Abstract
Neural tissues contain high levels of the cellular homologue of the transforming protein of Rous sarcoma virus (RSV)1–4, but neither the specific cell types expressing high levels of c-src, nor the function of the cellular src (c-src) protein has been determined. Using primary culture methods, we have found that pure neurones and astrocytes derived from the rat central nervous system (CNS) contain 15- to 20-times higher levels of the c-src protein than fibroblasts. However, the specific activity of the c-src protein from the neuronal cultures is 6- to 12-times higher than that from the astrocyte cultures. In addition, the c-src protein expressed in neuronal cultures contains a structural alteration within the aminoterminal region of the molecule that causes a shift in the mobility of the c-src protein on the SDS-polyacrylamide gels. These results indicate that a structurally distinct form of the cellular src protein that possesses an activated tyrosylkinase activity is expressed at very high levels in post-mitotic CNS neurones.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Cotton, P. C. & Brugge, J. S. Molec. cell. Biol. 3, 1157–1162 (1983).
Barnekow, A. & Bauer, H. Biochim. biophys. Acta 782, 94–102 (1984).
Levy, B. T., Sorge, L. K., Meymandi, A. & Maness, P. Devl Biol. 104, 9–17 (1984).
Sorge, L. K., Levy, B. T. & Maness, P. F. Cell 36, 249–256 (1984).
Kaufman, L. F. & Barrett, J. N. Science 220, 1394–1396 (1984).
Mirsky, R., Wendon, L. M., Black, P., Stolkin, C. & Bray, D. Brain Res. 148, 251–259 (1978).
Yen, S. H. & Fields, K. L. J. Cell Biol. 88, 115–126 (1981).
Bignami, A., Eng, L. F., Dahl, L. D. & Uyeda, C. T. Brain Res. 43, 429–435 (1972).
Eisenbarth, C. S., Walsh, F. S. & Nirenberg, M. Proc. natn. Acad. Sci. U.S.A. 76, 4913–4917 (1979).
Lipsich, L. A., Lewis, A. J. & Brugge, J. S. J. Virol. 48, 352–360 (1983).
Cotton, P. C. thesis, SUNY, New York (1984).
Cotton, P. C. & Brugge, J. S. J. molec. Biol (submitted).
Bolen, J. B. et al. Cell 38, 767–777 (1984).
Yonemoto, W., Jarvis-Morar, M., Brugge, J. S., Bolen, J. & Israel, M. Proc. natn. Acad. Sci. U.S.A. (in the press).
Iba, H., Takeya, T., Cross, F., Hanafusa, T. & Hanafusa, H. Proc. natn. Acad. Sci. U.S.A. 81, 4424–4428 (1984).
Iba, H., Cross, F. R., Garber, E. & Hanafusa, H. Molec. cell. Biol. 5, 1058–1066 (1985).
Keane, R. W., Lipsich, L. A. & Brugge, J. S. Devl Biol. 103, 38–52 (1984).
Fiszman, M. Y. & Fuchs, P. Nature 254, 429–431 (1975).
Holtzer, H., Biehl, J., Yeoh, G., Meganathan, R. & Kaji, A. Proc. natn. Acad. Sci. U.S.A. 72, 4051 (1975).
Pacifici, M., Boettiger, D., Roby, K. & Holtzer, H. Cell 11, 891–988 (1977).
Boettiger, D., Roby, K., Brumbaugh, J., Biehl, J. & Holtzer, H. Cell 11, 881–890 (1977).
Collett, M. S. & Erikson, R. L. Proc. natn. Acad. Sci. U.S.A. 75, 2021–2024 (1978).
Levinson, A. D., Oppermann, H., Levintow, L., Varmus, H. E. & Bishop, J. B. Cell 15, 561–572 (1978).
Hunter, T. & Sefton, B. M. Proc. natn. Acad. Sci. U.S.A. 77, 1311–1315 (1980).
Collett, M. S., Erikson, E., Purchio, A. F., Brugge, J. S. & Erikson, R. L. Proc. natn. Acad. Sci. U.S.A. 76, 3159–3163 (1979).
Oppermann, H., Levinson, A. D., Varmus, H. E., Levintow, L. & Bishop, J. M. Proc. natn. Acad. Sci. U.S.A. 76, 1804–1808 (1979).
Rohrschneider, L. R., Eisenman, R. N. & Leitch, C. R. Proc. natn. Acad. Sci. U.S.A. 76, 4479–4483 (1979).
Parker, R., Varmus, H. & Bishop, M. Cell 37, 131–139 (1984).
Shalloway, D., Coussens, P. M. & Yacluk, P. Cancer Cell Vol. 2 (eds Van de Woude, G. F., Levine, A. J., Topp, W. C. & Watson, J. D.) 9–18 (Cold Spring Harbor Laboratory, New York, (1983).
Lowry, O. H., Rosebrough, N. J., Fan, A. L. & Randall, R. J. J. biol. Chem. 193, 265–285 (1951).
Laemmli, U. K. Nature 227, 680–685 (1970).
Brugge, J. S. & Erikson, R. L. Nature 269, 346–348 (1977).
Cleveland, D. W., Fischer, S. G., Kirschner, M. W. & Laemmli, U. K. J. biol. Chem. 252, 1102–1106 (1977).
Collett, M. S., Erikson, E. & Erikson, R. L. J. Virol. 29, 770–781 (1979).
Smart, J. E. et al. Proc. natn. Acad. Sci. U.S.A. 78, 6013–6017 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Brugge, J., Cotton, P., Queral, A. et al. Neurones express high levels of a structurally modified, activated form of pp60c-src. Nature 316, 554–557 (1985). https://doi.org/10.1038/316554a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/316554a0
This article is cited by
-
MicroExonator enables systematic discovery and quantification of microexons across mouse embryonic development
Genome Biology (2021)
-
Inhibition of Maternal c-Src Ameliorates the Male Offspring Hypertension by Suppressing Inflammation and Neurotransmitters in the Paraventricular Nucleus
Cardiovascular Toxicology (2021)
-
Morphine activation of mu opioid receptors causes disinhibition of neurons in the ventral tegmental area mediated by β-arrestin2 and c-Src
Scientific Reports (2017)
-
Inhibition of N1-Src kinase by a specific SH3 peptide ligand reveals a role for N1-Src in neurite elongation by L1-CAM
Scientific Reports (2017)
-
A Ser75-to-Asp phospho-mimicking mutation in Src accelerates ageing-related loss of retinal ganglion cells in mice
Scientific Reports (2017)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.