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Response of malignant and nonmalignant epidermal cell lines to tunicamycin

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Summary

Exposure of fibroblasts to tunicamycin has been found to be cytotoxic for transformed cells, but not for nontransformed cells. With two mouse epidermal cell lines of common origin, we observe a contrary pattern: The malignant cells are more resistant to tunicamycin than their nonmalignant counterparts, as measured by growth and viability. With respect to the glycosylation of sugar precursors, the incorporation of mannose is more inhibited than that of glucosamine, while fucose is least impacted. Sugar incorporation is less reduced for the malignant cells, by a factor of two for fucose and more modestly for the other two sugars. There are no significant morphological changes; in particular, the desmosomal junctions are not affected. On polyacrylamide gels, we note intensity variations in several protein bands in response to tunicamycin, but little difference between malignant and nonmalignant cells when using either Coomassie stains or Concanavalin A overlays.

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References

  • Brysk MM, Snider JM (1982) Concanavalin A binding glycoproteins of epidermal cells. J Invest Dermatol 79:193–197

    Google Scholar 

  • Brysk MM, Miller J, Walker GK (1984) Characteristics of human epidermal squamous carcinoma cell line at different extra cellular calcium concentrations. Exp Cell Res 150:329–337

    Google Scholar 

  • Burridge K (1976) Changes in cellular glycoproteins after transformation: identification of specific glycoproteins and antigens in sodium dodecyl sulfate gels. Proc Natl Acad Sci USA 73:4457–4461

    Google Scholar 

  • Caulfield JB (1957) Effects of varying the vehicle for OsO4 in tissue fixation. J Biophys Biochem Cytol 3:827–830

    Google Scholar 

  • Chatterjee S, Kwiterovich PO Jr., Sekerke CS (1979) Effects of tunicamycin on the binding and degradation of low density lipoprotein and glycoprotein synthesis in cultured human fibroblasts. J Biol Chem 254:3704–3707

    Google Scholar 

  • Cohen SM, Gorbsky G, Steinberg MS (1983) Immunochemical characterization of related families of glycoproteins in desmosomes. J Biol Chem 258:2621–2627

    Google Scholar 

  • Damsky CH, Levy-Benshimol A, Buck CA, Warren L (1979) Effect of tunicamycin on the synthesis, intracellular transport and shedding of membrane glycoprotein in BHK cells. Exp Cell Res 119:1–13

    Google Scholar 

  • Duksin D, Bornstein P (1977) Changes in surface properties of normal and transformed cells caused by tunicamycin, an inhibitor of protein glycosylation. Proc Natl Acad Sci USA 74:3433–3437

    Google Scholar 

  • Heifetz A, Lennarz WJ (1979) Biosynthesis of N-glycosidically linked glycoproteins during gastrulation of sea urchin embryos. J Biol Chem 254:6119–6127

    Google Scholar 

  • Hickman S, Kulszycki A, Lynch RG, Kornfeld S (1977) Studies of the mechanism of tunicamycin inhibition of IgA and IgE secretion by plasma cells. J Biol Chem 252:4402–4408

    Google Scholar 

  • Horowitz MI (1977) Purification of glycoproteins and criteria of purity. In: Horowitz MI, Pigman W (eds) The glycoconjugates. Vol. 1. Mammalian glycoproteins and glycolipids. Academic Press, New York San Francisco London, pp 15–50

    Google Scholar 

  • Hughes RC (1976) Membrane glycoproteins and growth control. In: Membrane glycoproteins. Butterworth, London, pp 269–284

    Google Scholar 

  • Hughes RC, Meager A, Nairn R (1977) Effect of 2-deoxy-D-glucose on the cellsurface glycoproteins of hamster fibroblasts. Eur J Biochem 72:265–273

    Google Scholar 

  • Hughes RC, Pena SDJ, Vischer P (1980) Cell surface glycoproteins in fibroblast adhesion. In: Curtis ASG, Pitts JD (eds) Cell adhesion and motility. Cambridge University Press, Cambridge, pp 329–356

    Google Scholar 

  • Irimura T, Gonzalez R, Nicolson GH (1981) Effects of tunicamycin on B16 metastatic melanoma cell surface glycoproteins and blood-borne arrest and survival properties. Cancer Res 41:3411–3418

    Google Scholar 

  • King IA, Tabiowo A (1981) Effect of tunicamycin on epidermal glycoprotein and glycosaminoglycan synthesis in vitro. Biochem J 198:331–338

    Google Scholar 

  • Kohno K, Hiragun A, Mitsui H, Takatsuki A, Tamura G (1979) Effect of tunicamycin on cell growth and morphology of nontransformed and transformed cell lines. Agricult Biol Chem 43:1553–1561

    Google Scholar 

  • Kornfeld R, Kornfeld S (1980) Structure of glycoproteins and their oligosaccharide units. In: Lennarz WJ (ed) The Biochemistry of glycoproteins and proteoglycans. Plenum Press, New York, PP 1–27

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    PubMed  Google Scholar 

  • Lam TY, Siu CH (1982) Inhibition of cell differentiation and cell adhesion by tunicamycin in Dictyostelium discoideum. Dev Biol 92:398–407

