Ionic permeability changes as the basis of the thermal dependence of the resting potential in barnacle muscle fibres

1. The thermal dependence of the resting potential of isolated barnacle muscle fibres was larger (1-2 mV/ degrees C) than predicted by Nernst's equation (about 0.2 mV/ degrees C). A comparative study was made of the influence on thermal dependence of parameters related to (a) passive permeability and to (b) Na extrusion.2. High [K](o) decreased the thermal dependence reversibly. [K(i)], [Na](i) and [Cl](i) were determined by chemical analysis, and Goldman's equation was fitted to data relating V to [K](o) at different temperatures, in the presence and absence of ouabain 5 x 10(-5)M. In both cases the behaviour of V when T was lowered from 20 to 4 degrees C was accounted for by increases in the calculated P(Na/PK) and P(Cl/PK) (from 0.006 to 0.043 and from 0.17 to 0.34 on the average, respectively.)3. Other parameters related to passive permeability (and which caused reversible depolarization): decreased [Cl](o) (methanesulphonate or gluconate substituted), and decreased pH(o) (below 5.0), also decreased the thermal dependence reversibly.4. Inhibitors (ouabain 5 x 10(-5)M, cyanide 2-10 x 10(-3)M, 2,4-dinitrophenol 2 x 10(-4)M) externally applied did not affect either resting potential or its thermal dependence for several hours.5. Increasing [Na](i) three- to fourfold by intracellular injection decreased both resting potential and its thermal dependence.6. Although a small effect by a Na electrogenic pump cannot be excluded, the largest part of the thermal effect on the resting potential is concluded to depend on temperature-induced variations in relative ionic permeabilities to cations and anions. A model is proposed which can account for the data assuming that (a) each permeant ion associates to a separate site in the membrane, and (b) the ion-site equilibrium is temperature-dependent.