We recently described a sodium gradient-dependent transport of phosphate through the brush border membrane vesicles from human placenta. In order to characterize this transport carrier further, we studied the influence of temperature and membrane potential on the transport of this electrolyte, the stoichiometry of the sodium-phosphate interaction, and the interrelationship between phosphate uptake and other sodium-dependent systems. Temperature influenced phosphate uptake by changing the maximal velocity and the affinity of the carrier for the substrate. The Arrhenius plot for uptake velocity exhibited an abrupt breakpoint at 28.6 degrees C, suggesting that membrane fluidity is a factor in phosphate uptake. Increasing the sodium concentration in the incubation medium augmented the phosphate uptake according to a sigmoid curve, and the Hill plot analysis of these data indicates that at least two sodium ions are transported with each phosphate radical. The effect of membrane potential on phosphate uptake was studied by inducing potassium diffusion with valinomycin and by using various sodium salts with different anion conductance in the incubation medium. In both series of experiments, the inside-negative potential significantly enhanced phosphate uptake. We concluded that the phosphate-sodium cotransport is an electrogenic process, a conclusion which is compatible with the observation that at least two sodium ions accompany each phosphate radical. Glycine, alanine and proline all inhibited phosphate uptake according to an uncompetitive type of inhibition. In contrast, the addition of glucose to the incubation medium had no effect.

Amino Acids↗

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Characterization of ATP-dependent Ca2+ transport in the basolateral membrane vesicles from proximal and distal tubules of the rabbit kidney.

Basolateral membrane vesicles were prepared from purified proximal and distal tubules of the rabbit kidney. The properties of the ATP-dependent Ca2+ transport were investigated. In both membranes, there was a high affinity, ATP-dependent Ca2+ transport system (Km = 0.1 microM). The optimal concentration of Mg2+ was 0.5 mM and the optimal concentration of ATP was 1 mM. The nucleotide specificity and pH dependence of the Ca2+ transport in both membranes were similar. In basolateral membrane vesicles, calmodulin had no effect on Ca2+ transport. However, in basolateral membrane vesicles depleted of calmodulin, exogenous calmodulin increased the Ca2+ transport by increasing maximal velocity. There were no major differences in the properties of the ATP-dependent Ca2+ transport system in these two membranes. These findings are discussed in relation to why parathyroid hormone differentially modulates Ca2+ transport in these two segments of the nephron.

Adenosine Triphosphate↗

PubMedDate not supplied

The X-linked hypophosphatemic vitamin D resistant rickets: old and new concepts.

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Animals↗