Sodium-coupled amino acid transport in renal tubule

Abstract

Amino acids are reabsorbed from the tubular lumen by a saturable, carrier-mediated, concentrative transport mechanism driven by a Na+ electrochemical gradient across the luminal membrane. This process is followed by efflux mainly via carrier-mediated, Na+-independent facilitated diffusion across the basolateral membrane. Individual amino acids may have two or more Na+-dependent transport systems with different kinetic characteristics along the luminal membrane of the proximal tubule, thereby enabling very efficient amino acid reabsorption. Dual Na+-coupled transport pathways for some amino acids located in both the luminal and the peritubular membranes may operate in concert to provide the tubular epithelial cell with essential nutrients. One or more Na+ ions, H+, Cl- and in the case of acidic amino acids, K+ ion, may be involved in the translocation of the carrier complex. For most amino acids this process is electrogenic positive, favored by a negative cell interior. At least seven distinct, but largely interacting, Na+-dependent amino acid transport systems have been identified in the brush border membrane. A diet-induced adaptation in Na+-coupled taurine transport and acidosis-induced adaptive response in Na+-dependent glutamine transport are expressed at the luminal and the basolateral membrane surfaces, respectively. The aminoaciduria of early life may be related to a rapid dissipation of the Na+ electrochemical gradient necessary for amino acid reabsorption.