Summary
Previous studies have suggested that gap junctions may have a role in various uterine functions, including parturition. Because nickel has been demonstrated to increase uterine contractility in vitro, the effect of nickel (II) chloride on gap junctional communication was assessed in a tumorigenic uterine cell line, SK-UT-1 (ATCC HTB 114). Cells were exposed in vitro to 25 and 50 µM NiCl2 for 24 h or 100 µM NiCl2 for 3, 12, and 24 h, then functional gap junctional communication was measured as the transfer of Lucifer yellow dye from microinjected donor cells to their primary neighbor cells. Dye transfer was significantly increased only in cell cultures exposed to 100 µM NiCl2 for 24h, compared to untreated controls, lower doses, and shorter exposure periods. This response was inhibited by the simultaneous co-treatment of SK-UT-1 cells with magnesium by adding 100 µM MgSO4 to the dosing medium. Possible mechanisms and implications for these findings are discussed.
Similar content being viewed by others
References
Azumi, N.; Ben-Ezra, J.; Battifora, H. Immunophenotypic diagnosis of leiomyosarcomas and rhabdomyosarcomas with monoclonal antibodies to muscle-specific actin and desmin in formalin-fixed tissue. Mod. Pathol. 1:469–474; 1988.
Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254; 1976.
Birukov, K. G.; Stephanova, O. V.; Nanaev, A. K., et al. Expression of calponin in rabbit and human aortic smooth muscle cells. Cell Tissue Res. 266:579–584; 1991.
Buss, W. C.; Frank, G. B. Calcium and excitation-contraction coupling in mammalian skeletal muscle. Arch. Int. Pharmacodyn. 181(1):15–26; 1969.
Bussolati, G.; Papotti, M.; Foschini, M. P., et al. The interest of actin immunocytochemistry in diagnostic histopathology. Basic Appl. Histochem. 31:165–176; 1987.
Caruso, R.; Juberg, D. R.; Caldwell, V., et al. Cultured myometrial cells establish communicating gap junctions. Cell Biol. Int. Rep. 14:905–916; 1990.
Cormane, R. H.; Spruit, D.; Kuiper, J. P. Stimulation of enzyme activity in the uterus of the guinea pig by nickel ions. Acta Physiol. Pharmacol. Neerl. 14:443–447; 1967.
De Mello, W. C. Modulation of junctional permeability. In: De Mello, W. C., ed. Cell-to-cell communication. New York: Plenum Press; 1987:29–64.
Demianczuk, N.; Towell, M. E.; Garfield, R. E. Myometrial electrophysiological activity and gap junctions in the pregnant rabbit. Am. J. Obstet. Gynecol. 149:485–491; 1984.
Fischman, D. A.; Swan, R. C. Nickel substitution for calcium in excitation-contraction coupling of skeletal muscle. J. Gen. Physiol. 50:1709–1728; 1967.
Freshney, R. I. Culture of animal cells: a manual of basic technique, 2nd ed. New York: Alan R. Liss, Inc.; 1987:70–71.
Garfield, R. E.; Hayashi, R. H. Appearance of gap junctions in the myometrium of women during labor. Am. J. Obstet. Gynecol. 140:254–260; 1981.
Garfield, R. E.; Sims, S.; Daniel, E. E. Gap junctions: their presence and necessity in myometrium during parturition. Science 198:958–960; 1977.
Garfield, R. E.; Sims, S. M.; Kannan, M. S., et al. Possible role of gap junctions in activation of myometrium during parturition. Am. J. Physiol. 235:C168-C179; 1978.
Garfield, R. E.; Ratrideau, S.; Challis, J. R. G., et al. Hormonal control of gap junction formation in sheep myometrium during parturition. Biol. Reprod. 21:999–1007; 1979.
Garfield, R. E.; Cole, W. C.; Blennerhassett, M. G. Gap junctions in uterine smooth muscle. In: Sperelakis, N.; Cole, W. C., eds. Cell interactions and gap junctions, vol. 2. Boca Raton, FL: CRC Press; 1989:239–266.
Goulet, F.; Normand, C.; Morin, O. Cellular interactions promote tissuespecific function, biomatrix deposition and junctional communication of primary cultured hepatocytes. Hepatology 8:1010–1018; 1988.
Kalimi, G. H.; Lo, C. W. Communication compartments in the gastrulating mouse embryo. J. Cell Biol. 107:241–255; 1988.
