Isolation and function of the amino acid transporter PAT1 (slc36a1) from rabbit and discrimination between transport via PAT1 and system IMINO in renal brush-border membrane vesicles

2005 ◽  
Vol 22 (6) ◽  
pp. 549-559 ◽  
Author(s):  
Seiji Miyauchi ◽  
Emily L. Abbot ◽  
Lina Zhuang ◽  
Radhika Subramanian ◽  
Vadivel Ganapathy ◽  
...  
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Amino Acid Transporter ◽  
Brush Border Membrane Vesicles ◽  
Renal Brush Border Membrane ◽  
Acid Transporter ◽  
And Function ◽  
Renal Brush Border

scholarly journals Reconstitution and identification of the major Na+-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles

1992 ◽  
Vol 281 (1) ◽  
pp. 95-102 ◽  
Author(s):  
F A Doyle ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Acid Transport ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

Amino acid transport activity from bovine renal brush-border membrane vesicles (BBMV) was reconstituted into phospholipid vesicles composed of phosphatidylcholine/5% stearylamine. Reconstitutable transport activity was enhanced in protein fractions binding to various lectins. When solubilized BBMV were fractionated on peanut lectin, a single protein band of average molecular mass 132 kDa was obtained. When this protein fraction was reconstituted into phospholipid membrane vesicles, amino acid transport activity was obtained with properties similar to those in native BBMV with regard to amino acid specificity, although the cation specificity was different. A monoclonal antibody which reacted with the same protein removed reconstitutable amino acid transport activity from solubilized BBMV. These findings may provide the first identification of a renal amino acid-transporting protein, although confirmation of this identification by other approaches will be required.

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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