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Research Article

Nuclear T3 Receptor : Depletion by Tunicamycin Despite the Absence of N-Linked Glycan Units in a Murine Preadipocyte Cell Line and Rat Liver

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Pages 683-698 | Published online: 26 Sep 2008

References

  • Towle H. C. Effects of thyroid hormones on cellular RNA metabolism. Molecular basis of thyroid hormone action, J. H. Oppenheimer, H. H. Samuels. Acad. Press, N.Y. 1983; 179–212
  • Oppenheimer J. H. Thyroid hormone action at the nuclear level. Ann. Intern. Med. 1985; 102: 374–384
  • Gharbi-Chihi J., Chabaud O., Torresani J. The role of triiodothyronine in the regulation of synthesis rate and translatable mRNA level of fatty acid synthetase in a preadipocyte cell line. Biochim. Biophys. Acta 1984; 783: 26–35
  • Nyborg J. K., Nguyen A. P., Spindler S. R. Relationship between thyroid and glucocorticoid hormone receptor occupancy, growth hormone gene transcription and mRNA accumulation. J. Biol. Chem. 1984; 259: 12377–12381
  • Yaffe B. M., Samuels H. H. Hormonal regulation of the growth hormone gene: relationship of the rate of transcription to the level of nuclear thyroid hormone-receptor complexes. J. Biol. Chem. 1984; 259: 6284–6291
  • Torresani J., Anselmet A., Wahl R. Properties of solubilized nuclear triiodothyronine binding proteins. Molec. Cell. Endocrinol. 1978; 9: 321–333
  • Bismuth J., Anselmet A., Torresani J. Triiodothyronine nuclear receptor: role of non-histone protein factors in vitro triiodothyronine binding. Biochim. Biophys. Acta 1985; 840: 271–279
  • Perlman A. J., Stanley F., Samuels H. H. Thyroid hormone nuclear receptor: evidence for multimeric organization in chromatin. J. Biol. Chem. 1982; 257: 930–938
  • Anselmet A., Gharbi-Chihi J., Torresani J. Nuclear triiodothyronine receptor in differentiating preadipocytes cloned from obese and lean mice. Endocrinology 1984; 114: 450–456
  • Casanova J., Horowitz Z. D., Copp R. P., Mc Intyre W. R., Pascual A., Samuels H. H. Photoaffinity labeling of thyroid hormone nuclear receptors. J. Biol. Chem. 1984; 259: 12084–12091
  • Dozin B., Cahnmann H. J., Nikodem V. Identification of thyroid hormone receptors in rat liver nuclei by photoaffinity labeling with L-thyroxine and triiodo-L-thyronine. Biochemistry 1985; 24: 5197–5202
  • Sap J., Munoz A., Damm K., Goldberg Y., Ghysdael J., Leutz A., Beug H., Vennström B. The c-erb-A protein is a high affinity receptor for thyroid hormone. Nature 1986; 324: 635–640
  • Weinberger C., Thompson C. C., Ong E. S., Lebo R., Gruol D. J., Evans R. M. The c-erb-A gene encodes a thyroid hormone receptor. Nature 1986; 324: 641–646
  • Green S., Chambon P. A superfamily of potentially oncogenic hormone receptors. Nature 1986; 324: 615–617
  • Reeves R., Chang D., Chung S. Carbohydrate modifications of the high mobility group proteins. Proc. Natl. Acad. Sci. USA 1981; 78: 6704–6708
  • Levy-Wilson B. Glycosylation, ADP-ribosylation and methylation of Tetrahymena histones. Biochemistry 1983; 22: 484–489
  • Hähnel R., Twaddle E., Brindle L. The influence of enzymes on the oestrogen receptors of human uterus and breast carcinoma. Steroids 1974; 24: 489–506
  • Blanchardie P., Lustenberger P., Denis M., Orsonneau J. L., Bernard S. Interaction of rat liver glucocorticoid receptor with lectins: is the glucocorticoid receptor a glycoprotein. J. Ster. Biochem. 1986; 24: 263–267
  • Tkacz J. S., Lampen J. O. Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf liver microsomes. Biochem. Biophys. Res. Commun. 1975; 65: 248–257
  • Negrel R., Grimaldi P., Ailhaud G. Establishment of preadipocyte clonal line from epididymal fat pad of ob/ob mouse that responds to insulin and to lipolytic hormones. Proc. Natl. Acad. Sci. USA 1978; 75: 6054–6058
