Effect of cystine loading and cystine dimethylester on renal brushborder membrane transport

1990 ◽  
Vol 10 (5) ◽  
pp. 455-459 ◽  
Author(s):  
John W. Foreman ◽  
Linda Benson
Keyword(s):  
Membrane Transport ◽  
Renal Tubule ◽  
Membrane Vesicles ◽  
Maximal Rate ◽  
Cystine Dimethylester ◽  
Tubule Cells

The effect of loading renal tubule cells with cystine was studied by incubating them with cystine dimethylester. Proline uptake into brushborder membrane vesicles isolated from the cystine loaded cells was not different from that observed into brushborder vesicles isolated from tubules incubated in buffer alone. Incubating brushborder membranes with 2 mM cystine dimethylester for 10 minutes reduced the uptake of proline by 27% after 15 seconds of incubation and by 21% after 60 seconds of incubation. There was no effect after 20 minutes of incubation. Pre-incubating brushborder membrane vesicles with cystine dimethylester had no statistically significant effect on the affinity of priline for the carrier, but did reduce the maximal rate of proline uptake by 49%.

scholarly journals Metabolic studies of rat renal tubule cells loaded with cystine: the cystine dimethylester model of cystinosis.

1995 ◽  
Vol 6 (2) ◽  
pp. 269-272
Author(s):  
J W Foreman ◽  
L L Benson ◽  
M Wellons ◽  
E D Avner ◽  
W Sweeney ◽  
...  
Keyword(s):  
Fanconi Syndrome ◽  
Renal Tubule ◽  
Renal Tissue ◽  
Renal Tubules ◽  
O2 Consumption ◽  
Metabolic Disturbances ◽  
Tissue Homogenates ◽  
Cystine Dimethylester ◽  
Tubule Cells ◽  
Isolated Rat

The cause of Fanconi syndrome in cystinosis is enigmatic. It has previously been shown that renal tubules could be loaded with cystine by incubating them with cystine dimethylester (CDE), mimicking the biochemical hallmark of cystinosis. Such tubules have impaired transport, decreased whole-cell O2 consumption, and substrate utilization. In this study, the metabolic disturbances in cystine-loaded renal tubule cells were further characterized. Isolated rat renal tubules were loaded with cystine by incubating them with 2 mM CDE for 10 min. This had no significant effect on total ATPase, Na(+)-K(+)-ATPase, or the ouabain-insensitive ATPase activity of renal tissue homogenates from these cystine-loaded tubules. Intracellular K was significantly lower in the cystine-loaded tubules (37 +/- 2 versus 47 +/- 3 nEq/mg; P < 0.008). Intracellular ATP was reduced by 39% in the cystine-loaded tubules (23.7 +/- 2.4 versus 38.1 +/- 3.3 nmol/mg of protein; P < 0.0025). CDE (2 mM) reduced isolated mitochondrial O2 consumption with glutamate as the substrate by 66% (4.7 +/- 0.7 versus 13.9 +/- 0.8 nm/min per mg of protein, P < 0.001) but had no effect on mitochondrial O2 consumption with succinate as the substrate. It was speculated that the impaired transport from cystine loading with CDE is secondary to a decrease in energy generation.

Cystine-glutamate transport interactions in rat renal cortical tubules, brushborder vesicles, and cultured renal tubule cells

1986 ◽  
Vol 6 (1) ◽  
pp. 113-119 ◽  
Author(s):  
John W. Foreman ◽  
Pamela D. McNamara ◽  
Margaret Ann Bowring ◽  
Judithann Lee ◽  
Claire Rea ◽  
...  
Keyword(s):  
Renal Tubule ◽  
Membrane Vesicles ◽  
Glutamate Transport ◽  
Serum Free ◽  
Defined Media ◽  
Tubule Cells ◽  
Isolated Rat

Glutamate had no significant effect on the uptake of 0.025 mM cystine by isolated rat renal cortical tubules and brushborder membrane vesicles in contrast to lysine which significantly inhibits cystine transport. Glutamate, however, markedly inhibited cystine uptake by rat renal tubule cells grown in a serum-free, hormonally defined media for 5 days. Lysine also inhibited cystine transport in these cultured renal tubule cells.