    Google Scholar 

  • Leavitt R, Schlesinger S, Kornfeld S (1977) Impaired intracellular migration and altered solubility of nonglycosylated glycoproteins of vesicular stomatitis virus and Sindbis virus. J Biol Chem 252:9018–9023

    Google Scholar 

  • Lever JA, Sari CE (1983) Effect of tunicamycin on polarized membrane functions of an established kidney epithelial cell line. Biochim Biophys Acta 762:265–271

    Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275

    CAS  PubMed  Google Scholar 

  • Michaels JE (1980) Alterations in the distribution of glycoproteins in epithelial cells of murine colon after injection of tunicamycin. Cell Tissue Res 210:121–132

    Google Scholar 

  • Morin MJ, Porter CW, McKernan P, Bernacki RJ (1983) The biochemical and ultrastructural effects of tunicamycin and Dglucosamine in L1210 leukemic cells. J Cell Physiol 114:162–172

    Google Scholar 

  • Nishikawa Y, Yammamoto Y, Onodera K, Tamura G, Mitsui H (1979) Altered molecular structure of HLA-DR antigens synthesized in the presence of tunicamycin. Biochem Biophys Res Commun 87:1235–1242

    Google Scholar 

  • Olden K, Pratt RM, Yamada KM (1978) Role of carbohydrates in protein secretion and turnover: Effects of tunicamycin on the major cell surface glycoproteins of chick embryo fibroblasts. Cell 13:461–473

    Google Scholar 

  • Olden K, Pratt RM, Jaworski C, Yamada K (1979 a) Evidence for role of glycoprotein carbohydrates in membrane transport: specific inhibition by tunicamycin. Proc Natl Acad Sci USA 76:791–795

    Google Scholar 

  • Olden K, Pratt RM, Yamada KM (1979 b) Selective cytotoxicity of tunicamycin for transformed cells. Int J Cancer 24:60–66

    Google Scholar 

  • Olden K, Hahn EL, Yamada KM (1980) Fibronectin: properties and role in cellular morphology and adhesion. In: Curtis ASG, Pitts JD (eds) Cell adhesion and motility. Cambridge University Press, Cambridge, pp 357–387

    Google Scholar 

  • Olden K, Law J, Hunter VA, Romain R, Parent JB (1981) Inhibition of fusion of embryonic muscle cells in culture by tunicamycin is prevented by leupeptin. J Cell Biol 88:199–204

    Google Scholar 

  • Olden K, Bernard BA, White SL, Parent JB (1982 a) Function of the carbohydrate moieties of glycoproteins. J Cell Biochem 18:313–335

    Google Scholar 

  • Olden K, Parent JB, White SL (1982 b) Carbohydrate moieties of glycoproteins: A re-evaluation of their function. Biochim Biophys Acta 650:209–232

    Google Scholar 

  • Overton J (1982) Inhibition of desmosome formation with tunicamycin and with lectin in corneal cell aggregates. Dev Biol 92:66–72

    Google Scholar 

  • Pouyssegur JM, Pastan I (1977) Mutants of mouse fibroblasts altered in the synthesis of cell surface glycoproteins. J Biol Chem 252:1639–1646

    Google Scholar 

  • Ray DA, Gibor A (1982) Tunicamycin-sensitive glycoproteins involved in the mating of Chlamydomonas reinhardi. Exp Cell Res 141:245–252

    Google Scholar 

  • Rosen OM, Chia GH, Fung C, Rubin CS (1979) Tunicamycinmediated depletion of insulin receptors in 3T3-L1 adipocytes. J Cell Physiol 99:37–42

    Google Scholar 

  • Schachter H, Narasimhan S, Gleeson P, Vella G (1983) Control of branching during the biosynthesis of asparagine-linked oligosaccharides. Can J Biochem Cell Biol 61:1049–1066

    Google Scholar 

  • Schwarz RT, Datema R (1982) Inhibition of lipid-dependent glycosylation In: Horowitz MI (ed) The glycoconjugates. Academic Press, New York, pp 46–79

    Google Scholar 

  • Thesleff I, Pratt RM (1980) Tunicamycin inhibits mouse tooth morphogenesis and odontoblast differentiation in vitro. J Embryol Exp Morphol 58:195–208

    Google Scholar 

  • Tkacz JS, Lampen JO (1975) Tunicamycin inhibition of polyisoprenyl N-acetyl-glucosaminyl pyrophosphate formation in calf-liver microsomes. Biochem Biophys Res Commun 65:248–257

    Google Scholar 

  • Waechter CJ, Lennarz WJ (1976) The role of polyprenol-linked sugars in glycoprotein synthesis. Ann Rev Biochem 45:95–112

    Google Scholar 

  • Watanabe K, Tamura G, Mitsui H (1979) Effects of tunicamycin on the proliferation, adhesion and differentiation of chick embryo chondrocytes in clonal cell cultures. Cell Struct Funct 4:127–134

    Google Scholar 

  • Yuspa SH, Hawley-Nelson P, Koehler B, Stanley JR (1980) A survey of transformation markers in differentiating epidermal cell lines in culture. Cancer Res 40:4694–4703

    Google Scholar 

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Brysk, M.M., Miller, J., Chen, SJ. et al. Response of malignant and nonmalignant epidermal cell lines to tunicamycin. Cell Tissue Res. 245, 215–221 (1986). https://doi.org/10.1007/BF00218103

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