Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis

Huber, Saskia; Asan, Esther; Jöns, Thomas; Kerscher, Christiane; Püschel, Bernd; Drenckhahn, Detlev

doi:10.1152/ajprenal.1999.277.6.f841

Cited by 27 publications

(24 citation statements)

References 21 publications

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“…For identification of V 2 mRNA-expressing tubular segments, rabbit polyclonal antibody against V2R was applied (39). For further cell-type-specific identification of the in situ signal, segment-specific antibodies were applied using double labeling or separate labeling of consecutive sections (3,6,7 (7); goat anti-AQP-2 antibody (Santa Cruz Biotechnology) for CNT, CCD, and MCD principal cells; and rabbit anti-vacuolar H ϩ -ATPase antibody (Santa Cruz Biotechnology) or rabbit anti-anion exchanger 1 (AE1) (16) antibody for intercalated cells. For separate immunohistochemical labeling, sections were dewaxed and boiled in citrate buffer (pH 6.0) for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Vasopressin V₂receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Mutig¹,

Paliege²,

Kahl³

et al. 2007

American Journal of Physiology-Renal Physiology

136

127

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Mutig K, Paliege A, Kahl T, Jöns T, Mü ller-Esterl W, Bachmann S. Vasopressin V 2 receptor expression along rat, mouse, and human renal epithelia with focus on TAL. Am J Physiol Renal Physiol 293: F1166-F1177, 2007. First published July 11, 2007; doi:10.1152/ajprenal.00196.2007.-In renal epithelia, vasopressin influences salt and water transport, chiefly via vasopressin V 2 receptors (V2Rs) linked to adenylyl cyclase. A combination of vasopressin-induced effects along several distinct portions of the nephron and collecting duct system may help balance the net effects of antidiuresis in cortex and medulla. Previous studies of the intrarenal distribution of V 2Rs have been inconclusive with respect to segmentand cell-type-related V 2R expression. Our study therefore aimed to present a high-resolution analysis of V 2R mRNA expression in rat, mouse, and human kidney epithelia, supplemented with immunohistochemical data. Cell types of the renal tubule were identified histochemically using specific markers. Pronounced V 2R signal in thick ascending limb (TAL) was corroborated functionally; phosphorylation of Na ϩ -K ϩ -2Cl Ϫ cotransporter type 2 (NKCC2) was established in cultured TAL cells from rabbit and in rats with diabetes insipidus that were treated with the V 2R agonist desmopressin. We found solid expression of V 2R mRNA in medullary TAL (MTAL), macula densa, connecting tubule, and cortical and medullary collecting duct and weaker expression in cortical TAL and distal convoluted tubule in all three species. Additional V 2R immunostaining of kidneys and rabbit TAL cells confirmed our findings. In agreement with strong V 2R expression in MTAL, kidneys from rats with diabetes insipidus and cultured TAL cells revealed sharp, selective increases in NKCC2 phosphorylation upon desmopressin treatment. Macula densa cells constitutively showed strong NKCC2 phosphorylation. Results suggest comparably significant effects of vasopressin-induced V 2R signaling in MTAL and in connecting tubule/collecting duct principal cells across the three species. Strong V 2R expression in macula densa may be related to tubulovascular signal transfer. antidiuretic hormone; thick ascending limb; kidney; sodium-potassiumchloride cotransporter type 2; bumetanide-sensitive cotransporter type 1 ANTIDIURETIC HORMONE [arginine vasopressin (AVP)] serves to regulate body fluid osmolality, blood volume, blood pressure, and vascular tone. In the kidney, two major receptor subtypes [V 1a and V 2 receptors (V 1a R and V 2 R)] have been characterized (22,24). V 1a Rs are principally localized in the renal vasculature and glomeruli and mediate the vasopressor effect of AVP (2, 32). The tubular antidiuretic effect of AVP is mediated by the V 2 R and adenylyl cyclase-dependent cAMP signaling (13,22). Since the early work of Morel (25), sites of V 2 R-mediated AVP action along the nephron have been defined at different levels, such as transport (13,15,17), ligand binding (2, 35, 44), receptor mRNA expression (9, 32, 47), and immunohistochemical localizat...

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Section: Methodsmentioning

confidence: 99%

Vasopressin V₂receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Mutig¹,

Paliege²,

Kahl³

et al. 2007

American Journal of Physiology-Renal Physiology

136

127

View full text Add to dashboard Cite

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“…This provides an attractive mechanism that would help explain observations from animal studies, that suggest that ICs increase kAE1 levels at the basolateral membrane during chronic metabolic acidosis and reduce kAE1 levels during acute metabolic alkalosis (Fejes-Toth et al, 1994;Huber et al, 1999;Sabolic et al, 1997;Verlander et al, 1994). This is similar to the regulation of Kir1.1 (ROMK) levels by tyrosine phosphorylation, depending on the availability of dietary potassium (Wang et al, 2002;Wei et al, 2001).…”

Section: Journal Of Cell Science 121 (20)mentioning

confidence: 86%

“…Since kAE1 localisation appears to be influenced by acidosis or alkalosis in the animal models (Huber et al, 1999;Sabolic et al, Journal of Cell Science 121 (20) 1997), we tested the effects of lowering the pH of the medium (mimicking acidosis) or raising pH using NaHCO 3 (mimicking alkalosis) on kAE1 tyrosine phosphorylation (Fig. 5A).…”

Section: An N-terminal Domain Tyrosine (Y359) Is Critical For Basolatmentioning

confidence: 99%

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Human kidney anion exchanger 1 localisation in MDCK cells is controlled by the phosphorylation status of two critical tyrosines

