scholarly journals MicroRNA-194 (miR-194) regulates ROMK channel activity by targeting intersectin 1

2014 ◽  
Vol 306 (1) ◽  
pp. F53-F60 ◽  
Author(s):  
Dao-Hong Lin ◽  
Peng Yue ◽  
Chengbiao Zhang ◽  
Wen-Hui Wang
Keyword(s):  
Collecting Duct ◽  
Luciferase Reporter ◽  
Pcr Analysis ◽  
Seed Sequence ◽  
Cortical Collecting Duct ◽  
Channel Activity ◽  
Luciferase Reporter Gene ◽  
High K ◽  
Low K

The aim of the study is to explore the role of miR-194 in mediating the effect of high-K (HK) intake on ROMK channel. Northern blot analysis showed that miR-194 was expressed in kidney and that HK intake increased while low-K intake decreased the expression of miR-194. Real-time PCR analysis further demonstrated that HK intake increased the miR-194 expression in the cortical collecting duct. HK intake decreased the expression of intersectin 1 (ITSN1) which enhanced With-No-Lysine Kinase (WNK)-induced endocytosis of ROMK. Expression of miR-194 mimic decreased luciferase reporter gene activity in HEK293 T cells transfected with ITSN-1–3′UTR containing the complementary seed sequence for miR-194. In contrast, transfection of miR-194 inhibitor increased the luciferase activity. This effect was absent in the cells transfected with mutated 3′UTR of ITSN1 in which the complimentary seed sequence was deleted. Moreover, the inhibition of miR-194 expression increased the protein level of endogenous ITSN1 in HEK293T cells. Expression of miR-194 mimic also decreased the translation of exogenous ITSN1 in the cells transfected with the ITSN1 containing 3′UTR but not with 3′UTR-free ITSN1. Expression of pre-miR-194 increased K currents and ROMK expression in the plasma membrane in ROMK-transfected cells. Coexpression of ITSN1 reversed the stimulatory effect of miR-194 on ROMK channels. This effect was reversed by coexpression of ITSN1. We conclude that miR-194 regulates ROMK channel activity by modulating ITSN1 expression thereby enhancing ITSN1/WNK-dependent endocytosis. It is possible that miR-194 is involved in mediating the effect of a HK intake on ROMK channel activity.

scholarly journals Angiotensin II type 2 receptor regulates ROMK-like K+ channel activity in the renal cortical collecting duct during high dietary K+ adaptation

2014 ◽  
Vol 307 (7) ◽  
pp. F833-F843 ◽  
Author(s):  
Yuan Wei ◽  
Yi Liao ◽  
Beth Zavilowitz ◽  
Jin Ren ◽  
Wen Liu ◽  
...  
Keyword(s):  
Collecting Duct ◽  
No Synthase ◽  
K Channel ◽  
Ang Ii ◽  
Cortical Collecting Duct ◽  
Channel Activity ◽  
High K ◽  
Pka Pathway

The kidney adjusts K+ excretion to match intake in part by regulation of the activity of apical K+ secretory channels, including renal outer medullary K+ (ROMK)-like K+ channels, in the cortical collecting duct (CCD). ANG II inhibits ROMK channels via the ANG II type 1 receptor (AT1R) during dietary K+ restriction. Because AT1Rs and ANG II type 2 receptors (AT2Rs) generally function in an antagonistic manner, we sought to characterize the regulation of ROMK channels by the AT2R. Patch-clamp experiments revealed that ANG II increased ROMK channel activity in CCDs isolated from high-K+ (HK)-fed but not normal K+ (NK)-fed rats. This response was blocked by PD-123319, an AT2R antagonist, but not by losartan, an AT1R antagonist, and was mimicked by the AT2R agonist CGP-42112. Nitric oxide (NO) synthase is present in CCD cells that express ROMK channels. Blockade of NO synthase with N-nitro-l-arginine methyl ester and free NO with 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide potassium salt completely abolished ANG II-stimulated ROMK channel activity. NO enhances the synthesis of cGMP, which inhibits phosphodiesterases (PDEs) that normally degrade cAMP; cAMP increases ROMK channel activity. Pretreatment of CCDs with IBMX, a broad-spectrum PDE inhibitor, or cilostamide, a PDE3 inhibitor, abolished the stimulatory effect of ANG II on ROMK channels. Furthermore, PKA inhibitor peptide, but not an activator of the exchange protein directly activated by cAMP (Epac), also prevented the stimulatory effect of ANG II. We conclude that ANG II acts at the AT2R to stimulate ROMK channel activity in CCDs from HK-fed rats, a response opposite to that mediated by the AT1R in dietary K+-restricted animals, via a NO/cGMP pathway linked to a cAMP-PKA pathway.

