Expression of AQP family in rat kidneys during development and maturation

1997 ◽  
Vol 272 (2) ◽  
pp. F198-F204 ◽  
Author(s):  
T. Yamamoto ◽  
S. Sasaki ◽  
K. Fushimi ◽  
K. Ishibashi ◽  
E. Yaoita ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Kidney Development ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Staining Intensity ◽  
Ribonuclease Protection Assay ◽  
Duct Cells ◽  
Apical Side ◽  
Basolateral Side ◽  
Collecting Duct Cells

The mRNA expression and localization of the aquaporin (AQP) family in rat kidney were examined by ribonuclease protection assay and immunohistochemistry. AQP1, AQP2, AQP3, and AQP4 mRNA were hardly detectable in 16-day gestation fetuses. AQP1 mRNA was explosively expressed at 1 wk, keeping the level throughout life. AQP2 mRNA expression was apparently noticed in 18-day fetuses and was enhanced gradually with age to reach a plateau at 4 wk. AQP3 and AQP4 mRNA expression was significantly found at birth but was not changed remarkably thereafter. AQP2 protein appeared first at the apical side of collecting duct cells in 18-day fetuses. The staining intensity at the site increased with age, and basolateral staining was added in adult rats. AQP3 was distinctly demonstrated at the basolateral side of collecting duct cells after birth, and the staining intensity was almost stable throughout life. The progressive induction of AQP2 expression in the first 4 wk after birth is presumed to contribute to the maturation of urinary concentrating capacity during the kidney development.

scholarly journals Urinary Reabsorption in the Rat Kidney by Anticholinergics

2021 ◽  
Author(s):  
Hideki Oe ◽  
Hatsumi Yoshiki ◽  
Xinmin Zha ◽  
Hisato Kobayashi ◽  
Yoshitaka Aoki ◽  
...  
Keyword(s):  
Absorption Rate ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Intracellular Camp ◽  
Dependent Manner ◽  
Bladder Epithelium ◽  
Duct Cells ◽  
Urine Production ◽  
Saline Administration ◽  
Collecting Duct Cells

Abstract Anticholinergics, therapeutic agents for overactive bladder, are clinically suggested to reduce urine output. We investigated whether this effect is due to bladder or kidney urine reabsorption. Various solutions were injected into the bladder of urethane-anesthetized SD rats. The absorption rate for 2 hr was examined following the intravenous administration of the anticholinergics imidafenacin (IM), atropine(AT), and tolterodine(TO). The bilateral ureter was then canulated and saline was administered to obtain a diuretic state. Anticholinergics or 1-deamino-[8-D-arginine]-vasopressin (dDAVP) were intravenously administered. After the IM and dDAVP administrations, the rat kidneys were immunostained with AQP2 antibody, and intracellular cAMP was measured. The absorption rate was ~10% of the saline injected into the bladder and constant even when anticholinergics were administered. The renal urine among peaked 2 hr after the saline administration. Each of the anticholinergics significantly suppressed the urine production in a dose-dependent manner, as did dDAVP. IM and dDAVP increased the intracellular cAMP levels and caused the AQP2 molecule to localize to the collecting duct cells' luminal side. The urinary reabsorption mechanism through the bladder epithelium was not activated by anticholinergic administration. Thus, anticholinergics suppress urine production via an increase in urine reabsorption in the kidneys' collecting duct cells via AQP2.

Expression of mRNA for natriuretic peptide receptor subtypes in bovine kidney

1994 ◽  
Vol 267 (2) ◽  
pp. F318-F324 ◽  
Author(s):  
T. Yamamoto ◽  
L. Feng ◽  
T. Mizuno ◽  
S. Hirose ◽  
K. Kawasaki ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Natriuretic Peptide ◽  
Collecting Duct ◽  
Biologically Active ◽  
Ribonuclease Protection Assay ◽  
Receptor Subtypes ◽  
Total Rna ◽  
Duct Cells ◽  
Glomerular Epithelial Cells ◽  
Collecting Duct Cells

The localization of mRNA for atrial natriuretic peptide (ANP) receptor subtypes (A, B, C) in the kidney was examined. Quantitative analysis of the ribonuclease protection assay showed that the numbers of type A receptor (ANPRA) mRNA were 6.9 x 10(7) in the glomeruli and 10.4 x 10(7) molecules/micrograms of total RNA in the inner medulla, and that of type C receptor (ANPRC) mRNA was 21.7 x 10(7) molecules/micrograms of total RNA in the glomeruli. The type B receptor (ANPRB) mRNA was present in smaller numbers (4.5-4.9 x 10(6) molecules/micrograms of total RNA) evenly throughout the kidney fractions. In situ hybridization demonstrated both ANPRA and ANPRC mRNA selectively in the glomerular epithelial cells and ANPRA mRNA in the collecting duct cells of the inner medulla. ANPRC was also localized on the foot processes of glomerular epithelial cells by immunohistochemistry using a specific antibody against the receptor. These results indicate that ANPRA is the major biologically active receptor for the ANP family of hormones in the kidney and is present selectively on the glomerular epithelial cells and inner medullary collecting duct cells. These cells are presumed to play a role in the regulation of glomerular filtration rate and sodium excretion induced by the family of ANP.

