Changes in Nuclear Proteins on Transformation of Rat Epithelial Thyroid Cells by a Murine Sarcoma Retrovirus

Cancer Research

Volumn 45, Issue , 1985, Pages 6051-6057

  Giancotti, Vincenzo ^a   Berlingieri, Maria Teresa ^b   DiFiore, Pier Paolo ^b   Fusco, Alfredo ^b   Vecchio, Giancarlo ^b   Crane Robinson, Colyn ^c  

^a UNIVERSITY OF TRIESTE   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c UNIVERSITY OF PORTSMOUTH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; NUCLEAR PROTEIN;

ANIMAL CELL; CELL DIFFERENTIATION; CELL LINE; CONTROLLED STUDY; ELECTROPHORESIS; ENDOCRINE SYSTEM; IN VITRO STUDY; KIRSTEN SARCOMA ONCOVIRUS; NONHUMAN; PRIORITY JOURNAL; RAT; THERAPY; THYROID CELL; TRANSFORMATION; VIRUS CELL TRANSFORMATION;

ANIMALS; CELL NUCLEUS; CELL TRANSFORMATION, VIRAL; EPITHELIUM; HIGH MOBILITY GROUP PROTEINS; HISTONES; ONCOGENES; PHOSPHOPROTEINS; RATS; SARCOMA VIRUSES, MURINE; THYROID GLAND;

EID: 0022410391     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article

References (21)

1. Aaronson, S. A. Unique aspects of the interactions of retroviruses with vertebrate cells: Rhodes memorial lecture. Cancer Res., 43:1–5,1983.
2. Leavitt, J., and Moysiz, R. Changes in gene expression accompanying neo-plastic transformation of Syrian hamster cells. J. Biol. Chem., 253:2497–2500, 1978.
3. Blat, C., Harel, L., Villandy, J., and Golde, A. Effects of transformation of chicken cells by Rous sarcoma virus on in vitro phosphorylation of nuclear non-histone proteins. Exp. Cell Res., 134:121–128,1981.
4. Blat, C., Harel, L., Villandy, J., and Golde, A. Rous sarcoma virus-induced changes in the pattern of phosphorylation of non-histone nuclear proteins. Exp. Cell Res., 145:305–314,1983.
5. Pumo, D. E., Stein, G. S., and Kleinsmith, L. J. Stimulated phosphorylation of non-histone phospho-proteins in SV-40 transformed WI-38 human diploid fibroblasts. Biochim. Biophys. Acta, 402:125–130.1975.
6. Balhom, P., Balhom, M., Morris, H. P., and Chalkley, R. Comparative high-resolution electrophoresis of tumor histories: variation in phosphorylation as a function of cell replication rate. Cancer Res., 32:1775–1784,1972.
7. Colletta, G., Pinto, A., di Fiore, P., Fusco, A., Ferrentino, M., Awedimento, V. E., Tsuchkda, N., and Vecchio, G. Dissociation between transformed and differentiated phenotype in rat thyroid epithelial cells after transformation with a temperature-sensitive mutant of the Kirsten murine sarcoma virus. Mol. Cell. Biol., 3: 2099–2109,1983.
8. Fusco, A., Pinto, A., Tramontano D., Tajana, G., Vecchio, G., and Tsuchida, N. Block in the expression of differentiation markers of rat thyroid epithelial cells by transformation with Kirsten murine sarcoma virus. Cancer Res., 42: 618–626,1982.
9. Der, C. J., Krontiris, T. G., and Cooper, G. M. Transforming genes of human bladder and lung carcinoma cell lines are homologous to the ras genes of Harvey and Kirsten sarcoma viruses. Proc. Natl. Acad. Sci. USA, 79; 3637–3640,1983.
10. Ambesi-lmpiombato, F. S., Parks, L. A. M., and Coon, H. G. Culture of hormone-dependent functional epithelial cells from rat thyroids. Proc. Natl. Acad. Sci. USA, 77: 3455–3459,1980.
11. Symmons, P. Ph.D. thesis, university of Tubingen, Federal Republic of Germany, 1984.
12. McGrath, J. P., Capon, D. J., Goeddel, D. V., and Levinson, A. D. Comparative biochemical properties of normal and activated human ras p21 protein. Nature (Lond.), 310: 644–649.1984.
13. Shin, T. Y., Papageorge, A. G. Stokes, P. E., Weeks, M. O., and Scolnick, E. M. Guanine nucleotide-binding and autophosphorylation activities associated with the p21src protein of Harvey murine sarcoma virus. Nature (Lond.), 287: 686–691.1980.
14. Gurtey, L. R., D'Ama, J. A., Barham, S. S., Deaven, L. L., and Tobey, R. A. Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells. Eur. J. Biochem., 84:1–15,1978.
15. Gurtey, L R., Walters, R. A., and Tobey, R. A. Cell-cycle-specific changes in histone phosphorylation associated with cell proliferation and chromosome condensation. J. CeN Biol., 60:356–364,1974.
16. Lund, T., Holtlund, J. Fredriksen, M., and Laland, S. G. On the presence of two new high mobility group-like proteins in HeLa S3 cells. FEBS Lett., 152: 163–167,1983.
17. Goodwin, G. H., Cockerill, P. N., Kellam, S. and Wright, C. A. Fractionation by high-performance liquid chromatography of the low-molecular-mass high-mobility-group (HMG) chromosomal proteins present in proliferating rat cells and an investigation of the HMG proteins present in virus transformed cells. Eur. J. Biochem., 149: 47–51,1985.
18. Cooper. E., and Spaulding, S. W. HMG (high mobility group)-14/17-like proteins in caff thyroid. Thyrotropin-dependent phosphorylation and comparison with calf thymus proteins. Biochem. J. 215:643–649,1983.
19. Walton, G. M., Gill, G. N., Cooper, E., and Spaulding, S. W. Thyrotropin-stimulated phosphorylation of high mobility group protein 14 in vivo at the site catalyzed by cyclic nucteotide-dependent protein kinase in vitro. J. Biol. Chem., 259:601–607,1984.
20. Weisbrod, S., and Weintraub, H. Isolation of a subclass of nuclear proteins responsible for conferring a DNase l-sensitive structure on globin chromatin. Proc. Natl. Acad. Sci. USA, 76:630–634,1979.
21. Busch, H. Nucleolar proteins: purification, isolation, and functional analysis. In: L S. Hinilica (ed.), Chromosomal Non-Histone Proteins, Vol. 4, Chap. 6, 233–286. Boca Raton, FL: CRC Press, Inc., 1984.