Increased Na + ‐taurine symporter in rat renal brush border membranes: preformed or newly synthesized?

1989 ◽  
Vol 3 (9) ◽  
pp. 2081-2085 ◽  
Author(s):  
Russell W. Chesney ◽  
Kent Jolly ◽  
Israel Zelikovic ◽  
Chris Iwahashi ◽  
Peter Lohstroh
Keyword(s):  
Brush Border ◽  
Brush Border Membranes ◽  
Renal Brush Border Membranes ◽  
Renal Brush Border

scholarly journals PHOSPHATE (Pi) TRANSPORT IN RENAL BRUSH BORDER MEMBRANES (BBMV) IN NEWBORN PUPPIES (P)

1984 ◽  
Vol 18 ◽  
pp. 366A-366A
Author(s):  
Eddie S Moore ◽  
Eunice G John ◽  
Lawrence Rufr ◽  
Christine S Mooers ◽  
Nochik Park ◽  
...  
Keyword(s):  
Brush Border ◽  
Brush Border Membranes ◽  
Pi Transport ◽  
Renal Brush Border Membranes ◽  
Renal Brush Border

Ion pathways in renal brush border membranes

1982 ◽  
Vol 685 (3) ◽  
pp. 260-272 ◽  
Author(s):  
C. Burnham ◽  
C. Munzesheimer ◽  
E. Rabon ◽  
G. Sachs
Keyword(s):  
Brush Border ◽  
Brush Border Membranes ◽  
Renal Brush Border Membranes ◽  
Renal Brush Border

scholarly journals PHOSPHATE (Pi) UPTAKE IN FETAL LAMB (FL) RENAL BRUSH BORDER MEMBRANES (BBMV)

1984 ◽  
Vol 18 ◽  
pp. 366A-366A
Author(s):  
Lawrence Rufer ◽  
Eddie S Moore ◽  
Christine S Mooers ◽  
Nochik Park
Keyword(s):  
Brush Border ◽  
Brush Border Membranes ◽  
Fetal Lamb ◽  
Renal Brush Border Membranes ◽  
Renal Brush Border

NAD+-dependent ADP-ribosyltransferase in renal brush-border membranes

1983 ◽  
Vol 245 (5) ◽  
pp. C449-C456 ◽  
Author(s):  
S. A. Kempson ◽  
N. P. Curthoys
Keyword(s):  
Brush Border ◽  
Gradient Centrifugation ◽  
Phosphate Transport ◽  
Adp Ribosylation ◽  
Brush Border Membranes ◽  
Snake Venom Phosphodiesterase ◽  
Renal Brush Border Membranes ◽  
Mechanism Of Interaction ◽  
Adp Ribosyltransferase ◽  
Renal Brush Border

Oxidized nicotinamide adenine dinucleotide (NAD+) in cytosol may interact with renal brush-border membranes (BBM) and inhibit BBM phosphate transport. The possible mechanism of interaction was investigated in the present study. Incubation of BBM with [adenine-3H]NAD+ led to acid-stable binding of 3H to the BBM, in contrast there was no binding of 14C when [carbonyl-14C]NAD+ was used. The data are consistent with an ADP-ribosylation mechanism involving transfer of ADP-ribose from NAD+ to BBM. This was confirmed by using [adenylate-32P]NAD+ and by the release of bound 32P in the form of 5'-[32P]AMP when the BBM were treated with snake venom phosphodiesterase. After gradient centrifugation of BBM the ADP-ribosyltransferase was recovered at the same density as known BBM enzymes, indicating that ADP-ribosyltransferase is an intrinsic BBM component and not a contaminant. These findings indicate that cytosolic NAD+ may be used for ADP-ribosylation of BBM proteins and that this may be a mechanism for regulating the BBM phosphate transport system.

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