Heat stress protein-associated cytoprotection of inner medullary collecting duct cells from rat kidney

1993 ◽  
Vol 265 (3) ◽  
pp. F333-F341 ◽  
Author(s):  
S. C. Borkan ◽  
A. Emami ◽  
J. H. Schwartz
Keyword(s):  
Heat Stress ◽  
Thermal Injury ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Metabolic Effects ◽  
Lactate Dehydrogenase Activity ◽  
Inner Medullary Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells ◽  
Medullary Collecting Duct

Although heat stress proteins (HSPs) mediate thermotolerance, the cellular targets of thermal injury and mechanisms of acquired cytoprotection are unknown. To describe the metabolic effects of hyperthermia and the potential mechanisms of thermotolerance, the following were measured in inner medullary collecting duct cells after a 43 degrees C and/or a 50 degrees C thermal insult: 1) state III mitochondrial respiration (SIII MR), 2) glycolytic rate, 3) lactate dehydrogenase activity, 4) membrane permeability, and 5) HSP 72 content. Compared with controls incubated at 37 degrees C, cells heated to 50 degrees C showed a 30 and 50% reduction in glycolysis and SIII MR, respectively. After heating to 50 degrees C, the cell membrane remained intact and immunoreactive HSP 72 was not detected. In contrast, heating to 43 degrees C induced accumulation of HSP 72 and transiently increased both SIII MR and glycolysis. In addition, prior exposure to 43 degrees C completely prevented the fall in SIII MR and glycolysis anticipated with a subsequent 50 degrees C insult. Cytoprotection gradually diminished over several days and correlated with the disappearance of HSP 72. Preservation of oxidative and anaerobic metabolism associated with HSPs may be important in developing resistance to thermal injury.

scholarly journals Transcriptional profiling of native inner medullary collecting duct cells from rat kidney

2008 ◽  
Vol 32 (2) ◽  
pp. 229-253 ◽  
Author(s):  
Panapat Uawithya ◽  
Trairak Pisitkun ◽  
Brian E. Ruttenberg ◽  
Mark A. Knepper
Keyword(s):  
Signal Intensity ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Transcriptional Profiling ◽  
High Signal ◽  
Inner Medullary Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells ◽  
Medullary Collecting Duct ◽  
V2 Vasopressin Receptor

Vasopressin acts on the inner medullary collecting duct (IMCD) in the kidney to regulate water and urea transport. To obtain a “parts list” of gene products expressed in the IMCD, we carried out mRNA profiling of freshly isolated rat IMCD cells using Affymetrix Rat 230 2.0 microarrays with ∼31,000 features; 7,913 annotated transcripts were found to be expressed above background in the IMCD cells. We have created a new online database (the “IMCD Transcriptome Database;” http://dir.nhlbi.nih.gov/papers/lkem/imcdtr/ ) to make the results publicly accessible. Among the 30 transcripts with the greatest signals on the arrays were 3 water channels: aquaporin-2, aquaporin-3, and aquaporin-4, all of which have been reported to be targets for regulation by vasopressin. In addition, the transcript with the greatest signal among members of the solute carrier family of genes was the UT-A urea transporter ( Slc14a2), which is also regulated by vasopressin. The V2 vasopressin receptor was strongly expressed, but the V1a and V1b vasopressin receptors did not produce signals above background. Among the 200 protein kinases expressed, the serum-glucocorticoid-regulated kinase ( Sgk1) had the greatest signal intensity in the IMCD. WNK1 and WNK4 were also expressed in the IMCD with a relatively high signal intensity, as was protein kinase A (β-catalytic subunit). In addition, a large number of transcripts corresponding to A kinase anchoring proteins and 14-3-3 proteins (phospho-S/T-binding proteins) were expressed. Altogether, the results combine with proteomics studies of the IMCD to provide a framework for modeling complex interaction networks responsible for vasopressin action in collecting duct cells.

scholarly journals Urinary reabsorption in the rat kidney by anticholinergics

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Hideki Oe ◽  
Hatsumi Yoshiki ◽  
Xinmin Zha ◽  
Hisato Kobayashi ◽  
Yoshitaka Aoki ◽  
...  
Keyword(s):  
Absorption Rate ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Intracellular Camp ◽  
Dependent Manner ◽  
Bladder Epithelium ◽  
Duct Cells ◽  
Urine Production ◽  
Saline Administration ◽  
Collecting Duct Cells

AbstractAnticholinergics, therapeutic agents for overactive bladder, are clinically suggested to reduce urine output. We investigated whether this effect is due to bladder or kidney urine reabsorption. Various solutions were injected into the bladder of urethane-anesthetized SD rats. The absorption rate for 2 h was examined following the intravenous administration of the anticholinergics imidafenacin (IM), atropine (AT), and tolterodine (TO). The bilateral ureter was then canulated and saline was administered to obtain a diuretic state. Anticholinergics or 1-deamino-[8-D-arginine]-vasopressin (dDAVP) were intravenously administered. After the IM and dDAVP administrations, the rat kidneys were immunostained with AQP2 antibody, and intracellular cAMP was measured. The absorption rate was ~ 10% of the saline injected into the bladder and constant even when anticholinergics were administered. The renal urine among peaked 2 h after the saline administration. Each of the anticholinergics significantly suppressed the urine production in a dose-dependent manner, as did dDAVP. IM and dDAVP increased the intracellular cAMP levels and caused the AQP2 molecule to localize to the collecting duct cells' luminal side. The urinary reabsorption mechanism through the bladder epithelium was not activated by anticholinergic administration. Thus, anticholinergics suppress urine production via an increase in urine reabsorption in the kidneys' collecting duct cells via AQP2.

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