scholarly journals MicroRNA-141 Targets Sirt1 and Inhibits Autophagy to Reduce HBV Replication

2017 ◽  
Vol 41 (1) ◽  
pp. 310-322 ◽  
Author(s):  
Ying Yang ◽  
Yanning Liu ◽  
Jihua Xue ◽  
Zhenggang Yang ◽  
Yu Shi ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Virus Replication ◽  
Luciferase Reporter ◽  
Pcr Analysis ◽  
Luciferase Reporter Gene ◽  
Gene Assay ◽  
B Virus

Background/Aims: About 400 million individuals are chronically infected with hepatitis B virus, at high risk of developing liver cirrhosis and hepatocellular carcinoma. Recent studies have demonstrated an interaction between hepatitis B virus replication and autophagy activity of hepatocytes. In the present study, we aimed to investigate the role of miR-141 in regulating autophagy and hepatitis B virus replication. Methods: The expression of HBV-DNA, miR-141 and Sirt1 mRNA was determined by quantitative real-time PCR analysis. The expression of HBsAg and HBeAg was determined by ELISA. Western blotting was performed to detect protein expression. The LC3 puncta was determined by immunofluorescence. To test whether miR-141 directly regulate the expression level of Sirt1 mRNA, dual-luciferase reporter gene assay was performed. Results: In vitro studies showed that miR-141 mimic inhibited the autophagic response, hepatitis B virus and the expression of Sirt1 in hepatocytes. And transfection with miR-141 inhibitor enhanced autophagic response and Sirt1 expression. The autophagy induced by overexpression of Sirt1 was inhibited by miR-141 mimic. In addition, miR-141 mimic also decreased the expression of Sirt1 mRNA. Sirt1 was predicted as a potential miR-141 target by bioinformatic analysis of its 3'-UTR, and confirmed by luciferase reporter assays which analyzing the interaction of miR-141 with the wild- type or the mutated Sirt1 3’-UTR. Conclusion: We have therefore demonstrated a role of miR-141 in regulating autophagy-mediated hepatitis B virus inhibition by targeting Sirt1, and may provide potential targets for drug development.

scholarly journals Role of WNK4 and kidney-specific WNK1 in mediating the effect of high dietary K+ intake on ROMK channel in the distal convoluted tubule

2018 ◽  
Vol 315 (2) ◽  
pp. F223-F230 ◽  
Author(s):  
Peng Wu ◽  
Zhong-Xiuzi Gao ◽  
Xiao-Tong Su ◽  
David H. Ellison ◽  
Juliette Hadchouel ◽  
...  
Keyword(s):  
Renal Clearance ◽  
Collecting Duct ◽  
Distal Convoluted Tubule ◽  
Cortical Collecting Duct ◽  
Cell Models ◽  
High K ◽  
Cell Recording ◽  
Clearance Study ◽  
Stimulation Of

With-no-lysine kinase 4 (WNK4) and kidney-specific (KS)-WNK1 regulate ROMK (Kir1.1) channels in a variety of cell models. We now explore the role of WNK4 and KS-WNK1 in regulating ROMK in the native distal convoluted tubule (DCT)/connecting tubule (CNT) by measuring tertiapin-Q (TPNQ; ROMK inhibitor)-sensitive K+ currents with whole cell recording. TPNQ-sensitive K+ currents in DCT2/CNT of KS- WNK1−/− and WNK4−/− mice were significantly smaller than that of WT mice. In contrast, the basolateral K+ channels (a Kir4.1/5.1 heterotetramer) in the DCT were not inhibited. Moreover, WNK4−/− mice were hypokalemic, while KS- WNK1−/− mice had normal plasma K+ levels. High K+ (HK) intake significantly increased TPNQ-sensitive K+ currents in DCT2/CNT of WT and WNK4−/− mice but not in KS- WNK1−/− mice. However, TPNQ-sensitive K+ currents in the cortical collecting duct (CCD) were normal not only under control conditions but also significantly increased in response to HK in KS- WNK1−/− mice. This suggests that the deletion of KS-WNK1-induced inhibition of ROMK occurs only in the DCT2/CNT. Renal clearance study further demonstrated that the deletion of KS-WNK1 did not affect the renal ability of K+ excretion under control conditions and during increasing K+ intake. Also, HK intake did not cause hyperkalemia in KS- WNK1−/− mice. We conclude that KS-WNK1 but not WNK4 is required for HK intake-induced stimulation of ROMK activity in DCT2/CNT. However, KS-WNK1 is not essential for HK-induced stimulation of ROMK in the CCD, and the lack of KS-WNK1 does not affect net renal K+ excretion.

