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Am J Physiol Renal Physiol 261: F670-F678, 1991;
0363-6127/91 $5.00
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AJP - Renal Physiology, Vol 261, Issue 4 670-F678, Copyright © 1991 by American Physiological Society


ARTICLES

Multiple carriers for dipeptide transport: carrier-mediated transport of glycyl-L-proline in renal BBMV

H. A. Skopicki, K. Fisher, D. Zikos, R. Bloch, G. Flouret and D. R. Peterson
Department of Physiology, University of Health Sciences/Chicago Medical School, Illinois 60064.

To determine whether multiple carriers are responsible for luminal uptake of glycyl-L-proline (Gly-Pro) in the renal proximal tubule, transport of Gly-[3H]Pro was measured in brush-border membrane vesicles (BBMV). A Line-weaver-Burk analysis of Michaelis-Menten kinetics revealed the presence of two carriers: a lower affinity, higher capacity carrier (Km = 1.3 x 10(-2) M; Vmax = 4.6 x 10(-8) mol.mg-1.min-1) and a higher affinity, lower capacity carrier (Km = 2.7 x 10(-7) M; Vmax = 7.8 x 10(-13) mol.mg-1.min-1). The dipeptides Gly-Sar, beta Ala-His, and pyroGlu-His competitively inhibited the low-affinity carrier. No effect on the Km or Vmax of Gly-Pro transport in this range was seen in the presence of the dipeptides Gly-Gly or cycloHis-Pro. The high-affinity carrier exhibited a different inhibition spectrum. Competitive inhibition of Gly-Pro transport was demonstrated for the dipeptides Gly-Gly and Gly-Sar. However, none of the other peptides tested above altered Gly-Pro transport in the high-affinity range, including pyroGlu-His, which is transported by a high-affinity carrier. At both low (4 x 10(-8) M) and high (4 x 10(-3) M) concentrations, uptake of Gly-Pro was stimulated in the presence of an inwardly directed H+ gradient but was unaffected by the presence of an inward Na+ gradient. In addition, measurements in the presence of valinomycin and an outwardly directed K+ gradient strongly suggest that H(+)-stimulated uptake at both concentrations is electrogenic.(ABSTRACT TRUNCATED AT 250 WORDS)


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U. Wenzel, D. Diehl, M. Herget, and H. Daniel
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1 cells
Am J Physiol Cell Physiol, December 1, 1998; 275(6): C1573 - C1579.
[Abstract] [Full Text] [PDF]




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