78-Kilodalton Glucose-Regulated Protein Is Induced in Rous Sarcoma Virus-Transformed Cells Independently of Glucose Deprivation

LITERATURE CITED

• Bedard, P.-A., D. L. Alcorta, D. L. Simmons, K.-C. Luk, and R. L. Erikson. 1987. Constitutive expression of a gene encoding a polypeptide homologous to biologically active human platelet protein in Rous sarcoma virus-transformed fibroblasts. Proc. Natl. Acad. Sci. USA 84:6715–6719.
   PubMedGoogle Scholar
• Cox, R. A. 1968. The use of guanidium chloride in the isolation of nucleic acids. Methods Enzymol. 12B:120–129.
   Google Scholar
• Davis, L. G., M. D. Dibner, and J. F. Battey. 1986. Basic methods in molecular biology. Elsevier Science Publishing Company, New York.
   Google Scholar
• Fagan, J. B., M. E. Sobel, K. M. Yamada, B. de Crombrugghe, and I. Pastan. 1981. Effects of transformation on fibronectin gene expression using cloned fibronectin cDNA. J. Biol. Chem. 256:520–525.
   PubMedGoogle Scholar
• Flier, J. S., M. M. Mueckler, P. Usher, and H. F. Lodish. 1987. Elevated levels of glucose transport and transporter messenger RNA are induced by ras or src oncogenes. Science 235:1492–1495.
   PubMed Web of Science ®Google Scholar
• Gal, S., and M. M. Gottesman. 1986. The major excreted protein of transformed fibroblasts is an activable acid-protease. J. Biol. Chem. 261:1760–1765.
   PubMed Web of Science ®Google Scholar
• Groudine, M., M. Peretz, and H. Weintraub. 1981. Transcriptional regulation of hemoglobin switching in chicken embryos. Mol. Cell. Biol. 1:281–288.
   PubMed Web of Science ®Google Scholar
• Haas, I. G., and M. Wabl. 1983. Immunoglobulin heavy chain binding protein. Nature (London) 306:387–389.
   PubMed Web of Science ®Google Scholar
• Hanafusa, H. 1969. Rapid transformation of cells by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 63:318–325.
   PubMedGoogle Scholar
• Hanafusa, H. 1977. Cell transformation by RNA tumor viruses, p. 401–483. In H. Fraenkel-Conrat and R. R. Wagner (ed.), Comprehensive virology, vol. 10. Plenum Publishing Corp., New York.
   Google Scholar
• Hendricks, M., and H. Weintraub. 1984. Multiple tropomyosin polypeptides in chicken embryo fibroblasts: differential repression of transcription by Rous sarcoma virus transformation. Mol. Cell. Biol. 4:1823–1833.
   PubMedGoogle Scholar
• Howard, B. H., S. L. Adams, M. E. Sobel, I. Pastan, and B. de Crombrugghe. 1978. Decreased levels of collagen mRNA in Rous sarcoma virus-transformed chick embryo fibroblasts. J. Biol. Chem. 253:5869–5874.
   PubMed Web of Science ®Google Scholar
• Hunt, C., and R. I. Morimoto. 1985. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. USA 82:6455–6459.
   PubMed Web of Science ®Google Scholar
• Huynh, T. V., R. A. Young, and R. W. Davis. 1984. Constructing and screening cDNA library in λgt10 and λgt11, p. 49–68. In D. M. Glover (ed.), DNA cloning techniques: a practical approach. IRL Press, Oxford.
   Google Scholar
• Isaka, T., and M. Yoshida. 1975. Alterations in membrane polypeptides of chick embryo fibroblasts induced by transformation with avian sarcoma viruses. Virology 65:226–237.
   PubMedGoogle Scholar
• Krueger, J. G., E. Wang, and A. R. Goldberg. 1980. Evidence that the src gene product of Rous sarcoma virus is membrane associated. Virology 101:25–40.
   PubMedGoogle Scholar
• Kyte, L., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105–132.
   PubMed Web of Science ®Google Scholar
• Lee, A. S. 1987. Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem. Sci. 12:20–23.
   Web of Science ®Google Scholar
• Lemischka, I. R., S. Farmer, V. R. Racaniello, and P. A. Sharp. 1981. Nucleotide sequence and evolution of a mammalian a-tubulin messenger RNA. J. Mol. Biol. 151:101–120.
   PubMed Web of Science ®Google Scholar
• Limbach, K. J., and R. Wu. 1983. Isolation and characterization of two alleles of the chicken cytochrome c gene. Nucleic Acids Res. 11:8931–8949.
   PubMed Web of Science ®Google Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
   Google Scholar
• Matrisian, L. M., N. Glaichenhaus, M.-C. Gesnel, and R. Breathnach. 1985. Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts. EMBO J. 4:1435–1440.
