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Título: | Cd2+ regulation of the hyperpolarization-activated current I(AB) in crayfish muscle |
Autor: | Araque, Alfonso CSIC ORCID; Cattaert, D.; Buño, Washington CSIC | Fecha de publicación: | 1995 | Editor: | Rockefeller University Press | Citación: | Journal of General Physiology 105: 725-744 (1995) | Resumen: | The effects of Cd2+ on the hyperpolarization-activated K+-mediated current called I(AB) (Araque, A., and W. Buno. 1994. Journal of Neuroscience. 14:399-408.) were studied under two-electrode voltage-clamp in opener muscle fibers of the crayfish Procambarus clarkii. I(AB) was reversibly reduced by extracellular Cd2+ in a concentration-dependent manner, obeying the Hill equation with IC50 = 0.452 ± 0.045 mM and a Hill coefficient of 1 (determined from the maximal chord conductance of I(AB)). Cd2+ decreased the I(AB) conductance (G(AB)) and shifted its voltage dependence towards hyperpolarized potentials in a similar degree, without affecting the slope of the voltage dependence. The I(AB) activation time constant increased, whereas the I(AB) deactivation time constant was not modified by Cd2+. The I(AB) equilibrium potential (E(AB)) was unmodified by Cd2+, indicating that the selective permeability of I(AB) channels was not altered. I(AB) was unaffected by intracellular Cd2+. The Cd2+-regulation of I(AB) did not depend on [K+](o), and the effects of [K+](o), on I(AB) were unchanged by Cd2+, indicating that Cd2+ did not compete with K+. Therefore, Cd2+ probably bound to a different site to that involved in the K+ permeability pathway. We conclude that Cd2+ affected the gating of I(AB) channels, interfering with their opening but not with their closing mechanism. The results can be explained by a kinetic model in which the binding of Cd2+ to the I(AB) channels would stabilize the gating apparatus at its resting position, increasing the energy barrier for the transition from the closed to the open channel states. | URI: | http://hdl.handle.net/10261/60764 | DOI: | 10.1085/jgp.105.6.725 | Identificadores: | doi: 10.1085/jgp.105.6.725 issn: 0022-1295 |
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