scholarly journals Therapeutic concentrations of cyclosporine A, but not FK506, increase P-glycoprotein expression in endothelial and renal tubule cells

1998 ◽  
Vol 54 (4) ◽  
pp. 1139-1149 ◽  
Author(s):  
Ingeborg A. Hauser ◽  
Michael Koziolek ◽  
Ulrich Hopfer ◽  
Frank Thévenod
Keyword(s):  
Cyclosporine A ◽  
Renal Tubule ◽  
P Glycoprotein ◽  
Tubule Cells

Reversed polarity of Na(+) -K(+) -ATPase: mislocation to apical plasma membranes in polycystic kidney disease epithelia

1991 ◽  
Vol 260 (3) ◽  
pp. F420-F430 ◽  
Author(s):  
P. D. Wilson ◽  
A. C. Sherwood ◽  
K. Palla ◽  
J. Du ◽  
R. Watson ◽  
...  
Keyword(s):  
Kidney Disease ◽  
Polycystic Kidney Disease ◽  
Plasma Membranes ◽  
Renal Tubule ◽  
Apical Membrane ◽  
Membrane Vesicles ◽  
Renal Tubules ◽  
Polycystic Kidney ◽  
Permeable Membrane ◽  
Reversed Polarity

Autosomal dominant polycystic kidney disease (ADPKD) is a genetic disorder in which renal tubules become enormously enlarged due to fluid accumulation. Na(+) -K(+) -ATPase was compared in normal and cystic regions of whole kidneys and in confluent primary cultures of microdissected renal tubule and cyst-lining epithelia. Immunostaining with antibodies directed against the Na(+) -K(+) -ATPase catalytic alpha-subunit was confined to apical, luminal plasma membranes of ADPKD epithelia, which was a complete reversal of the normal renal tubule polarized location in basolateral membranes. Mislocated Na(+) -K(+) -ATPase was shown to be functionally active, because identical intense apical staining was observed by use of a cytochemical assay. In addition, biochemical assays showed a significant increase in these ouabain-inhibitable Na(+) -K(+) -ATPase specific activity levels in ADPKD kidneys compared with age-matched normal kidneys. Specific binding of [3H] ouabain was not only increased but also confined to the apical membrane vesicles prepared from cystic regions of ADPKD kidneys compared with normal age-matched controls, in which binding was confined to basolateral membrane vesicles. Although steady-state levels of Na(+) -K(+) -ATPase alpha- and beta-subunit in mRNAs were increased somewhat in ADPKD kidneys, this alone was not sufficient to account for the observed activation. Confluent ADPKD epithelia grown on dual-chamber, permeable membrane supports also showed reversed polarity of 22NaCl vectorial transport, because this was from basal to apical media compartments. Because this transport could also be blocked by ouabain, this suggested apical Na(+) -K(+) -ATPase was responsible and implicated altered polarity of Na(+) -K(+) -ATPase and resultant Na+ secretion as a mechanism for cyst formation in ADPKD. Because no reversal of polarity of other basolateral or apical membrane proteins was detected, an intracellular sorting defect specific for Na(+) -K(+) -ATPase is proposed.

Na,K-ATPase Activity in Renal Tubule Cells From Milan Hypertensive Rats

1989 ◽  
Vol 2 (7) ◽  
pp. 563-566 ◽  
Author(s):  
Maria-Luisa Melzi ◽  
Alejandro Bertorello ◽  
Yutaka Fukuda ◽  
Ingrid Muldin ◽  
Fabio Sereni ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Renal Tubule ◽  
Hypertensive Rats ◽  
Tubule Cells

Abstract 215: Adam17 Regulates Renal Function

Circulation ◽  
2020 ◽  
Vol 142 (Suppl_4) ◽  
Author(s):  
Bo Zhang ◽  
Kai Chen ◽  
Zhongjie Sun
Keyword(s):  
Renal Function ◽  
Kidney Function ◽  
Renal Tubule ◽  
Renal Diseases ◽  
Normal Kidney ◽  
Normal Kidney Function ◽  
Membrane Bound ◽  
Tubule Cells ◽  
A Disintegrin And Metalloproteinase