Abstract 134: Activation of the Mineralocorticoid Receptor by O-glycosylation Through Hyperglycemia

Hypertension ◽  
2015 ◽  
Vol 66 (suppl_1) ◽  
Author(s):  
Maniselvan Kuppusamy ◽  
Elise Gomez-Sanchez ◽  
Celso Gomez-Sanchez
Keyword(s):  
High Glucose ◽  
Mineralocorticoid Receptor ◽  
Transcriptional Activity ◽  
Collecting Duct ◽  
Cardiovascular Complications ◽  
Luciferase Reporter ◽  
Cortical Collecting Duct ◽  
Luciferase Reporter Gene ◽  
Reporter Activity ◽  
The Metabolic Syndrome

Introduction: Hypertension and diabetes are independent risk factors for cardiovascular disease, however why they frequently occur together is not clear. Inappropriate mineralocorticoid receptor (MR) activation is associated with diabetes and the metabolic syndrome, as well as hypertension and abnormal cardiovascular remodeling. MR antagonists are effective in reducing hypertension and delaying the onset of renal and cardiovascular complications in diabetes despite circulating aldosterone levels that are within normal limits. Glucose concentrations increase O-glycosylation of many proteins, thus alter their function. Hence, we hypothesized that increased O-GlcNac modification of the MR by high glucose enhances MR activation. Methods: MR transcriptional activity was studied in a mouse cortical collecting duct (M1) cell line stably transfected with a cDNA construct including the MR and one with a hormone-response element driving a Gaussia luciferase reporter gene. The cells were incubated for 48 h with low (5mM) or high (25mM) glucose media with and without Thiamet-G (TMG), an O-GlcNAcase inhibitor to inhibit deglycosylation, and 6-diazo-5-oxonorleucine (DON), a glucosamine-fructose-6-phosphate amidotransferase inhibitor (GFAT) to reduce O-GlcNAc levels. Additionally, MR and GR antagonists were used to identify receptor specificity under low and high glucose conditions. O-GlcNac-modified MR was co-immunoprecipitated with an MR antibody and detected with an O-GlcNAc antibody. Results: 1. Co-immunoprecipitation assays showed that high glucose and TMG increased O-GlcNac-MR by 3-fold. 2. Compared to low glucose, treatment with high glucose and with TMG increased the transcriptional activity of MR by 300%. 3. DON decreased MR-reporter activity by 75%. 4. High glucose alone had no significant basal effect but significantly increased MR activation by aldosterone. 5. MR reporter activity was increased similarly by aldosterone and corticosterone. Conclusion: High glucose increased glycosylation of the MR, augmenting its transcriptional activity. Enhancement of MR activation by hyperglycemia may explain how MRs play a significant role in the cardiorenal pathology in Diabetes.

scholarly journals Protein phosphatase 1 modulates the inhibitory effect of With-no-Lysine kinase 4 on ROMK channels

2012 ◽  
Vol 303 (1) ◽  
pp. F110-F119 ◽  
Author(s):  
Dao-Hong Lin ◽  
Peng Yue ◽  
Jesse Rinehart ◽  
Peng Sun ◽  
Zhijian Wang ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Collecting Duct ◽  
Inhibitory Effect ◽  
Protein Phosphatase 1 ◽  
Cortical Collecting Duct ◽  
Channel Activity ◽  
Serine Residue ◽  
Volume Depletion ◽  
K Secretion