Madden, C.; Owen, J.; Hauth, J. C. Magnesium tocolysis: serum levels versus success. Am. J. Obstet. Gynecol. 162:1177–1180; 1990.
Mikalsen, S. Effects of heavy metal ions on intercellular communication in Syrian hamster embryo cells. Carcinogenesis 11:1621–1626; 1990.
Miki, H.; Kasprzak, K. S.; Kenney, S., et al. Inhibition of intercellular communication by nickel(II): antagonistic effect of magnesium. Carcinogenesis 8(11):1757–1760; 1987.
Peaceman, A. M.; Meyer, B. A.; Thorp, J. A., et al. The effect of magnesium sulfate tocolysis on the fetal biophysical profile. Am. J. Obstet. Gynecol. 161:771–774; 1989.
Richardson, M. R.; Taylor, D. A.; Casey, M. L., et al. Biochemical markers of contraction in human myometrial smooth muscle cells in culture. In Vitro Cell. Dev. Biol. 23:21–28; 1987.
Rubanyi, G.; Balogh, I. Effect of nickel on uterine contraction and ultrastructure in the rat. Am. J. Obstet. Gynecol. 142(8):1016–1020; 1982.
Rubanyi, G.; Inovay, J. Effect of nickel ions on spontaneous, electrically and norepinephrine stimulated isometric contractions in the isolated portal vein of the rat. Acta Physiol. Acad. Sci. Hung. 59(2):181–186; 1982.
Ruch, R. J.; Klaunig, J. E. Kinetics of phenobarbital inhibition of intercellular communication in mouse hepatocytes. Cancer Res. 48:2519–2523; 1988.
Schild, H. O. The effect of metals on the S-S polypeptide receptor in depolarized rat uterus. Br. J. Pharmacol. 36:329–349; 1969.
Schurch, W.; Skalli, O.; Seemayer, T. A., et al. Intermediate filament proteins and actin isoforms as markers for soft tissue tumor differentiation and origin. I. Smooth muscle tumors. Am. J. Pathol. 128:91–103; 1987.
Smith, J. B.; Cragoe, E. J.; Smith, L. Na+/Ca2+ antiport in cultured arterial smooth muscle cells. Inhibition by magnesium and other divalent cations. J. Biol. Chem. 262:11988–11994; 1987.
Spruit, D.; Kuiper, J. P. The interaction of some metal ions with the uterus of the guinea pig. Acta Physiol. Pharmacol. Neerl. 14:434–442; 1967.
Stewart, W. W. Functional connections between cells as revealed by dyecoupling with a highly fluorescent naphthalimide tracer. Cell 14:741–759; 1978.
U.S. Assembly of Life Sciences Committee on Medical and Biological Effects of Environmental Pollutants. Nickel. Washington, DC: National Academy of Sciences; 1975:62–96.
Warner, A. E.; Guthrie, S. C.; Gilula, N. B. Antibodies to gap-junctional protein selectively disrupt junctional communication in the early amphibian embryo. Nature 311:127–131; 1984.
Watanabe, K.; Saito, A.; Wakabayashi, H., et al. Two autopsy cases of primary leiomyosarcoma of the liver. Superiority of muscle-specific actin immunoreactivity in diagnosis. Acta Pathol. Jpn. 41:461–465; 1991.
Yamasaki, H.; Enomoto, T.; Shiba, Y., et al. Intercellular communication capacity as a possible determinant of transformation sensitivity of BALB/c 3T3 clonal cells. Cancer Res. 45:637–641; 1985.
Yamasaki, H.; Hollstein, M.; Mesnil, M., et al. Selective lack of intercellular communication between transformed and nontransformed cells as a common property of chemical and oncogene transformation of BALB/c 3T3 cells. Cancer Res. 47:5658–5664; 1987.
Zidell, R. H.; Loch-Caruso, R. A simple dye-coupling assay for evaluating gap junctional communication: the importance of transcription and translation on the establishment of dye-coupling. Cell Biol. Int. Rep. 14:613–628; 1990.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Marty, M.S., Loch-caruso, R. Nickel-induced increases in gap junctional communication in the uterine cell line SK-UT-1. In Vitro Cell Dev Biol - Animal 29, 215–220 (1993). https://doi.org/10.1007/BF02634186
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02634186