y., Lando, D., Lamande, N., Grasso, A. and Gros, F. (1980). Expression of a specific neuronal protein 14–3–2 during in vitro differentiation of neuroblastoma cells. Exp. Cell Res., 125, 233.PubMedCrossRefGoogle Scholar
  31. 29).
    Pickel, V.M., Reis, D.J., Marangos, P.J., Zouzely Neurath, C. (1976). Immunocytochemical localization of nervous system specific proteins (NSP-R) in rat brain. Brain Res., 105, 184.PubMedCrossRefGoogle Scholar
  32. 29a).
    Zouzely Neurath, C. and Keller, A. (1977). Mechanisms of regulation and special function of protein synthesis in the brain. (eds. S. Roberts, A. Latjha and W.H. Gispen), Elsevier/North Holland Biomedical Press, Amsterdam, p. 279.Google Scholar
  33. 29b).
    Moore, B.W. (1972). Chemistry and biology of two proteins S100 and 14–3–2 specific to the nervous system. Int. Rev. Neurobiol. 15, 215.PubMedCrossRefGoogle Scholar
  34. 30).
    Felsani, A., Berthelot, F., Gros, F. and Croizat, B. (1978). Complexity of polysomal poly(A) RNA in undifferentiated and differentiated neuroblastoma cells. Eur. J. Biochem, 92, 569.PubMedCrossRefGoogle Scholar
  35. 31).
    Berthelot, F., Gros, F. and Croizat, B. (1980). Complexity of polysomal poly(A) RNA in different developmental stages of non-differentiating neuroblastoma clone. FEBS Lett. 122, 109.PubMedCrossRefGoogle Scholar
  36. 32).
    Gros, F., Croizat, B., Portier, M-M., Berthelot, F. and Felsani, A. (1982). The regulation of gene expression during terminal neurogenesis. In: Molecular Genetic Neurosciences, (eds. F.O. Schmidt, S.J. Bird and F.E. Bloom), p. 335, Raven Press, New York.Google Scholar
  37. 33).
    Legault-Demare, L., Lamande, N., Zeitoun, Y., Gros, F., Scarna, H., Keller, A., Lando, D. and Cousin, M.A. (1981). Transition between isozymic forms of enolase during in vitro differentiation of neuroblastoma cells. Neurochemistry Int., 3, No 5, 303.CrossRefGoogle Scholar
  38. 34).
    Lazar, M. and Vigny, M. (1980). Modulation of the distribution of acetylcholinesterase molecular forms in a murine neuroblastoma x sympathetic ganglion cell hybrid cell lines. J. Neurodhem., 35, 1067.CrossRefGoogle Scholar
  39. 35).
    Thibault, J., Vidal, D. and Gros, F. (1981). In vitro translation of mRNA from rat pheochromocytoma tumours, characterization of tyrosine hydrolase. Biochem. Biophys. Res. Comm. 99, 960.PubMedCrossRefGoogle Scholar
  40. 36).
    Berwald-Netter, Y., Moutot, N.M., Koulakoff, A. and Couraud, F. (1981). Na+ channel associated scorpion toxin receptor sites as probes for neuronal evolution in vivo and in vitro. Proc. Natl. Acad. Sci. USA, 78, 1245.PubMedCrossRefGoogle Scholar
  41. 37).
    Croizat, B., Berthelot, F., Ferrandes, B., Eymard, P. and Sahuquillo, C. (1979). DiffErenciation morphologique du neuroblastome par l’acide 1-methyl cyclohexane carbosilique (CCA) et certains dérivés en C1. C.R. Acad. Sci. Paris, 289, 1283.Google Scholar
  42. 38).
    Gozes, I., Saya, D. and Littauer, U.Z. (1979). Tubulin micro-heterogeneity in neuroblastoma and glioma cell lines differs from that of the brain. Brain Res., 171, 171.PubMedCrossRefGoogle Scholar
  43. 39).
    Chan, V. and Baxter, C. (1979). Compartments of tubulins and tubulin-like proteins in differentiating neuroblastoma cells. Brain Res., 174, 135.PubMedCrossRefGoogle Scholar
  44. 40).