A disintegrin and metalloproteinase 17 (ADAM17) is a ubiquitously expressed membrane-bound sheddase that cleaves a diverse variety of membrane-bound molecules, including cytokines, growth factors, and their receptors to activate or inactivate various cellular signaling pathways. Although it was reported that ADAM17 may mediate renal diseases, the role of ADAM17 in the regulation of normal kidney function has never been identified. The objective of this study is to investigate whether renal ADAM17 plays a role in maintaining normal kidney function and structure. Tamoxifen-inducible kidney-specific cre (Ksp) and ADAM17-floxed mice were cross-bred for generating Ksp/ADAM17-floxed mice. Injection of tamoxifen initiated deletion of the ADAM17 gene in renal tubule cells. We found that conditional kidney-specific knockout of ADAM1 7 gene (Ksp-ADAM17 -/-) decreased urinary creatinine and sodium excretion were decreased in Ksp-ADAM17 -/- mice, indicating that ADAM17 gene deficiency impairs kidney function. H&E staining showed glomerulus collapse and tubule dilation in Ksp-ADAM17 -/- mice. The epithelial cells fall off into the lumen in the renal tubule. Mesangial expansion and fibrosis were found in glomeruli in Ksp-ADAM17 -/- mice. Moreover, apoptosis was increased in tubule cells in both cortex and medulla areas in Ksp-ADAM17 -/- mice. In conclusion, ADAM17 is critical to the maintenance of normal renal function and structure.

Role of intracellular calcium in renal proximal tubule cell volume regulation

1992 ◽  
Vol 263 (5) ◽  
pp. R1086-R1092 ◽  
Author(s):  
D. A. Terreros ◽  
H. Kanli
Keyword(s):  
Carassius Auratus ◽  
Renal Tubule ◽  
Cell Volume Regulation ◽  
K Channel ◽  
Renal Tubules ◽  
Proximal Tubule Cell ◽  
Tubule Cell ◽  
Proximal Renal Tubule ◽  
Tubule Cells

Osmoregulatory Ca2+ signaling in hypotonic solutions was studied with videometric techniques in 158 proximal renal tubules isolated from the teleost Carassius auratus. Absence of extracellular Ca2+, hypoxia (23 mmHg), or NaCN (3 mM) did not alter regulatory volume decreases (RVD). Nevertheless, decrements of intracellular Ca2+ via the A23187 ionophore or after intracellular Ca2+ chelation with indo-1/AM (5 microM) inhibited RVD. In tubules depleted of Ca2+, RVD could only be fully elicited when intracellular Ca2+ pulses were given within 1 min after hypotonic stimulation. While inhibition of Ca2+ release from the endoplasmic reticulum (ER) with 8-(diethylamino)octyl 3,4,5-trimethoxybenzoate hydrochloride (TMB-8, 50 microM) blunted RVD, some of its effects could be reversed with the anion carrier tributyltin (1 microM). Dibutyryl adenosine 3',5'-cyclic monophosphate (cAMP, 0.5 and 1.0 mM) and forskolin (0.25 mM) also impeded RVD; however, their effects could be partially reversed with the K+ ionophore gramicidin (0.5 microM). In conclusion, in Carassius auratus proximal renal tubule cells, RVD is activated by an intracellular Ca2+ signal that likely emanates from the ER and not from the extracellular media or the mitochondrial Ca2+ pool. Ca2+ activation of a cAMP-modulated osmoregulatory K+ channel appears to play an important role.

Toxicity of ifosfamide and its metabolite chloroacetaldehyde in cultured renal tubule cells

1999 ◽  
Vol 35 (6) ◽  
pp. 314-317 ◽  
Author(s):  
James Springate ◽  
Kenneth Chan ◽  
Hong Lu ◽  
Sherry Davies ◽  
Mary Taub
Keyword(s):  
Renal Tubule ◽  
Tubule Cells
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