Subtypes of intercalated cells in rat kidney collecting duct defined by antibodies against erythroid band 3 and renal vacuolar H+-ATPase.

Alper, Seth L.; Natale, Joanne; Gluck, Stephen L.; Lodish, Harvey F.; Brown, Dennis

doi:10.1073/pnas.86.14.5429

Cited by 356 publications

(347 citation statements)

References 43 publications

Supporting

Mentioning

328

Contrasting

Order By: Relevance

“…The present studies now confirm that a similar pattern of V1a RNA expression is also seen in human and mouse kidney. The present studies further show expression of V1a in mouse kidney colocalizes with basolateral AE-1 immunoreactivity, consistent with this cell-type being the alpha-intercalated cell (2).…”

Section: Discussionsupporting

confidence: 61%

Axial heterogeneity of vasopressin-receptor subtypes along the human and mouse collecting duct

Carmosino¹,

Brooks²,

Cai³

et al. 2007

American Journal of Physiology-Renal Physiology

View full text Add to dashboard Cite

Vasopressin and vasopressin antagonists are finding expanded use in mouse models of disease and in clinical medicine. To provide further insight into the physiological role of V1a and V2 vasopressin receptors in the human and mouse kidney, intrarenal localization of the receptors mRNA was determined by in situ hybridization. V2-receptor mRNA was predominantly expressed in the medulla, whereas mRNA for V1a receptors predominated in the cortex. The segmental localization of vasopressinreceptor mRNAs was determined using simultaneous in situ hybridization and immunohistochemistry for segment-specific markers, including aquaporin-2, Dolichos biflorus agglutinin, epithelial Na channels, Tamm Horsfall glycoprotein, and thiazide-sensitive Na ϩ -Cl Ϫ cotransporter. Notably, V1a receptor expression was exclusively expressed in V-ATPase/anion exchanger-1-labeled alpha-intercalated cells of the medullary collecting duct in both mouse and human kidney. In cortical collecting ducts, V1a mRNA was more widespread and detected in both principal and intercalated cells. V2-receptor mRNA is diffusely expressed along the collecting ducts in both mouse and human kidney, with higher expression levels in the medulla. These results demonstrate heterogenous axial expression of both V1a and V2 vasopressin receptors along the human and mouse collecting duct. The restricted expression of V1a-receptor mRNA in intercalated cells suggests a role for this receptor in acid-base balance. These findings further suggest distinct regulation of renal transport function by AVP through V1a and V2 receptors in the cortex vs. the medulla. in situ hybridization; vasopressin receptors; intercalated cell ARGININE VASOPRESSIN (AVP) is the key hormone responsible for producing a concentrated urine and is secreted in high concentrations during antidiuresis. At least two different vasopressin

show abstract

Section: Discussionsupporting

confidence: 61%

Axial heterogeneity of vasopressin-receptor subtypes along the human and mouse collecting duct

Carmosino¹,

Brooks²,

Cai³

et al. 2007

American Journal of Physiology-Renal Physiology

View full text Add to dashboard Cite

show abstract

“…Kidney AE1 (kAE1) lacks the first 65 amino acids in humans (8,96). AE1 expression is basolateral and its presence characterizes type A intercalated cells in the collecting system (9). AE1 mediates basolateral release of intracellular bicarbonate against extracellular chloride thereby secreting newly generated bicarbonate into the interstitial space/ blood.…”

Section: Ae1mentioning

confidence: 99%

Regulated acid–base transport in the collecting duct

Wagner

Devuyst

Bourgeois

et al. 2009

Pflugers Arch - Eur J Physiol

161

142

View full text Add to dashboard Cite

The renal collecting system serves the fine-tuning of renal acid-base secretion. Acid-secretory type-A intercalated cells secrete protons via a luminally expressed V-type H(+)-ATPase and generate new bicarbonate released by basolateral chloride/bicarbonate exchangers including the AE1 anion exchanger. Efficient proton secretion depends both on the presence of titratable acids (mainly phosphate) and the concomitant secretion of ammonia being titrated to ammonium. Collecting duct ammonium excretion requires the Rhesus protein RhCG as indicated by recent KO studies. Urinary acid secretion by type-A intercalated cells is strongly regulated by various factors among them acid-base status, angiotensin II and aldosterone, and the Calcium-sensing receptor. Moreover, urinary acidification by H(+)-ATPases is modulated indirectly by the activity of the epithelial sodium channel ENaC. Bicarbonate secretion is achieved by non-type-A intercalated cells characterized by the luminal expression of the chloride/bicarbonate exchanger pendrin. Pendrin activity is driven by H(+)-ATPases and may serve both bicarbonate excretion and chloride reabsorption. The activity and expression of pendrin is regulated by different factors including acid-base status, chloride delivery, and angiotensin II and may play a role in NaCl retention and blood pressure regulation. Finally, the relative abundance of type-A and non-type-A intercalated cells may be tightly regulated. Dysregulation of intercalated cell function or abundance causes various syndromes of distal renal tubular acidosis underlining the importance of these processes for acid-base homeostasis.