Williamson

Brown

Mawby

et al. 2008

Journal of Cell Science

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An important question in renal physiology is how the α-intercalated cells of the kidney regulate the distribution of the basolateral kidney anion exchanger 1 (kAE1) according to systemic acid-base status. Previous work using a MDCKI model system demonstrated that kAE1 basolateral targeting requires an N-terminal determinant and a critical C-terminal tyrosine (Y904). Here, we show that the N-terminal determinant is residue Y359, because a Y359A substitution mutant was mistargeted to the apical membrane. Further determinants might exist because a range of N-terminal kAE1 truncations that contained Y359 were incorrectly targeted to the TGN. Y359 and Y904 in kAE1 are phosphorylated upon pervanadate treatment and this phosphorylation is sensitive to specific Src kinase family inhibitors. We tested a range of stimuli on this model system and only the application of high nonphysiological concentrations of extracellular bicarbonate, and to a lesser extent hypertonicity or hyperosmolarity, induced tyrosine phosphorylation of kAE1. Treatment with pervanadate caused internalisation of kAE1 from the plasma membrane, but treatment with high concentrations of bicarbonate did not, because of the hypertonicity of the solution. We propose that α-intercalated cells control the distribution of kAE1 by reversible phosphorylation of tyrosine residues Y359 and Y904.

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“…The present study thus explored whether liver tissue expresses SLC26A4 and whether hepatic SLC26A4 expression is influenced by acid-base balance in a similar way as in the kidney. To this end, SLC26A4 transcript and protein levels were quantified in liver and kidney from mice treated with bicarbonate to induce metabolic alkalosis [20], ammonium chloride to trigger metabolic acidosis [21] and acetazolamide to inhibit carbonic anhydrase [22].…”

Section: Introductionmentioning

confidence: 99%

Impact of Bicarbonate, Ammonium Chloride, and Acetazolamide on Hepatic and Renal SLC26A4 Expression

Alesutan¹,

Daryadel²,

Mohebbi³

et al. 2011

Cell Physiol Biochem

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SLC26A4 encodes pendrin, a transporter exchanging anions such as chloride, bicarbonate, and iodide. Loss of function mutations of SLC26A4 cause Pendred syndrome characterized by hearing loss and enlarged vestibular aqueducts as well as variable hypothyroidism and goiter. In the kidney, pendrin is expressed in the distal nephron and accomplishes HCO(3)(-) secretion and Cl(-) reabsorption. Renal pendrin expression is regulated by acid-base balance. The liver contributes to acid-base regulation by producing or consuming glutamine, which is utilized by the kidney for generation and excretion of NH(4)(+), paralleled by HCO(3)(-) formation. Little is known about the regulation of pendrin in liver. The present study thus examined the expression of Slc26a4 in liver and kidney of mice drinking tap water without or with NaHCO(3) (150 mM), NH(4)Cl (280 mM) or acetazolamide (3.6 mM) for seven days. As compared to Gapdh transcript levels, Slc26a4 transcript levels were moderately lower in liver than in renal tissue. Slc26a4 transcript levels were not significantly affected by NaHCO(3) in liver, but significantly increased by NaHCO(3) in kidney. Pendrin protein expression was significantly enhanced in kidney and reduced in liver by NaHCO(3). Slc26a4 transcript levels were significantly increased by NH(4)Cl and acetazolamide in liver, and significantly decreased by NH(4)Cl and by acetazolamide in kidney. NH(4)Cl and acetazolamide reduced pendrin protein expression significantly in kidney, but did not significantly modify pendrin protein expression in liver. The observations point to expression of pendrin in the liver and to opposite effects of acidosis on pendrin transcription in liver and kidney. Little is known about the regulation of pendrin in liver. The present study thus examined the expression of Slc26a4 in liver and kidney of mice drinking tap water without or with NaHCO 3 (150 mM), NH 4 Cl (280 mM) or acetazolamide (3.6 mM) for seven days. As compared to Gapdh transcript levels, Slc26a4 transcript levels were moderately lower in liver than in renal tissue. Slc26a4 transcript levels were not significantly affected by NaHCO 3 in liver, but significantly increased by NaHCO 3 in kidney. Pendrin protein expression was significantly enhanced in kidney and reduced in liver by NaHCO 3 . Slc26a4 transcript levels were significantly increased by NH 4 Cl and acetazolamide in liver, and significantly decreased by NH 4 Cl and by acetazolamide in kidney. NH 4 Cl and acetazolamide reduced pendrin protein expression significantly in kidney, but did not significantly modify pendrin protein expression in liver. The observations point to expression of pendrin in the liver and to opposite effects of acidosis on pendrin transcription in liver and kidney.

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Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis

Cited by 27 publications

References 21 publications

Vasopressin V₂receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Vasopressin V₂receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Human kidney anion exchanger 1 localisation in MDCK cells is controlled by the phosphorylation status of two critical tyrosines

Impact of Bicarbonate, Ammonium Chloride, and Acetazolamide on Hepatic and Renal SLC26A4 Expression

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Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis

Cited by 27 publications

References 21 publications

Vasopressin V2receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Vasopressin V2receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Human kidney anion exchanger 1 localisation in MDCK cells is controlled by the phosphorylation status of two critical tyrosines

Impact of Bicarbonate, Ammonium Chloride, and Acetazolamide on Hepatic and Renal SLC26A4 Expression

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Vasopressin V₂receptor expression along rat, mouse, and human renal epithelia with focus on TAL

Vasopressin V₂receptor expression along rat, mouse, and human renal epithelia with focus on TAL