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. 1988 Jan;8(1):497–501. doi: 10.1128/mcb.8.1.497

Augmented mitogenic responsiveness to epidermal growth factor in murine fibroblasts that overexpress pp60c-src.

D K Luttrell 1, L M Luttrell 1, S J Parsons 1
PMCID: PMC363160  PMID: 2447487

Abstract

C3H10T1/2 murine fibroblasts overexpressing chicken pp60c-src showed a two- to fivefold enhanced incorporation of [3H]thymidine into DNA in response to epidermal growth factor (EGF) relative to that of the parent line. No difference in growth characteristics, number and affinity of EGF receptors, or hormone potency was attributable to c-src overexpression. These results suggest that pp60c-src may interact with the mitogenic signal transduction pathway of EGF in some event distal to hormone binding.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Collett M. S., Brugge J. S., Erikson R. L. Characterization of a normal avian cell protein related to the avian sarcoma virus transforming gene product. Cell. 1978 Dec;15(4):1363–1369. doi: 10.1016/0092-8674(78)90061-2. [DOI] [PubMed] [Google Scholar]
  2. Cotton P. C., Brugge J. S. Neural tissues express high levels of the cellular src gene product pp60c-src. Mol Cell Biol. 1983 Jun;3(6):1157–1162. doi: 10.1128/mcb.3.6.1157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Courtneidge S. A., Levinson A. D., Bishop J. M. The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60proto-src) are associated with the plasma membrane. Proc Natl Acad Sci U S A. 1980 Jul;77(7):3783–3787. doi: 10.1073/pnas.77.7.3783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Downward J., Yarden Y., Mayes E., Scrace G., Totty N., Stockwell P., Ullrich A., Schlessinger J., Waterfield M. D. Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences. Nature. 1984 Feb 9;307(5951):521–527. doi: 10.1038/307521a0. [DOI] [PubMed] [Google Scholar]
  5. Gentry L. E., Chaffin K. E., Shoyab M., Purchio A. F. Novel serine phosphorylation of pp60c-src in intact cells after tumor promoter treatment. Mol Cell Biol. 1986 Feb;6(2):735–738. doi: 10.1128/mcb.6.2.735. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Golden A., Nemeth S. P., Brugge J. S. Blood platelets express high levels of the pp60c-src-specific tyrosine kinase activity. Proc Natl Acad Sci U S A. 1986 Feb;83(4):852–856. doi: 10.1073/pnas.83.4.852. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gould K. L., Woodgett J. R., Cooper J. A., Buss J. E., Shalloway D., Hunter T. Protein kinase C phosphorylates pp60src at a novel site. Cell. 1985 Oct;42(3):849–857. doi: 10.1016/0092-8674(85)90281-8. [DOI] [PubMed] [Google Scholar]
  8. Hamlin J. L., Pardee A. B. S phase synchrony in monolayer CHO cultures. Exp Cell Res. 1976 Jul;100(2):265–275. doi: 10.1016/0014-4827(76)90147-6. [DOI] [PubMed] [Google Scholar]
  9. Heath J. K., Mahadevan L., Foulkes J. G. The role of EGF receptor transmodulation in embryonal carcinoma-derived growth factor-induced mitogenesis. EMBO J. 1986 Aug;5(8):1809–1814. doi: 10.1002/j.1460-2075.1986.tb04430.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Heldin C. H., Westermark B. Growth factors: mechanism of action and relation to oncogenes. Cell. 1984 May;37(1):9–20. doi: 10.1016/0092-8674(84)90296-4. [DOI] [PubMed] [Google Scholar]
  11. Johnson P. J., Coussens P. M., Danko A. V., Shalloway D. Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells. Mol Cell Biol. 1985 May;5(5):1073–1083. doi: 10.1128/mcb.5.5.1073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Levy B. T., Sorge L. K., Meymandi A., Maness P. F. pp60c-src Kinase is in chick and human embryonic tissues. Dev Biol. 1984 Jul;104(1):9–17. doi: 10.1016/0012-1606(84)90031-9. [DOI] [PubMed] [Google Scholar]
  13. McCarley D. J., Parsons S. J. Reduced tyrosine kinase specific activity is associated with hypophosphorylation of pp60c-src in cells infected with avian erythroblastosis virus. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5793–5797. doi: 10.1073/pnas.84.16.5793. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Oppermann H., Levinson A. D., Varmus H. E., Levintow L., Bishop J. M. Uninfected vertebrate cells contain a protein that is closely related to the product of the avian sarcoma virus transforming gene (src). Proc Natl Acad Sci U S A. 1979 Apr;76(4):1804–1808. doi: 10.1073/pnas.76.4.1804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ralston R., Bishop J. M. The product of the protooncogene c-src is modified during the cellular response to platelet-derived growth factor. Proc Natl Acad Sci U S A. 1985 Dec;82(23):7845–7849. doi: 10.1073/pnas.82.23.7845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Reznikoff C. A., Brankow D. W., Heidelberger C. Establishment and characterization of a cloned line of C3H mouse embryo cells sensitive to postconfluence inhibition of division. Cancer Res. 1973 Dec;33(12):3231–3238. [PubMed] [Google Scholar]
  17. Rozengurt E. Early signals in the mitogenic response. Science. 1986 Oct 10;234(4773):161–166. doi: 10.1126/science.3018928. [DOI] [PubMed] [Google Scholar]
  18. Shalloway D., Coussens P. M., Yaciuk P. Overexpression of the c-src protein does not induce transformation of NIH 3T3 cells. Proc Natl Acad Sci U S A. 1984 Nov;81(22):7071–7075. doi: 10.1073/pnas.81.22.7071. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sorrentino V., Drozdoff V., McKinney M. D., Zeitz L., Fleissner E. Potentiation of growth factor activity by exogenous c-myc expression. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8167–8171. doi: 10.1073/pnas.83.21.8167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Southern P. J., Berg P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J Mol Appl Genet. 1982;1(4):327–341. [PubMed] [Google Scholar]
  21. Standaert M. L., Schimmel S. D., Pollet R. J. The development of insulin receptors and responses in the differentiating nonfusing muscle cell line BC3H-1. J Biol Chem. 1984 Feb 25;259(4):2337–2345. [PubMed] [Google Scholar]
  22. Tamura T., Friis R. R., Bauer H. pp60c-src is a substrate for phosphorylation when cells are stimulated to enter cycle. FEBS Lett. 1984 Nov 5;177(1):151–156. doi: 10.1016/0014-5793(84)81001-7. [DOI] [PubMed] [Google Scholar]
  23. Taparowsky E. J., Heaney M. L., Parsons J. T. Oncogene-mediated multistep transformation of C3H10T1/2 cells. Cancer Res. 1987 Aug 1;47(15):4125–4129. [PubMed] [Google Scholar]
  24. Wakelam M. J., Davies S. A., Houslay M. D., McKay I., Marshall C. J., Hall A. Normal p21N-ras couples bombesin and other growth factor receptors to inositol phosphate production. Nature. 1986 Sep 11;323(6084):173–176. doi: 10.1038/323173a0. [DOI] [PubMed] [Google Scholar]
  25. Wigler M., Pellicer A., Silverstein S., Axel R., Urlaub G., Chasin L. DNA-mediated transfer of the adenine phosphoribosyltransferase locus into mammalian cells. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1373–1376. doi: 10.1073/pnas.76.3.1373. [DOI] [PMC free article] [PubMed] [Google Scholar]

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