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. 1984 May 15;220(1):15-24.
doi: 10.1042/bj2200015.

Renal transport of neutral amino acids. Tubular localization of Na+-dependent phenylalanine- and glucose-transport systems

Renal transport of neutral amino acids. Tubular localization of Na+-dependent phenylalanine- and glucose-transport systems

U Kragh-Hansen et al. Biochem J. .

Abstract

The transport properties for phenylalanine and glucose in luminal-membrane vesicles from outer cortex (pars convoluta) and outer medulla (pars recta) of rabbit kidney were studied by a spectrophotometric method. Uptake of phenylalanine as well as of glucose by the two types of membrane vesicles was found to be Na+-dependent, electrogenic and stereospecific. Na+-dependent transport of L-phenylalanine by outer-cortical membrane vesicles could be accounted for by one transport system (KA congruent to 1.5 mM). By contrast, in the outer-medullary preparation, L-phenylalanine transport occurred via two transport systems, namely a high-affinity system with K1A congruent to 0.33 mM and a low-affinity system with K2A congruent to 7 mM respectively. Na+-dependent uptake of D-glucose by pars convoluta and pars recta membrane vesicles could be described by single, but different, transport systems, namely a low-affinity system with KA congruent to 3.5 mM and a high-affinity system with KA congruent to 0.30 mM respectively. Attempts to calculate the stoichiometry of the different Na+/D-glucose transport systems by using Hill-type plots revealed that the ratio of the Na+/hexose co-transport probably is 1:1 in the case of pars convoluta and 2:1 in membrane vesicles from pars recta. The Na+/L-phenylalanine stoichiometry of the pars convoluta transporter probably is 1:1. Both the high-affinity and the low-affinity Na+-dependent L-phenylalanine transport system of pars recta membrane vesicles seem to operate with a 1:1 stoichiometry. The physiological importance of the arrangement of low-affinity and high-affinity transport systems along the kidney proximal tubule is discussed.

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References

    1. Am J Physiol. 1966 Jun;210(6):1293-8 - PubMed
    1. J Physiol. 1972 Dec;227(2):565-90 - PubMed
    1. Biochim Biophys Acta. 1974 Jul 31;356(2):231-43 - PubMed
    1. J Biol Chem. 1975 Aug 10;250(15):6032-9 - PubMed
    1. Biochem J. 1975 Oct;151(1):61-6 - PubMed

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