With-no-Lysine kinase 4 (WNK4) inhibited ROMK (Kir1.1) channels and the inhibitory effect of WNK4 was abolished by serum-glucocorticoid-induced kinase 1 (SGK1) but restored by c-Src. The aim of the present study is to explore the mechanism by which Src-family tyrosine kinase (SFK) modulates the effect of SGK1 on WNK4 and to test the role of SFK-WNK4-SGK1 interaction in regulating ROMK channels in the kidney. Immunoprecipitation demonstrated that protein phosphatase 1 (PP1) binds to WNK4 at amino acid (aa) residues 695–699 (PP1#1) and at aa 1211–1215 (PP1#2). WNK4−PP1#1 and WNK4−PP1#2, in which the PP1#1 or PP1#2 binding site was deleted or mutated, inhibited ROMK channels as potently as WNK4. However, c-Src restored the inhibitory effect of WNK4 but not WNK4−PP1#1 on ROMK channels in the presence of SGK1. Moreover, expression of c-Src inhibited SGK1-induced phosphorylation of WNK4 but not WNK4−PP1#1 at serine residue 1196 (Ser1196). In contrast, coexpression of c-Src restored the inhibitory effect of WNK4−PP1#2 on ROMK in the presence of SGK1 and diminished SGK1-induced WNK4 phosphorylation at Ser1196 in cells transfected with WNK4−PP1#2. This suggests the possibility that c-Src regulates the interaction between WNK4 and SGK1 through activating PP1 binding to aa 695–9 thereby decreasing WNK4 phosphorylation and restoring the inhibitory effect of WNK4. This mechanism plays a role in suppressing ROMK channel activity during the volume depletion because inhibition of SFK or serine/threonine phosphatases increases ROMK channel activity in the cortical collecting duct of rats on a low-Na diet. We conclude that regulation of phosphatase activity by SFK plays a role in determining the effect of aldosterone on ROMK channels and on renal K secretion.

scholarly journals Conservation of Na+ vs. K+ by the rat cortical collecting duct

2011 ◽  
Vol 301 (1) ◽  
pp. F14-F20 ◽  
Author(s):  
Gustavo Frindt ◽  
Véronique Houde ◽  
Lawrence G. Palmer
Keyword(s):  
Collecting Duct ◽  
Immunoblot Analysis ◽  
Cortical Collecting Duct ◽  
Channel Activity ◽  
Distal Nephron ◽  
Whole Cell ◽  
Regulation Of Transport ◽  
Low K ◽  
Na Depletion ◽  
K Depletion

Regulation of transport by principal cells of the distal nephron contributes to maintenance of Na+ and K+ homeostasis. To assess which of these ions is given a higher priority by these cells, we investigated the upregulation of epithelial Na+ channels (ENaC) in the rat cortical collecting duct (CCD) during Na depletion with and without simultaneous K depletion. ENaC activity, assessed as whole cell amiloride-sensitive current in split-open tubules, was 260 ± 40 pA/cell in K-repleted but virtually undetectable (3 ± 1 pA/cell) in K-depleted animals. This difference was confirmed biochemically by the reduced amounts of the cleaved forms of both the α-ENaC and γ-ENaC subunits measured in immunoblots. In contrast, in K-depleted rats, simultaneously reducing Na intake did not affect the activity of ROMK channels, assessed as tertiapin-Q-sensitive whole cell currents, in the CCDs. The lack of Na current in K-depleted animals was the result of reduced levels of aldosterone in plasma, rather than a reduced sensitivity to the hormone. However, rats on a low-Na, low-K diet for 1 wk did not excrete more Na than those on a low-Na, control-K diet for the same period of time. Immunoblot analysis indicated increased levels of the thiazide-sensitive NaCl cotransporter and the apical Na-H exchanger NHE3. This suggests that with reduced K intake, Na balance is maintained despite reduced aldosterone and Na+ channel activity by upregulation of Na+ transport in upstream segments. Under these conditions, Na+ transport by the aldosterone-sensitive distal nephron is reduced, despite the low-Na intake to minimize K+ secretion and urinary K losses.

scholarly journals Dietary K regulates ROMK channels in connecting tubule and cortical collecting duct of rat kidney

