The Mechanism of Human Placental Urea Transport: A Study Using Placental Brush Border (Microvillous) Membrane Vesicles

2010 ◽  
Vol 17 (1) ◽  
pp. 67-72 ◽  
Author(s):  
Hiroyasu Hisanaga ◽  
Hideaki Iioka ◽  
Ikuko Moriyama ◽  
Kaoru Nabuchi ◽  
Keiko Morimoto ◽  
...  
1985 ◽  
Vol 249 (6) ◽  
pp. F806-F812
Author(s):  
A. S. Verkman ◽  
J. A. Dix ◽  
J. L. Seifter ◽  
K. L. Skorecki ◽  
C. Y. Jung ◽  
...  

Radiation inactivation was used to determine the nature and molecular weight of water and urea transport pathways in brush border membrane vesicles (BBMV) isolated from rabbit renal cortex. BBMV were frozen to -50 degrees C, irradiated with 1.5 MeV electrons, thawed, and assayed for transport or enzyme activity. The freezing process had no effect on enzyme or transport kinetics. BBMV alkaline phosphatase activity gave linear ln(activity) vs. radiation dose plots with a target size of 68 +/- 3 kDa, similar to previously reported values. Water and solute transport were measured using the stopped-flow light-scattering technique. The rates of acetamide and osmotic water transport did not depend on radiation dose (0-7 Mrad), suggesting that transport of these substances does not require a protein carrier. In contrast, urea and thiourea transport gave linear ln(activity) vs. dose curves with a target size of 125-150 kDa; 400 mM urea inhibited thiourea flux by -50% at 0 and 4.7 Mrad, showing that radiation does not affect inhibitor binding to surviving transporters. These studies suggest that BBMV urea transport requires a membrane protein, whereas osmotic water transport does not.


Placenta ◽  
1993 ◽  
Vol 14 (1) ◽  
pp. 93-102 ◽  
Author(s):  
Hideaki Iioka ◽  
Hiroyasu Hisanaga ◽  
Shinobu Akada ◽  
Takako Shimamoto ◽  
Yoshihiko Yamada ◽  
...  

Placenta ◽  
1992 ◽  
Vol 13 (2) ◽  
pp. 179-190 ◽  
Author(s):  
Hideaki Iioka ◽  
Hiroyasu Hisanaga ◽  
Ikuko S. Moriyama ◽  
Shinobu Akada ◽  
Takako Shimamoto ◽  
...  

1990 ◽  
Vol 35 (3) ◽  
pp. 333-339 ◽  
Author(s):  
B. U. K. Li ◽  
Paul M. Bummer ◽  
John W. Hamilton ◽  
Hallgrimur Gudjonsson ◽  
George Zografi ◽  
...  

1989 ◽  
Vol 257 (5) ◽  
pp. C971-C975 ◽  
Author(s):  
H. A. Skopicki ◽  
K. Fisher ◽  
D. Zikos ◽  
G. Flouret ◽  
D. R. Peterson

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.


2021 ◽  
Vol 139 ◽  
pp. 109940
Author(s):  
Lesbia Cristina Julio-Gonzalez ◽  
F. Javier Moreno ◽  
María Luisa Jimeno ◽  
Elisa G. Doyagüez ◽  
Agustín Olano ◽  
...  

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