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J. Biol. Chem., Vol. 259, Issue 23, 14508-14514, Dec, 1984
LH Lash and DP Jones
Na+-dependent GSH transport in basal-lateral membrane vesicles from rat
kidney exhibited saturation kinetics while Na+-independent flux increased
linearly up to 10 mM GSH. Inhibitor studies showed that GSH transport was
not dependent upon the catalytic activity of gamma- glutamyltransferase.
K+, choline and NH+4 ions did not stimulate GSH transport, but Li+
partially substituted for Na+. Na+-dependent GSH transport was inhibited by
other gamma-glutamyl amino acids. The membrane also showed Na+-dependent
transport of glutathione disulfide (GSSG) and gamma-glutamylglutamate.
These results show that specificity resides in the gamma-glutamyl moiety
and suggest that this system may be a general transport system for
gamma-glutamyl compounds. Results from four types of experiments showed
that Na+-dependent GSH transport was electrogenic. Transport was stimulated
by negative and inhibited by positive valinomycin-induced K+ diffusion
potentials; the transport rate was influenced by the anion component of the
Na+ salt in the order NaSCN greater than NaCl greater than Na2SO4; analysis
of the Na+ concentration dependence indicated coupling of at least 2
Na+/GSH; comparison of GSH-dependent Na+ transport and Na+-dependent GSH
transport gave a Na+:GSH stoichiometry of 2:1. Thus, energy is coupled to
the transport of GSH in the form of the cellular Na+ gradient and the
membrane potential. This system, if it functions in vivo, can act as a
mechanism for extraction of GSH from the renal circulation.
Renal glutathione transport. Characteristics of the sodium-dependent system in the basal-lateral membrane
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