   PubMed Web of Science ®Google Scholar
• Mayer, B. J., R. Jove, J. F. Krane, F. Poirier, G. Calothy, and H. Hanafusa. 1986. Genetic lesions involved in temperature sensitivity of the src gene products of four Rous sarcoma virus mutants. J. Virol. 60:858–867.
   PubMedGoogle Scholar
• Morimoto, R. I., C. Hunt, S.-Y. Huang, K. L. Berg, and S. S. Banergi. 1986. Organization, nucleotide sequence, and transcription of the chicken HSP70 gene. J. Biol. Chem. 261:1269212699.
   Google Scholar
• Munro, S., and H. R. B. Pelham. 1986. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46:291–300.
   PubMed Web of Science ®Google Scholar
• Munro, S., and H. R. B. Pelham. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899–907.
   PubMed Web of Science ®Google Scholar
• Olden, K., R. M. Pratt, C. Jaworski, and K. M. Yamada. 1979. Evidence for role of glycoprotein carbohydrates in membrane transport: specific inhibition by tunicamycin. Proc. Natl. Acad. Sci. USA 76:791–795.
   PubMed Web of Science ®Google Scholar
• Pelham, H. R. B. 1986. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46:959–961.
   PubMed Web of Science ®Google Scholar
• Peluso, R. W., R. A. Lamb, and P. W. Choppin. 1978. Infection with paramyxoviruses stimulates synthesis of cellular polypeptides that are also stimulated in cells transformed by Rous sarcoma virus or deprived of glucose. Proc. Natl. Acad. Sci. USA 75:6120–6124.
   PubMedGoogle Scholar
• Reitzer, L. R., B. M. Wice, and D. Kennell. 1980. The pentose cycle. J. Biol. Chem. 255:5616–5626.
   PubMed Web of Science ®Google Scholar
• Resendez, E., Jr., J. W. Attenello, A. Grafsky, C. S. Chang, and A. S. Lee. 1985. Calcium ionophore A21387 induces expression of glucose-regulated genes and their heterologous fusion genes. Mol. Cell. Biol. 5:1212–1219.
   PubMed Web of Science ®Google Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Scarpula, R. C., K. M. Agne, and R. Wu. 1981. Isolation and structure of a rat cytochrome c gene. J. Biol. Chem. 256:6480–6486.
   PubMedGoogle Scholar
• Shawver, L. K., S. A. Olson, M. D. White, and M. J. Weber. 1987. Degradation and biosynthesis of the glucose transporter protein in chicken embryo fibroblasts transformed by the src oncogene. Mol. Cell Biol. 7:2112–2118.
   PubMed Web of Science ®Google Scholar
• Shiu, R. P. C., and I. Pastan. 1979. Properties and purification of a glucose-regulated protein from chick embryo fibroblasts. Biochim. Biophys. Acta 576:141–150.
   PubMedGoogle Scholar
• Shiu, R. P. C., J. Pouyssegur, and I. Pastan. 1977. Glucose depletion accounts for the induction of two transformationsensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc. Natl. Acad. Sci. USA 74:3840–3844.
   PubMed Web of Science ®Google Scholar
• Stone, K. R., R. E. Smith, and W. K. Joklik. 1974. Changes in membrane polypeptides that occur when chick embryo fibroblasts and NRK cells are transformed with avian sarcoma viruses. Virology 58:86–100.
   PubMedGoogle Scholar
• Sugano, S., M. Y. Stoeckle, and H. Hanafusa. 1987. Transformation by Rous sarcoma virus induces a novel gene with homology to a mitogenic platelet protein. Cell 49:321–328.
   PubMed Web of Science ®Google Scholar
• Valenzuela, P., M. Quiroga, J. Zalvidar, W. J. Rutter, M. W. Kirschner, and D. W. Cleveland. 1981. Nucleotide and corresponding amino acid sequences encoded by α and β tubulin mRNAs. Nature (London) 289:650–655.
   PubMed Web of Science ®Google Scholar
• von Heijne, G. 1983. Patterns of amino acids near signalsequence cleavage sites. Eur. J. Biochem. 133:17–21.
   PubMedGoogle Scholar
• Welch, W. J., J. I. Garrels, G. P. Thomas, J. J.-C. Lin, and J. R. Feramisco. 1983. Biochemical characterization of the mammalian stress proteins and identification of two stress proteins as glucose-and Ca+2-ionophore-regulated proteins. J. Biol. Chem. 258:7102–7111.
   PubMed Web of Science ®Google Scholar
• Wice, B. M., L. J. Reitzer, and D. Kennell. 1981. The continuous growth of vertebrate cells in the absence of sugar. J. Biol. Chem. 256:7812–7819.
   PubMedGoogle Scholar
• Zehner, Z. E., and B. M. Paterson. 1983. Vimentin gene expression during myogenesis: two functional transcripts from a single copy gene. Nucleic Acids Res. 11:8317–8332.
   PubMedGoogle Scholar