show abstract

“…We could not perform double localization studies of RhBG and ankyrin-B, because the anti-RhBG and anti-ankyrin-B used in this study were both raised in rabbit. Thus, to identify precisely the connecting tubules and the collecting ducts, we rather performed double labeling studies using a monoclonal antibody that interacts with the Cl Ϫ /HCO 3 Ϫ exchanger AE1, a specific marker of ␣-intercalated cells of the connecting tubule and the collecting ducts (31). As illustrated in Fig.…”

Section: Rhbg Colocalizes With Ankyrin-g But Not Ankyrin-b In Rat Kmentioning

confidence: 99%

The Ammonium Transporter RhBG

Lopez

Métral

Eladari

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

RhBG is a nonerythroid member of the Rhesus (Rh) protein family, mainly expressed in the kidney and belonging to the Amt/Mep/Rh superfamily of ammonium transporters. The epithelial expression of renal RhBG is restricted to the basolateral membrane of the connecting tubule and collecting duct cells. We report here that sorting and anchoring of RhBG to the basolateral plasma membrane require a cis-tyrosine-based signal and an association with ankyrin-G, respectively. The Rhesus (Rh) 1 family is composed of four protein homologues, Rh, RhAG, RhBG, and RhCG, all of which are predicted to be polytopic transmembrane proteins with 12 membrane spanning domains and intracytoplasmic N and C termini (1). Rh and RhAG are expressed on red cells only, where they define the core of the Rh membrane complex, which also includes the unrelated accessory chains CD47, LW/ICAM-4, and GPB (2, 3). Conversely, RhBG and RhCG are not expressed in erythroid tissues but are both expressed in kidney and differentially in other organs as follows: testis, brain, pancreas, and prostate for RhCG and liver, skin, and ovary for RhBG (4, 5). Primary structure homology (30 -35%) with the methylammonium-ammonium permease/ammonia transporters (Mep/Amt) from the lower organisms and plants has raised the possibility that Rh, RhAG, RhBG, and RhCG should represent the mammalian members of an Amt/Mep/Rh superfamily of ammonium transporters (1, 6, 7). Accordingly, ammonium (NH 4 ϩ and/or NH 3 ) transport capacity of RhAG, RhBG, and RhCG has been demonstrated in different heterologous expression systems (8 -11). Moreover, recent ammonium transport analysis performed in red blood cells from human and mouse genetic variants with Rh and/or RhAG deficiencies indicated that RhAG facilitates NH 3 movement across the red blood cell membrane and thus represents a potential example of gas transporter in mammalian cells (12). Supporting this finding, three-dimensional structure elucidation and transport experiments in an acellular model demonstrated that bacterial AmtB is a channel that conducts uncharged NH 3 (13).Rh proteins also represent, at least in red blood cells, important structural components of the cell membrane, as first evidenced by the morphological abnormalities (stomato-spherocytosis) of Rh null red cells that lack Rh and/or RhAG (2). It has been demonstrated recently that the Rh complex constitutes, as the previously described AE1-protein 4.2-ankyrin and GPCprotein 4.1-p55 complexes (14, 15), a major anchoring site between the red cell membrane bilayer and the underlying spectrin-based skeleton, and that the disruption of this interaction results in part in the morphological abnormalities of Rh null red cells (16 -18). The Rh complex interacts with the erythrocyte skeleton through direct binding of the cytoplasmic C-terminal tails of Rh and RhAG with the second repeat subdomain (D2) of the membrane binding domain of ankyrin-R (18). Based on these results and on the observation that expression of Rh proteins and AE1 (type 1 anion exchanger) is collecti...

show abstract

Subtypes of intercalated cells in rat kidney collecting duct defined by antibodies against erythroid band 3 and renal vacuolar H+-ATPase.

Cited by 356 publications

References 43 publications

Axial heterogeneity of vasopressin-receptor subtypes along the human and mouse collecting duct

Axial heterogeneity of vasopressin-receptor subtypes along the human and mouse collecting duct

Regulated acid–base transport in the collecting duct

The Ammonium Transporter RhBG

Contact Info

Product

Resources

About