Angiotensin II Activates H+-ATPase in Type A Intercalated Cells

Pech, Vladimir; Zheng, Wencui; Pham, Truyen D.; Verlander, Jill W.; Wall, Susan M.

doi:10.1681/asn.2007030277

Cited by 64 publications

(58 citation statements)

References 43 publications

(66 reference statements)

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“…We thus examined the impact of TK disruption on transepithelial K + (J K ) and Na + (J Na ) fluxes and on transepithelial voltage (V te ) by using in vitro microperfusion of isolated CCDs. We and others have shown that CCDs do not exhibit any significant Na + or K + transport and do not generate a lumen-negative transepithelial voltage, when mice are fed a Na + -replete diet (17,18). Accordingly, CCDs isolated from TK +/+ mice neither reabsorbed sodium nor secreted potassium (Fig.…”

Section: Resultsmentioning

confidence: 73%

Tissue kallikrein permits early renal adaptation to potassium load

Moghrabi

Houillier

Picard

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Tissue kallikrein (TK) is a serine protease synthetized in renal tubular cells located upstream from the collecting duct where renal potassium balance is regulated. Because secretion of TK is promoted by K + intake, we hypothesized that this enzyme might regulate plasma K + concentration ([K + ]). We showed in wild-type mice that renal K + and TK excretion increase in parallel after a single meal, representing an acute K + load, whereas aldosterone secretion is not modified. Using aldosterone synthase-deficient mice, we confirmed that the control of TK secretion is aldosterone-independent. Mice with TK gene disruption ( TK −/− ) were used to assess the impact of the enzyme on plasma [K + ]. A single large feeding did not lead to any significant change in plasma [K + ] in TK +/+ , whereas TK −/− mice became hyperkalemic. We next examined the impact of TK disruption on K + transport in isolated cortical collecting ducts (CCDs) microperfused in vitro. We found that CCDs isolated from TK −/− mice exhibit net transepithelial K + absorption because of abnormal activation of the colonic H + ,K + -ATPase in the intercalated cells. Finally, in CCDs isolated from TK −/− mice and microperfused in vitro, the addition of TK to the perfusate but not to the peritubular bath caused a 70% inhibition of H + ,K + -ATPase activity. In conclusion, we have identified the serine protease TK as a unique kalliuretic factor that protects against hyperkalemia after a dietary K + load.

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Section: Resultsmentioning

confidence: 73%

Tissue kallikrein permits early renal adaptation to potassium load

Moghrabi

Houillier

Picard

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…126 The findings that the collecting duct is a key site of local RAS activity, where renin is produced in abundance by collecting duct principal cells 127 suggest an Ang-IIdependent activation of the collecting duct v-H + -ATPase and modulation of urinary acidification. 128,129 In agreement with these results, Advani et al 113 concluded that the (P)RR has a primary role in distal nephron proton transport, which at least in part, an Ang-II-dependent phenomenon.…”

Section: The Cross-talk: (P)rrs and Wnt/fz Signaling Systemmentioning

confidence: 70%

Potential cross-talk between (pro)renin receptors and Wnt/frizzled receptors in cardiovascular and renal disorders

Balakumar

Jagadeesh

2011

Hypertens Res

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The renin-angiotensin system and Wnt/frizzled receptor signaling pathways are important in the development of essential organs, and their aberrant activation results in cardiovascular and renal pathologies. The (pro)renin receptor ((P)RR)-bound (pro)renin is enzymatically active generating angiotensin-II and activating mitogen-activated protein kinases, leading to cell proliferation and to upregulation of profibrotic genes expression, resulting in end-organ damage. The (P)RR does more than bind to (pro)renin, because it is functionally linked to the vacuolar-H + -ATPase (v-H + -ATPase) that regulates pH of cellular and intracellular vesicles, and to Wnt signaling. This signaling pathway is essential for cell survival, embryonic development and has had a role in various disease states as evidenced by mutation or genetic ablation of the (P)RR gene. This suggests two types of functions of (P)RRs, first one as a receptor for (pro)renin and second one as an accessory subunit of the v-H + -ATPase and a cofactor of the Wnt/Fz receptor complex. This review will discuss both of these functions of (P)RRs thereby giving new perspectives as to the roles of (P)RRs in cardiovascular and renal pathologies.

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“…In intercalated cells of connecting tubules and cortical collecting ducts, ANG II stimulated H + -ATPase and may have contributed to the regulation of chloride reabsorption and bicarbonate secretion [110]. In the α intercalated cells of the mouse cortical collecting duct, ANG II stimulated the secretion of H + into the lumen, which drove Cl -reabsorption via apical Cl -/HCO 3-exchange and generated a more favorable electrochemical gradient for epithelial Na + channel (ENaC)-mediated Na + reabsorption [111]. ANG II stimulated ENaC in the rat cortical collecting duct via a Ca 2+ -independent PKC pathway that activated NADPH oxidase (NOX), resulting in an increase in superoxide generation.…”

Section: Distal Nephronmentioning

confidence: 99%

ANG II, ANG-(1-7), ALDO and AVP biphasic effects on Na+/H+ transport: the role of cellular calcium

Mello-Aires¹,

Dellova²,

Castelo‐Branco³

et al. 2017

Nephrol Renal Dis

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This article reviews the main body of knowledge regarding NHE1 and NHE3 exchangers and their interaction with Angiotensin II, Angiotensin-(1-7), Aldosterone and Arginine Vasopressin, particularly their renal actions. This work addresses the biphasic effects of different hormonal doses on NHE1 or NHE3 in proximal tubule in Wistar, SHR (hypertensives) and their control WKY (normotensives) rats or MDCK cells (which share similarities with the collecting duct). The hormones were applied alone, with their inhibitors or plus agents that change the [Ca 2+ ]i. The data are compatible with hormonal stimulation of these exchangers by increases of [Ca 2+ ]i in lower range, and inhibition at high [Ca 2+ ]i. In MDCK cells and Wistar rats, low doses of ANG II, ALDO or AVP stimulated the exchangers, while high doses inhibited them. ANG-(1-7), in Wistar or WKY rats has inverse, dose-dependent effects. In SHR rats, the biphasic effects of ANG-(1-7) were similar to the effects of ANG II, ALDO or AVP in Wistar rats. The interactions between these effects may represent a mechanism that regulates extracellular volume. In hypertensives animals, a high plasma level of ANG-(1-7) inhibited NHE3 in the proximal tubule, which mitigated hypertension. Figure 6 shows a schematic model to describe these biphasic hormonal effects.

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Angiotensin II Activates H+-ATPase in Type A Intercalated Cells

Abstract: We reported previously that angiotensin II (AngII)

Cited by 64 publications

References 43 publications

Tissue kallikrein permits early renal adaptation to potassium load

Tissue kallikrein permits early renal adaptation to potassium load

Potential cross-talk between (pro)renin receptors and Wnt/frizzled receptors in cardiovascular and renal disorders

ANG II, ANG-(1-7), ALDO and AVP biphasic effects on Na+/H+ transport: the role of cellular calcium

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