Abstract
Nerve growth factor (NGF) is thought to have a profound effect on the development and maintenance of sympathetic and embryonic sensory neurones (see refs 1–3 for review). NGF activity isolated from the male mouse submaxillary gland (MSG) consists of three types of subunits, α, β and γ, which specifically interact to form a 7S, ∼130,000-molecular weight (Mr) complex. The 7S complex contains two identical 118-amino acid β-chains, which are solely responsible for the nerve growth-stimulating activity of NGF. While NGF is found in almost all vertebrates4, most research has focused on murine NGF, as the mouse male submaxillary gland contains higher levels of this polypeptide than other tissues4. Even so, β-NGF comprises only ∼0.1% of the protein in this small gland, which has made the study of this polypeptide difficult. The amino acid sequence of the mouse NGF β-chain has been determined5 and some information has been obtained regarding the size of a mouse precursor molecule6, pro-β-NGF, but little was known about the structure and relatedness of β-NGF from other vertebrates. Here we describe the isolation of mouse β-NGF complementary DNA (cDNA) and present its nucleotide sequence, which predicts a prepro-β-NGF molecule of Mr 27,000 (27K) and a pro-β-NGF molecule of Mr 25K. We have used the mouse β-NGF cDNA clone to isolate the human β-NGF gene, the coding regions of which are highly homologous to the mouse prepro-β-NGF nucleotide and amino acid sequences.
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References
Levi-Montalcini, R. A. Rev. Neurosci. 5, 341–362 (1982).
Yanker, B. A. & Shooter, E. M. A. Rev. Biochem. 51, 845–868 (1982).
Bradshaw, R. A. A. Rev. Biochem. 47, 191–216 (1978).
Harper, G. P. & Thoenin, H. J. Neurochem. 34, 893–903 (1980).
Angeletti, R. H., Mercanti, D. & Bradshaw, R. A. Biochemistry 12, 90–100 (1973).
Berger, E. A. & Shooter, E. M. Proc. natn. Acad. Sci. U.S.A. 74, 3647–3651 (1977).
Ishii, D. N. & Shooter, E. M. J. Neurochem. 25, 843–851 (1975).
Crea, R. & Horn, T. Nucleic Acids Res. 8, 2331–2348 (1980).
Lehrach, H., Diamond, D., Wozney, J. M. & Boedtker, H. Biochemistry 16, 4743–4751 (1977).
Angeletti, R. H., Hermodson, M. A. & Bradshaw, R. A. Biochemistry 12, 100–115 (1973).
Noda, M. et al. Nature 295, 202–206 (1982).
Kakidani, H. et al. Nature 298, 245–249 (1982).
Nakanishi, S. et al. Nature 278, 423–427 (1979).
Amara, S. G., Jonmas, V., Rosenfeld, M. G., Ong, E. S. & Evans, R. M. Nature 298, 240–244 (1982).
Smith, A. P., Varon, S. & Shooter, E. M. Biochemistry 7, 3259–3268 (1968).
Kozak, M. Nucleic Acids Res. 9, 5233–5252 (1981).
Blobel, G. et al. Soc. exp. Biol. Symp. 23, 9–36 (1979).
Lingappa, V. R., Lingappa, J. R., Prasad, R., Ebner, K. B. & Blobel, G. Proc. natn. Acad. Sci. U.S.A. 75, 2338–2342 (1978).
Lawn, R. M., Fritsch, E. F., Parker, R. C., Lake, G. B. & Maniatis, T. Cell 15, 1157–1163 (1978).
Southern, E. J. molec. Biol. 98, 503–517 (1975).
Maxam, A. M. & Gilbert, W. Proc. natn. Acad. Sci. U.S.A. 74, 560–564 (1977).
Proudfoot, N. J. & Brownlee, G. G. Nature 263, 211–214 (1976).
Tosi, M., Young, R. A., Hagenbuchle, O. & Schibler, U. Nucleic Acids Res. 9, 2313–2323 (1981).
Sharp, P. A. Cell 23, 643–646 (1981).
Ullrich, A., Dull, T. J., Gray, A., Brosius, J. & Sures, I. Science 209, 612–615 (1980).
Lomedico, P. et al. Cell 18, 545–556 (1979).
Breathnach, R., Benoist, C., O'Hare, K., Gannon, F. & Chambon, P. Proc. natn. Acad. Sci. U.S.A. 75, 4853–4857 (1978).
Wickens, M. P., Buell, G. N. & Schimke, R. T. J. biol. Chem. 253, 2483–2495 (1978).
Wallace, B. et al. Nucleic Acids Res. 9, 879–894 (1981).
Taylor, J. M., Illmensee, R. & Summers, J. Biochim. biophys. Acta 4, 324–330 (1976).
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Ullrich, A., Gray, A., Berman, C. et al. Human β-nerve growth factor gene sequence highly homologous to that of mouse. Nature 303, 821–825 (1983). https://doi.org/10.1038/303821a0
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DOI: https://doi.org/10.1038/303821a0
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