## Abstract The effect of Ca^+2^ on the transport and intracellular distribution of Na^+^ and K^+^ in Ehrlich ascites tumor cells was investigated in an effort to establish the mechanism of Ca^+2^โinduced hyperpolarization of the cell membrane. Inclusion of Ca^+2^ (2mM) in the incubation medium lea
Variable coupling of active NA+ + K+ transport in Ehrlich ascites tumor cells: Regulation by external NA+ and K+
โ Scribed by Thomas C. Smith; Susan C. Robinson
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 884 KB
- Volume
- 106
- Category
- Article
- ISSN
- 0021-9541
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โฆ Synopsis
Abstract
The effects of altered external sodium and potassium concentrations on steady state, active Na^+^ + K^+^ transport in Ehrlich ascites tumor cells have been investigated. Membrane permeability to Na^+^ and K^+^, intracellular [Na^+^] and [K^+^], and membrane potential were measured. Active cation fluxes were calculated as equal and membrane potential were measured. Active cation fluxes were calculated as equal and opposite to the net, diffusional leak fluxes. Elevation of external K^+^ (6โ60 Mm)by equivalent replacement of Na^+^ (154โ91 mM) inhibits both active Na^+^ and K^+^ fluxes, but not proportionally. This results in a decrease of the coupling ratio (r~p~ = โJ~k~^p^/J) as external K^+^ is increased. Elevation of external K^+^ (3โ68 mM) at constant Na^+^ (92mM) inbibits J, but is without effect on J. The coupling ratio declines from 1.01 ยฑ 0.14 to 0.07 ยฑ 0.05, a 14โfold alteration. Reduction of external Na^+^ (154โ25 mM) at constant K^+^ (6mM) depresses J, but is without effect on J. The coupling ratio increases from 0.63 ยฑ 0.04 at 154 mM Na^+^ to 4.5 ยฑ 2.04 at 25 mM Na^+^. The results of this investigation are consistent with the independent regulation of active cation fluxes by the transported species. Kinetic analysis of the data indicates that elevation of external sodium stimulates active sodium efflux by interacting at โmodifier sitesโ at the outer cell surface. Similarly, external potassium inhibits active potassium influx by interaction at separate modifier sites.
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