2009 ◽  
Vol 296 (2) ◽  
pp. F347-F354 ◽  
Author(s):  
Gustavo Frindt ◽  
Anish Shah ◽  
Johan Edvinsson ◽  
Lawrence G. Palmer
Keyword(s):  
Collecting Duct ◽  
Rat Kidney ◽  
Outward Current ◽  
Equilibrium Potential ◽  
Cortical Collecting Duct ◽  
Pipette Solution ◽  
Connecting Tubule ◽  
Outward Currents ◽  
High K ◽  
Low K

The activity of ROMK channels in rat kidney tubule cells was assessed as tertiapin-Q (TPNQ)-sensitive current under whole cell clamp conditions. With an external K+ concentration of 5 mM and an internal K+ concentration of 140 mM and the membrane potential clamped to 0 mV, TPNQ blocked outward currents in principal cells of the cortical collecting duct (CCD) outer medullary collecting duct and connecting tubule (CNT). The apparent Ki was 5.0 nM, consistent with its interaction with ROMK. The TPNQ-sensitive current reversed at voltages close to the equilibrium potential for K+. The currents were reduced when the pipette solution contained ATP. In the CCD, the average TPNQ-sensitive outward current ( ISK) was 476 ± 48 pA/cell in control animals on a 1% KCl diet. ISK increased to 1,255 ± 140 pA when animals were maintained on a high-K (10% KCl) diet for 7 days and decreased to 314 ± 46 pA after 7 days on a low-K (0.1% KCl) diet. In the CNT, ISK was 360 ± 30 pA on control, 1,160 ± 110 on high-K, and 166 ± 16 pA on low-K diets. The results indicate that ROMK channel activity is highly regulated by dietary K in both the CCD and the CNT.

Regulation of ATP-sensitive K+ channel by membrane-bound protein phosphatases in rat principal tubule cell

1995 ◽  
Vol 269 (3) ◽  
pp. F355-F362 ◽  
Author(s):  
M. Kubokawa ◽  
C. M. McNicholas ◽  
M. A. Higgins ◽  
W. Wang ◽  
G. Giebisch
Keyword(s):  
Katp Channel ◽  
Collecting Duct ◽  
K Channel ◽  
Cortical Collecting Duct ◽  
Channel Activity ◽  
Inhibitory Effects ◽  
Patch Clamp Technique ◽  
Cytosolic Side ◽  
Membrane Bound

The role of membrane-bound protein serine/threonine phosphatases (PP) in modulating the renal ATP-sensitive K+ (KATP) channel was examined using the patch-clamp technique in principal cells of rat cortical collecting duct. In the absence of ATP, channel activity rapidly (11.2 s) declines (channel "rundown") upon excision of the membrane patches into control bath solutions (1 mM Mg2+, Ca2+ free). Both orthovanadate (5 mM), a broad-spectrum inhibitor of phosphatases except for Ca(2+)-dependent PP (PP-2B), and okadaic acid (OA, 1 microM), a potent inhibitor of PP types 1 and 2A (PP-1 and PP-2A), significantly slowed channel rundown. Removal of Mg2+ from the bath also slowed the rundown process. Incubation of cells with OA in the absence of Mg2+ or with orthovanadate in ATP-free solution maintained channel activity at levels of approximately 70% of control values for 3 min after membrane excision. In contrast, Ca2+ (0.1 mM) and calmodulin (1 microM) in the presence of 1 mM Mg2+, a condition in which PP-2B is stimulated, had no significant effect on the channel activity that persisted in the presence of OA and orthovanadate. Application of exogenous PP-2A (1 U/ml) to the cytosolic side of membrane in inside-out patches significantly inhibited channel activity to 35.0% of control, but the inhibitory-effects of PP-1 (1 U/ml) and PP-2B (20 micrograms/ml) were minor. These results suggest that rundown of the renal KATP channel after membrane excision results mainly from dephosphorylation of the channel or an associated protein by membrane-bound phosphatases.(ABSTRACT TRUNCATED AT 250 WORDS)

Role of the cytoskeleton in mediating effect of vasopressin and herbimycin A on secretory K channels in CCD

2002 ◽  
Vol 282 (4) ◽  
pp. F680-F686 ◽  
Author(s):  
Yuan Wei ◽  
Wen-Hui Wang
Keyword(s):  
Collecting Duct ◽  
Cytochalasin D ◽  
Mediating Effect ◽  
Microtubule Assembly ◽  
Sk Channels ◽  
Cortical Collecting Duct ◽  
Channel Activity ◽  
Patch Clamp Technique ◽  
Herbimycin A

