scholarly journals Role of N-linked oligosaccharides in the transport activity of the Na+/H+ antiporter in rat renal brush-border membrane.

1988 ◽  
Vol 263 (27) ◽  
pp. 13683-13691 ◽  
Author(s):  
A N Yusufi ◽  
M Szczepanska-Konkel ◽  
T P Dousa
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
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.

scholarly journals Hydrolysis of nicotinamide-adenine dinucleotide by purified renal brush-border membranes. Mechanism of NAD+ inhibition of brush-border membrane phosphate-transport activity

1982 ◽  
Vol 204 (3) ◽  
pp. 635-638 ◽  
Author(s):  
H S Tenenhouse ◽  
Y L Chu
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Reciprocal Relationship ◽  
Brush Border Membrane Vesicles ◽  
Transport Activity ◽  
Freezing And Thawing ◽  
Pi Transport ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

Purified rat renal brush-border membrane vesicles possess a heat-labile enzyme activity which hydrolyses NAD+. A reciprocal relationship exists between the disappearance of NAD+ and the appearance of adenosine; 2 mol of Pi are liberated from each mol of NAD+ incubated with brush-border membrane vesicles. Freezing and thawing brush-border membrane vesicles does not enhance the initial rate of NAD+ hydrolysis. Preincubation of brush-border membrane vesicles with NAD+ results in inhibition of Na+-dependent Pi-transport activity, whereas Na+-dependent glucose transport is not affected. EDTA, which prevents the release of Pi from NAD+ and which itself has no direct effect on brush-border membrane Pi transport, reverses the NAD+ inhibition of Na+-dependent Pi transport. These results suggest that it is the Pi liberated from NAD+ and not NAD+ itself that inhibits Na+-dependent Pi transport.

scholarly journals Thyroid hormones modulate zinc transport activity of rat intestinal and renal brush-border membrane

1999 ◽  
Vol 276 (4) ◽  
pp. E774-E782 ◽  
Author(s):  
Rajendra Prasad ◽  
Vivek Kumar ◽  
Rajinder Kumar ◽  
Kiran Pal Singh
Keyword(s):  
Thyroid Hormone ◽  
Thyroid Hormones ◽  
Membrane Fluidity ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Maximal Velocity ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
Hormone Status ◽  
Renal Brush Border

Thyroid hormone status influences the Zn2+ and metallothionein levels in intestine, liver, and kidney. To evaluate the impact of thyroid hormones on Zn2+ metabolism, Zn2+ uptake studies were carried out in intestinal and renal brush-border membrane vesicles (BBMV). Steady-state Zn2+ transport in intestinal and renal cortical BBMV was increased in hyperthyroid (Hyper-T) rats and decreased in the hypothyroid (Hypo-T) rats relative to euthyroid (Eu-T) rats. In both the intestinal and renal BBMV, Hyper-T rats showed a significant increase in maximal velocity compared with Eu-T and Hypo-T rats. Apparent Michaelis constant was unaltered in intestinal and renal BBMV prepared from the three groups. Fluorescence anisotropy of diphenyl hexatriene was decreased significantly in intestinal and renal brush-border membrane (BBM) isolated from Hyper-T rats compared with Hypo-T and Eu-T rats. A significant reduction in the microviscosity and transition temperature for Zn2+ uptake in intestinal and renal BBM from Hyper-T rats is in accordance with the increased fluidity of these BBMs. These findings suggest that the increased rate of Zn2+ transport in response to thyroid hormone status could be associated with either an increase in the number of Zn2+ transporters or an increase in the active transporters due to alteration in the membrane fluidity. Thus the thyroid hormone-mediated change in membrane fluidity might play an important role in modulating Zn2+ transport activity of intestinal and renal BBM.

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