PubMed · 4884849
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A Katchalsky, R Spangler. 1968. Dynamics of membrane processes.. https://doi.org/10.1017/s0033583500000524
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NHA1 encodes a K(+) (Na(+))/H(+) antiporter in the plasma membrane of Saccharomyces cerevisiae. We report that cells expressing the NHA1 gene contained less K(+) than the mutant lacking the gene when grown without K(+) limitation. They also grew better at low K(+) and showed higher affinity of transport than the nha1 strain. In agreement with the function of an electroneutral cation/H(+) antiporter, the effect was only observed at acidic pH. The improved growth and transport depended on the presence of Trk1p (the main K(+) influx system) and did not require the product of TRK2. We propose that Nha1p regulates the potassium content of the cell and, as a consequence, can affect the activity of the main K(+) influx system (Trk1p).
The fluorescein transport characteristics of the human intestinal epithelial Caco-2 cell line were examined in monolayer cultures. The initial uptake rate was concentration-dependent and saturable; the Michealis constant and the maximum velocity were 0.40 mM and 1.32 nmol/min/mg protein, respectively. A protonophore, carbonyl cyanide m-chlorophenyl-hydrazone, reduced uptake significantly. The replacement of extracellular sodium ions by lithium ions did not alter the initial uptake rate. These facts imply that the transport is driven by a proton gradient. The initial uptake rate was strongly dependent upon extracellular pH, and the uptake was optimal at approximately pH 5.5. Based on the protolytic constants, the main species of fluorescein in the pH range of 5.5 to 6.0 was calculated to be a monoanion, suggesting that fluorescein was taken up by Caco-2 cells as a monocarboxylate. The following findings support this conclusion: the uptake was inhibited significantly by monocarboxylate compounds such as salicylate and pravastatin, but not by di- or tricarboxylic acids or by acidic amino acids. Furthermore, salicylate-preloaded cells showed remarkably enhanced uptake of fluorescein, indicating that monocarboxylates and fluorescein share a common transport carrier. The transporter has a wide spectrum of substrate recognition and seems likely to be different from MCT1.
Ion channels catalyze the transport of ions across biological membranes. A proper understanding of ion-channel functioning is essential to our knowledge of cell physiology, and, in this context, ion-channel selectivity is a key concept. The extent to which a channel permeates two ion species, a and b, is expressed by the permeability ratio, P(a)/P(b). This paper addresses a complication in the calculation of P(a)/P(b) that is related to the existence of surface potentials (psi) and that so far has not been fully appreciated. This paper shows the rather surprising effect of psi on the calculated P(a)/P(b) of a channel that is permeable to two ion species of different valence. If we ignore psi, we conclude, for instance, P(a) > P(b). If we implement psi in the calculation of P(a)/P(b), we may, however, conclude exactly the reverse, i.e., P(a) < P(b). Because electrostatic potentials arise at the surface of essentially all biological membranes, this paper argues for a more critical evaluation of ion channel selectivity measurements.