We have previously demonstrated that inhibiting protein tyrosine kinase (PTK) and stimulating protein kinase A (PKA) increase the activity of the small-conductance K (SK) channel in the cortical collecting duct (CCD) of rat kidneys (Cassola AC, Giebisch G, and Wang WH. Am J Physiol Renal Fluid Electrolyte Physiol 264: F502–F509, 1993; Wang WH, Lerea KM, Chan M, and Giebisch G. Am J Physiol Renal Physiol 278: F165–F171, 2000). In the present study, we used the patch-clamp technique to study the role of the cytoskeleton in mediating the effect of herbimycin A, an inhibitor of PTK, and vasopressin on the SK channels in the CCD. The addition of colchicine, an inhibitor of microtubule assembly, or taxol, an agent that blocks microtubule reconstruction, had no significant effect on channel activity. However, colchicine and taxol treatment completely abolished the stimulatory effect of herbimycin A on the SK channels in the CCD. Removal of the microtubule inhibitors restored the stimulatory effect of herbimycin A. In contrast, treatment of the tubules with either taxol or colchicine did not block the stimulatory effect of vasopressin on the SK channels. Moreover, the effect of herbimycin A on the SK channels was also absent in the CCDs treated with either cytochalasin D or phalloidin. In contrast, the stimulatory effect of vasopressin was still observed in the tubules treated with phalloidin. However, cytochalasin D treatment abolished the effect of vasopressin on the SK channels. Finally, the effects of vasopressin and herbimycin A are additive because inhibiting PTK can still increase the channel activity in CCD that has been challenged by vasopressin. We conclude that an intact cytoskeleton is required for the effect on the SK channels of inhibiting PTK and that the SK channels that are activated by inhibiting PTK were differently regulated from those stimulated by vasopressin.

scholarly journals Kidney-specific WNK1 inhibits sodium reabsorption in the cortical thick ascending limb

2012 ◽  
Vol 303 (5) ◽  
pp. F667-F673 ◽  
Author(s):  
Chih-Jen Cheng ◽  
Thao Truong ◽  
Michel Baum ◽  
Chou-Long Huang
Keyword(s):  
Collecting Duct ◽  
Urine Volume ◽  
Sodium Reabsorption ◽  
Renal Tubules ◽  
Thick Ascending Limb ◽  
Cortical Collecting Duct ◽  
Wild Type ◽  
High K

Kidney-specific WNK1 (KS-WNK1) is a variant of full-length WNK1. Previous studies have reported that KS-WNK1 is predominantly expressed in the distal convoluted tubule (DCT) where it regulates sodium-chloride cotransporter. The role of KS-WNK1 in other nephron segments is less clear. Here, we measured the expression of KS-WNK1 transcript in microdissected renal tubules and found that KS-WNK1 was most abundant in the DCT, followed by cortical thick ascending limb (cTAL), connecting tubule, and cortical collecting duct. A high K+ diet enhanced the expression of KS-WNK1 in the DCT and cTAL, selectively. It has been reported that a high-K diet suppresses Na+ reabsorption in TAL. To understand the role of KS-WNK1 in Na+ transport in cTAL and the regulation by dietary K+, we examined Na+ reabsorption using in vitro microperfusion in cTAL isolated from KS-WNK1-knockout mice and wild-type littermates fed either a control-K+ or high-K+ diet. Furosemide-sensitive Na+ reabsorption in cTAL was higher in KS-WNK1-knockout (KO) mice than in wild-type. A high-K+ diet inhibited Na+ reabsorption in cTAL from wild-type mice, but the inhibition was eliminated in KS-WNK1-KO mice. We further examined the role of KS-WNK1 using transgenic mice that overexpress KS-WNK1. Na+ reabsorption in cTAL was lower in transgenic than in wild-type mice. In whole animal clearance studies, a high-K+ diet increased daily urine volume and urinary Na+ and K+ excretion in wild-type mice, which was blunted in KS-WNK1-KO mice. Thus KS-WNK1 inhibits Na+ reabsorption in cTAL and mediates the inhibition of Na+ reabsorption in the segment by a high-K diet.

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