Cadmium Binding and Sodium-Dependent Solute Transport in Renal Brush-Border Membrane Vesicles

1999 ◽  
Vol 154 (3) ◽  
pp. 212-218 ◽  
Author(s):  
Do Whan Ahn ◽  
Young Mook Kim ◽  
Kyoung Ryong Kim ◽  
Yang Saeng Park
Keyword(s):  
Solute Transport ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Renal Brush Border Membrane ◽  
Sodium Dependent ◽  
Renal Brush Border

Sodium-pyrazinoate cotransport in rabbit renal brush border membrane vesicles

1985 ◽  
Vol 249 (3) ◽  
pp. F400-F408 ◽  
Author(s):  
M. Manganel ◽  
F. Roch-Ramel ◽  
H. Murer
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Organic Anion ◽  
Membrane Vesicles ◽  
Sodium Concentration ◽  
Brush Border Membrane Vesicles ◽  
Renal Brush Border Membrane ◽  
Sodium Dependent ◽  
Dependent Transport ◽  
Renal Brush Border

Pyrazinoate (PZA) is an organic anion actively reabsorbed and secreted in the mammalian kidney. In experiments with rabbit renal brush border membrane vesicles, we characterized a sodium-PZA cotransport mechanism that could be involved in reabsorption. An inwardly directed sodium gradient stimulated the influx of PZA. The sodium-dependent transport was electroneutral, suggesting a 1:1 stoichiometry. The kinetic constants for sodium-PZA cotransport were measured under initial linear flux and zero trans conditions for both sodium and PZA. The apparent Km for sodium was about 60 mM. At 90 mM sodium the apparent Km for PZA was about 1.1 mM; increasing the sodium concentration augmented the apparent affinity for PZA. Cis inhibition of sodium-dependent PZA uptake was observed by the addition of nicotinate, lactate, probenecid, succinate, beta-hydroxybutyrate, and salicylate. Urate had no effect. [14C]PZA uptake was trans stimulated by PZA itself, lactate, and nicotinate. PZA shares a transport system(s) involved in the proximal tubular reabsorption of these two anions.

Low-affinity transport of pyroglutamyl-histidine in renal brush-border membrane vesicles

1989 ◽  
Vol 257 (5) ◽  
pp. C971-C975 ◽  
Author(s):  
H. A. Skopicki ◽  
K. Fisher ◽  
D. Zikos ◽  
G. Flouret ◽  
D. R. Peterson
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Proximal Tubular Cells ◽  
Tubular Cells ◽  
Luminal Membrane ◽  
Renal Brush Border Membrane ◽  
Proximal Tubular ◽  
Renal Brush Border

These studies were performed to determine if a low-affinity carrier is present in the luminal membrane of proximal tubular cells for the transport of the dipeptide, pyroglutamyl-histidine (pGlu-His). We have previously described the existence of a specific, high-affinity, low-capacity [transport constant (Kt) = 9.3 X 10(-8) M, Vmax = 6.1 X 10(-12) mol.mg-1.min-1] carrier for pGlu-His in renal brush-border membrane vesicles. In the present study, we sought to demonstrate that multiple carriers exist for the transport of a single dipeptide by determining whether a low-affinity carrier also exists for the uptake of pGlu-His. Transport of pGlu-His into brush-border membrane vesicles was saturable over the concentration range of 10(-5)-10(-3) M, yielding a Kt of 6.3 X 10(-5) M and a Vmax of 2.2 X 10(-10) mol.mg-1.min-1. Uptake was inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and carnosine but not by the tripeptide pyroglutamyl-histidyl-prolinamide. We conclude that 1) pGlu-His is transported across the luminal membrane of the proximal tubule by multiple carriers and 2) the lower affinity carrier, unlike the higher affinity carrier, is nonspecific with respect to other dipeptides.

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