    Dahl, J.L. and Weibel, V.J. (1979). Changes in tubulin heterogeneity during postnatal development of rat brain. Biochem. Biophys. Res. Comm. 86, 822.PubMedCrossRefGoogle Scholar
  45. 41).
    Shelanski, M.L. and Liem, R.K.H. (1979). Neurofilaments. J. Neurochem., 33, 5.PubMedCrossRefGoogle Scholar
  46. 42).
    Portier, M.M. and Croizat, B. Personal CommunicationsGoogle Scholar
  47. 43).
    Edde, B., Jeantet, C. and Gros, F. (1981). One β-tubulin sub-unit accumulates during neurite outgrowth in mouse neuroblastoma cells. Biochem. Biophys. Res. Comm. 103, 1035.PubMedCrossRefGoogle Scholar
  48. 44).
    Shelanski, M.L. and Feit, H. (1972). In: The Structure and Functions of the Nervous Tissue, (ed. G.A. Bourne), 6, p.47, Academic Press, New York.Google Scholar
  49. 45).
    Thao, N.B., Wooten, G.H., Axelrod, J. and Kopin, I.J. (1972). Inhibition of release of dopamine-β-hydrolase and norepinephrine from synpathetic nerves by colchicine, vinblastine, or cytochalasin-B. Proc. Natl. Acad. Sci. USA, 69, 520.CrossRefGoogle Scholar
  50. 46).
    Denoulet, P., Edde, B., Jeantet, C. and Gros, F. (1982) Evolution of tubulin heterogeneity during mouse brain development. Biochimie, 64, 165.PubMedCrossRefGoogle Scholar
  51. 47).
    Edde, B., Portier, M-M., Sahuquillo, C., Jeantet, C. and Gros, F. (1982). Changes in some cytoskeletal proteins during neuroblastoma cell differentiation. Biochimie, 64, 141PubMedCrossRefGoogle Scholar
  52. 48).
    Ginzburg, I., Bechar, L., Gival, D. and Littauer, U.Z. (1981) The nucleotide sequence of rat α-tubulin: 3′-end characteristics, and evolutionaly conservation. Nucl. Acids Res., 9, 2691PubMedCrossRefGoogle Scholar
  53. 49).
    Cleveland, D.W., Lopata, M.A., Mcdonald, R.J., Cowan, W.J., Rutter, W.J. and Kirschner, M.W. (1980). Number and evolutionary conservation of α and β tubulin and cytoplasmic β and γ actin genes using specific cDNA probes. Cell, 20, 95.PubMedCrossRefGoogle Scholar
  54. 49a).
    Sanchez, F., Natzic, J., Cleveland, D.W., Kirschner, M.W. and McCarthy, B. (1980) A dispersed multigene family encoding tubulin in Drosophila melanogaster. Cell, 22, 845.PubMedCrossRefGoogle Scholar
  55. 49b).
    Silflow, C.D. and Roenbaum, J.L. (1981). Multiple a and s tubulin genes in Chlamydomonas and regulation of tubulin in RNA levels after deflagellation. Cell 24, 81.PubMedCrossRefGoogle Scholar
  56. 50).
    Piperno, G. and Luck, D.J. (1976). Phosphorylation of axonemal proteins in Chlamydomonas reinhardtii. J. Biol. Chem., 251, 2161PubMedGoogle Scholar
  57. 51).
    Raybin, D. and Flavin, M. (1977). Modification of tubulin by tyrosylation in cells and extracts and its effect on assembly in vitro. J. Cell Biol., 73, 492.PubMedCrossRefGoogle Scholar
  58. 52).
    Feit, H. and Shelanski, M.L. (1975) Is tubulin a glycoprotein? Biochem. Biophys. Res. comm. 66, 920.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • M. M. Portier
    • 1
  • B. Croizat
    • 1
  • F. Berthelot
    • 1
  • B. Edde
    • 1
  • D. Paulin
    • 1
    • 2
  • F. Gros
    • 1
  1. 1.Laboratoire de Biochimie CellulaireCollège de FranceParisFrance
  2. 2.Département de Biologie MoléculaireInstitut PasteurParisFrance

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