  • Labarca C., Paigen K. A simple, rapid and sensitive DNA assay procedure. Anal. Biochem. 1980; 102: 344–352
  • Tulsiani D. R.P., Touster O. Swainsonine causes the production of hybrid glycoproteins by human skin fibroblasts and rat liver Golgi preparations. J. Biol. Chem. 1983; 258: 7578–7585
  • Franc J. L., Hovsépian S., Fayet G., Bouchilloux S. Inhibition of N-linked oligosaccharide processing does not prevent the secretion of thyroglobulin. Eur. J. Biochem. 1986; 157: 225–232
  • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976; 72: 248–254
  • Dulaney J. T. Factors affecting the binding of glycoproteins to concanavalin A and Ricinus communis agglutinin and the dissociation of their complexes 1979; 99: 254–267
  • Krusius T., Finne J., Rauvala H. The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin A-Sepharose. FEBS Lett. 1976; 71: 117–120
  • Narasimhan S., Wilson J. R., Martin E., Schachter H. A structural basis for four distinct elution profiles on concanavalin A-Sepharose affinity chromatography of glycopeptides. Canad. J. Biochem. 1979; 57: 83–96
  • Kornfeld K., Reitman M. L., Kornfeld R. The carbohydrate-binding specificity of pea and lentil lectins. J. Biol. Chem. 1981; 256: 6633–6640
  • Debray H., Pierce-Cretel A., Spik G., Montreuil J. Affinity of ten insolubilized lectins towards various glycopeptides with the N-glycosylamine linkage and related oligosaccharides. Lectins III, T. C. Bog-Hansen, G. A. Sprengler. De Gruyter, Berlin 1983; 335–350
  • Yamamoto K., Tsuji T., Matsumoto I., Osawa T. Structural requirements for the binding of oligosaccharides and glycopeptides to immobilized wheat germ agglutinin. Biochemistry 1981; 20: 5894–5899
  • Yamashita K., Hitoi A., Kobata A. Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides. J. Biol. Chem. 1983; 258: 14753–14755
  • Baenziger J. U., Fiete D. Structural determinants of Ricinus Communis agglutinin and toxin specificity for oligosaccharides. J. Biol. Chem. 1979; 254: 9795–9799
  • Seve A. P., Hubert J., Bouvier D., Masson C., Geraud G., Bouteille M. In situ distribution in different cell types of nuclear glycoconjugates detected by two lectins. J. Submicrosc. Cytol. 1984; 4: 631–641
  • Hollenberg S. M., Weinberger C., Ong E. S., Cerelli G., Oro A., Lebo R., Thompson E. B., Rosenfeld M., Evans R. M. Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature 1985; 318: 635–641
  • Krust A., Green S., Argos P., Kumar V., Walter P., Bornet J. P., Chambon P. The chicken oestrogen receptor sequence; homology with v-erb-A and the human oestrogen and glucocorticoid receptor. The EMBO J. 1986; 5: 891–897
  • Loosfelt H., Atger M., Misrahi M., Guiochon-Mantel A., Meriel C., Logeat F., Benarous R., Milgrom E. Cloning and sequence analysis of rabbit progesterone receptor complementary DNA. Proc. Natl. Acad. Sci. USA 1986; 83: 9045–9049
  • Holt G. D., Hart G. W. The subcellular distribution of terminal N-acetylglucosamine moieties. J. Biol. Chem. 1986; 261: 8049–8057
  • Pou M. A., Bismuth J., Gharbi-Chihi J., Torresani J. Triiodothyronine-induced down-regulation of the nuclear T3 receptor in mouse preadipocyte cell lines. Endocrinology 1986; 119: 2360–2367
  • DeGroot L. J., Coleoni A. H., Rue P. A, Seo H., Martino E., Refetoff S. Reduced nuclear triiodothyronine receptors in starvation-induced hypothyroidism. Biochem. Biophys. Res. Commun. 1977; 79: 173–178
  • Bismuth J., Gharbi-Chihi J., Pou M. A., Torresani J. Modulation of the nuclear T3 receptor in mouse preadipocyte cell lines. Ann. Endocrinol. 1986; 47: 44A

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