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Cell and Organelle Structure and Assembly

Enhanced Transcription of the 78,000-Dalton Glucose-Regulated Protein (GRP78) Gene and Association of GRP78 with Immunoglobulin Light Chains in a Nonsecreting B-Cell Myeloma Line (NS-1)

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Pages 2233-2238 | Received 09 Nov 1988, Accepted 27 Jan 1989, Published online: 31 Mar 2023

LITERATURE CITED

  • Artishevsky, A., A. M. Delegeane, and A. S. Lee. 1984. Use of a cell cycle mutant to delineate the critical period for the control of histone mRNA levels in the mammalian cell cycle. Mol. Cell. Biol. 4:2364–2369.
  • Artishevsky, A., S. Wooden, A. Sharma, E. Resendez, Jr., and A. S. Lee. 1987. Cell cycle regulatory sequences in a hamster histone promoter and their interactions with cellular factors. Nature (London) 328:823–827.
  • Bole, D. G., L. M. Hendershot, and J. F. Kearney. 1986. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J. Cell Biol. 102:1558–1566.
  • Bos, T. J., D. Bohmann, H. Tsuchie, R. Tijan, and P. K. Vogt. 1988. v-jun encodes a nuclear protein with enhancer binding properties of AP-1. Cell 52:705–712.
  • Chirico, W. J., M. G. Waters, and G. Blobel. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature (London) 332:805–810.
  • Cowan, N. J., D. S. Secher, and L. Milstein. 1974. Intracellular immunoglobulin chain synthesis in non-secreting variants of a mouse myeloma: detection of inactive light-chain messenger RNA. J. Mol. Biol. 90:691–701.
  • Deans, R. J., K. A. Denis, A. Taylor, and R. Wall. 1984. Expression of an immunoglobulin heavy chain gene transfected into lymphocytes. Proc. Natl. Acad. Sci. USA 81:1291–1296.
  • Deshaies, R. J., B. D. Koch, M. Werner-Washburne, E. A. Craig, and R. Schekman. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature (London) 332:800–805.
  • Dorner, A. J., D. G. Bole, and R. J. Kaufman. 1987. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J. Cell Biol. 105:2665–2674.
  • Feige, J.-J., G.-A. Keller, and I. E. Scheffler. 1988. Temperature-sensitive Chinese hamster cell mutant with a defect in glycoprotein synthesis: accumulation of the EGF receptor in the endoplasmic reticulum and the role of the glucose-regulated protein GRP78. J. Cell. Physiol. 136:33–42.
  • Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
  • Gething, M.-J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: a role of folding in intracellular transport. Cell 46:939–950.
  • Hass, I. G., and M. Wabl. 1983. Immunoglobulin heavy chain binding protein. Nature (London) 306:387–389.
  • Hendershot, L. M., and J. F. Kearney. 1988. A role for human heavy chain binding protein in the developmental regulation of immunoglobulin transport. Mol. Immun. 25:585–595.
  • Hendershot, L. M., J. Ting, and A. S. Lee. 1988. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. Mol. Cell. Biol. 8:4250–4256.
  • Horibata, K., and A. W. Harris. 1970. Mouse myelomas and lymphomas in culture. Exp. Cell Res. 60:61–77.
  • Kassenbrock, C. K., P. D. Garcia, P. Walter, and R. B. Kelly. 1988. Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro. Nature (London) 333:90–93.
  • Kim, K. S., and A. S. Lee. 1986. The effect of extracellular Ca2+ and temperature on the induction of the heat-shock and glucoseregulated proteins in hamster fibroblasts. Biochem. Biophys. Res. Commun. 140:881–887.
  • Kim, Y. K., and A. S. Lee. 1987. Transcriptional activation of the glucose-regulated protein genes and their heterologous fusion genes by β-mercaptoethanol. Mol. Cell. Biol. 7:2974–2976.
  • Klotz, J. L., M. L. Philips, M. M. Miller, and R. L. Teplitz. 1981. Monoclonal autoantibody production by hybrid cell lines. Clin. Immunol. Immunopathol. 18:368–374.
  • Knopf, P. M., A. Destree, and R. Hyman. 1973. Antibody-induced changes in expression of an immunoglobulin surface antigen. Eur. J. Immunol. 3:251–259.
  • Kozutsumi, Y., M. Segal, K. Normington, M.-J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature (London) 332:462–464.
  • Kwan, S.-P., S. Rudikoff, J. G. Seidman, P. Leder, and M. D. Scharff. 1981. Nucleic acid and protein sequences of phospho-choline-binding light chains. J. Exp. Med. 153:1366–1370.
  • Lee, A. S.. 1981. The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12. J. Cell. Physiol. 106:119–125.
  • 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.
  • Lee, A. S., A. M. Delegeane, V. Baker, and P. C. Chow. 1983. Transcriptional regulation of two genes specifically induced by glucose starvation in a hamster mutant fibroblast cell line. J. Biol. Chem. 258:597–603.
  • Lin, A. Y., and A. S. Lee. 1984. Induction of two genes by glucose starvation in hamster fibroblasts. Proc. Natl. Acad. Sci. USA 81:988–992.
  • Mazzarella, R. A., and M. Green. 1987. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J. Biol. Chem. 262:8875–8883.
  • Munro, S., and H. R. B. Pelham. 1986. An hsp 70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46:291–300.
  • Resendez, E., Jr., J. W. Attenello, A. Grafsky, C. S. Chang, and A. S. Lee. 1985. Calcium ionophore A23187 induces expression of glucose-regulated genes and their heterologous fusion genes. Mol. Cell. Biol. 5:1212–1219.
  • Ting, J., S. K. Wooden, R. Kriz, K. Kelleher, R. J. Kaufman, and A. S. Lee. 1987. The nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat. Gene 55:147–152.
  • Wooden, S. K., R. P. Kapur, and A. S. Lee. 1988. The organization of the rat GRP78 gene and A23187-induced expression of fusion gene products targeted intracellularly. Exp. Cell Res. 178:84–92.

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