Cystine and lysine reabsorption in the isolated perfused rat kidney.
Renal tubular reabsorption of cystine and lysine were studied in the isolated perfused rat kidney to bridge the gap between in vivo clearance studies, and in vitro transport studies of tubule fragments, cells, and brush-border membranes. Lysine was reabsorped by a saturable transport system shared by the dibasics. Cystine was also reabsorbed by a saturable transport system, which was shared in part by the dibasics (maximum inhibition 30%). The lysine threshold (Fmin) was 0.9 mumol.min-1.g-1, with a tubular maximum (TM) of 2.4 mumol.min-1.g-1. The cystine Fmin was 0.06 mumol.min-1.g-1; the TM could not be estimated because it was above the limit of cystine solubility. There was no evidence of cystine "secretion." The gamma-glutamyltransferase inhibitor, AT-125, decreased cystine excretion, but only in the presence of glutathione, glycine, glutamate, and the diabasic amino acids. This suggests that cystine from glutathione degradation at the brush border may contribute to urinary cystine (an explanation of the phenomenon of cystine secretion), but only under certain conditions.
Roby
K A
KA
Division of Biochemical Development and Molecular Diseases, Children's Hospital of Philadelphia, Pennsylvania.
Segal
S
S
D000596:Amino Acids / Q000494:pharmacology; D000818:Animals; D003553:Cystine / Q000493:pharmacokinetics*; D005978:Glutathione / Q000494:pharmacology; D066298:In Vitro Techniques; D007555:Isoxazoles / Q000494:pharmacology; D007668:Kidney / Q000378:metabolism*; D008239:Lysine / Q000493:pharmacokinetics*; D008297:Male; D010477:Perfusion; D051381:Rats; D011919:Rats, Inbred Strains; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors
D000596:Amino Acids; D007555:Isoxazoles; D003553:Cystine; D005723:gamma-Glutamyltransferase; D005978:Glutathione; D008239:Lysine; C006303:acivicin