Abstract
Metal-binding chelators may interact with biological systems by either of two mechanisms: they may combine with an essential metal, which can be either freely dissociated or part of an enzyme prosthetic group, or they may react with a metal ion to form a biologically reactive metal–chelate complex1. As trace metals are always present as contaminants in serum-supplemented culture media used to study chelating agents, it is frequently difficult to distinguish between the two possibilities. Here we describe the use of a nontoxic, copper-specific chelating agent, bathocuproine sulphonate2,3 (Fig. 1) which, by combining with available endogenous copper in a tissue culture preparation, abolished the toxicity of three structurally unrelated chelating agents. These three agents may therefore be considered to be biologically active by the second mechanism.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Albert, A. in Selective Toxicity 5th edn, 334–391 (Chapman & Hall, London, 1972).
Blair, D. & Diehl, H. Talanta 7, 163–174 (1961).
Landers, J. W. & Zak, B. Am. J. clin. Path. 29, 590–592 (1958).
Thorn, G. D. & Ludwig, R. A. The Dithiocarbamates and Related Compounds, 169–192 (Elsevier, Amsterdam, 1962).
Reid, E. E. Organic Chemistry of Bivalent Sulfur Vol. 4, 196–256 (Chemical Publishing, New York, 1962).
Rigas, D. A., Eginitis-Rigas, C., Bigley, R. H., Stankova, L. & Head, C. Int. J. Radiat. Biol. 38, 257–266 (1980).
Heikkila, R. E., Cabbat, F. S. & Cohen, G. J. biol. Chem. 251, 2182–2185 (1976).
Pottathil, R., Chandrabose, K. A., Cuatrecasas, P. & Lang, D. J. Proc. natn. Acad. Sci. U.S.A. 78, 3343–3347 (1981).
Booth, B. A. & Sartorelli, A. C. Molec. Pharmac. 3, 290–302 (1967).
Van Giessen, G. J., Crim, J. A., Petering, D. H. & Petering, H. G. J. natn. Cancer Inst. 51, 139–146 (1973).
Berger, N. A., Johnson, E. S. & Skinner, A. M. Sr. Expl Cell Res. 96, 145–155 (1975).
Falchuk, K. H. & Krishan, A. Cancer Res. 37, 2050–2056 (1977).
James, B. R. & Williams, R. J. P. J. chem. Soc. 2007–2019 (1961).
Hall, J. R., Marchant, N. K. & Plowman, R. A. Aust. J. Chem. 16, 34–41 (1962).
Murthy, Y. K. S., Thiemann, J. E., Coronelli, C. & Semsi, P. Nature 211, 1198 (1966).
Powis, G. & Kovach, J. S. Biochem. Pharmac. 30, 771–776 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Mohindru, A., Fisher, J. & Rabinovitz, M. Bathocuproine sulphonate: a tissue culture-compatible indicator of copper-mediated toxicity. Nature 303, 64–65 (1983). https://doi.org/10.1038/303064a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/303064a0
- Springer Nature Limited
This article is cited by
-
Mutation of copper binding sites on cellular prion protein abolishes its inhibitory action on NMDA receptors in mouse hippocampal neurons
Molecular Brain (2021)
-
Investigation of the effects of the proton transfer salts of 2-aminopyridine derivatives with 5-sulfosalicylic acid and their Cu(II) complexes on cancer-related carbonic anhydrases: CA IX and CA XII
Chemical Papers (2020)
-
Differential modulation of NMDA and AMPA receptors by cellular prion protein and copper ions
Molecular Brain (2018)
-
Photo-catalytic degradation of methylene blue over nano titanium/nickel oxide prepared from supported Schiff base complex on titanium dioxide
Journal of Materials Science: Materials in Electronics (2016)
-
Dielectrical properties and conduction mechanism of quinoline Schiff base and its complexes
Research on Chemical Intermediates (2016)