Long-term regulation of vacuolar H+-ATPase by angiotensin II in proximal tubule cells

Carraro‐Lacroix, Luciene Regina; Girardi, Adriana C. C.; Malnic, Gerhard

doi:10.1007/s00424-009-0668-9

Cited by 19 publications

(6 citation statements)

References 42 publications

(61 reference statements)

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“…The renin- and/or Ang II-dependent activation of MAP kinases ERK1/2 appears to have been well established. Ang II also appears to stimulate V-ATPase activity in rat proximal tubule cells via mechanisms involving tyrosine kinase, p38 MAPK, and PI3K [31]. Since PRR is structurally identical to CAPER protein (endoplasmic reticulum-localized type 1 transmembrane adaptor precursor) and vacuolar H + -ATPase (V-ATPase), intracellular PRR may also mediate the intracellular actions of prorenin or renin [1,57,198].…”

Section: Overview Of the Prorenin/prr/map Kinases Erk 1/2 Axis In mentioning

confidence: 99%

New insights and perspectives on intrarenal renin-angiotensin system: Focus on intracrine/intracellular angiotensin II

2011

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Although renin, the rate-limiting enzyme of the renin-angiotensin system (RAS), was first discovered by Robert Tigerstedt and Bergman more than a century ago, the research on the RAS still remains stronger than ever. The RAS, once considered to be an endocrine system, is now widely recognized as dual (circulating and local/tissue) or multiple hormonal systems (endocrine, paracrine and intracrine). In addition to the classical renin/angiotensin I-converting enzyme (ACE)/angiotensin II (Ang II)/Ang II receptor (AT1/AT2) axis, the prorenin/(Pro)renin receptor (PRR)/MAP kinase axis, the ACE2/Ang (1-7)/Mas receptor axis, and the Ang IV/AT4/insulin-regulated aminopeptidase (IRAP) axis have recently been discovered. Furthermore, the roles of the evolving RAS have been extended far beyond blood pressure control, aldosterone synthesis, and body fluid and electrolyte homeostasis. Indeed, novel actions and underlying signaling mechanisms for each member of the RAS in physiology and diseases are continuously uncovered. However, many challenges still remain in the RAS research field despite of more than one century's research effort. It is expected that the research on the expanded RAS will continue to play a prominent role in cardiovascular, renal and hypertension research. The purpose of this article is to review the progress recently being made in the RAS research, with special emphasis on the local RAS in the kidney and the newly discovered prorenin/PRR/MAP kinase axis, the ACE2/Ang (1-7)/Mas receptor axis, the Ang IV/AT4/IRAP axis, and intracrine/intracellular Ang II. The improved knowledge of the expanded RAS will help us better understand how the classical renin/ACE/Ang II/AT1 receptor axis, extracellular and/or intracellular origin, interacts with other novel RAS axes to regulate blood pressure and cardiovascular and kidney function in both physiological and diseased states.

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Section: Overview Of the Prorenin/prr/map Kinases Erk 1/2 Axis In mentioning

confidence: 99%

New insights and perspectives on intrarenal renin-angiotensin system: Focus on intracrine/intracellular angiotensin II

2011

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“…The B2 subunit is ubiquitously expressed, and it may be responsible for the translocation of V-ATPase from the cytosol to the membrane. Carraro-Lacroix et al demonstrated that immortalized rat proximal tubular cells exposed to angiontensin II exhibited an upregulation of V-ATPase activity that was partially caused by increased B2 cell surface expression; the B2 subunit contains an F-actin binding site, which interacts with actin filaments and allows trafficking to the cell surface 27 . The B2 subunit was upregulated in V-ATPase B1 subunit-deficient mice to compensate for the lack of B1, which was sufficient to maintain basal acid-base homeostasis, despite the downregulation of other V-ATPase subunits in the animal model 28 .…”

Section: Discussionmentioning

confidence: 99%

Interaction between V-ATPase B2 and (Pro) renin Receptors in Promoting the progression of Renal Tubulointerstitial Fibrosis

Liu

Zuo

et al. 2016

Sci Rep

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To investigate the levels of (Pro) renin receptor [(P) RR], α-smooth muscle actin (α-SMA), fibronectin (FN), and vacuolar H+-ATPase (V-ATPase) subunits (B2, E, and c) in rat unilateral ureteral obstruction (UUO) models and rat proximal tubular epithelial cells (NRK-52E) treated with prorenin to elucidate the role of V-ATPase in these processes by activating the (P) RR. UUO significantly upregulated (P) RR, V-ATPase subunits, α-SMA and FN expression in tubulointerstitium or tubular epithelial cells. A marked colocalization of (P) RR and the B2 subunit was also observed. Prorenin treatment upregulated α-SMA, FN, (P) RR, and V-ATPase subunits and activity in NRK52E cell in a dose- and time-dependent manner. The V-ATPase inhibitor bafilomycin A1 partially blocked prorenin-induced (P) RR, FN, and α-SMA expression. Co-immunoprecipitate and immunofluorescence results demonstrated that the V-ATPase B2 subunit bound to the (P) RR, which was upregulated after prorenin stimulation. Either siRNA-mediated (P) RR or B2 subunit knockdown partially reduced V-ATPase activity and attenuated prorenin-induced FN and α-SMA expression. From the data we can assume that activation of (P) RR and V-ATPase may play an important role in tubulointerstitial fibrosis with possible involvement of interaction of V-ATPase B2 subunit and (P)RR.

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“…In the in vitro perfused rabbit proximal tubule, the mechanism of the stimulation involved both apical Na + /H + exchange and basolateral Na + -base transport (236). Angiotensin II increased the Vmax of apical Na + /H + exchange and at higher concentrations also increased H + -ATPase activity in a proximal tubule OKP cell line by enhancing plasma membrane expression involving signaling through tyrosine kinase, PI3K, and P38 (140, 603). Angiotensin II has also been reported to increase apical H + -ATPase membrane vesicle insertion in rat proximal tubule fragments (727).…”

Section: Regulation Of Proximal Tubule H+/base Transporters and Wholementioning

confidence: 97%

Molecular Mechanisms and Regulation of Urinary Acidification

Kurtz

2014

Comprehensive Physiology

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The H+ concentration in human blood is kept within very narrow limits, ~ 40 nM, despite the fact that dietary metabolism generates acid and base loads that are added to the systemic circulation throughout the life of mammals. One of the primary functions of the kidney is to maintain the constancy of systemic acid-base chemistry. The kidney has evolved the capacity to regulate blood acidity by performing three key functions: 1) reabsorb HCO3− that is filtered through the glomeruli to prevent its excretion in the urine; 2) generate a sufficient quantity of new HCO3− to compensate for the loss of HCO3− resulting from dietary metabolic H+ loads and loss of HCO3− in the urea cycle; and 3) excrete HCO3− (or metabolizable organic anions) following a systemic base load. The ability of the kidney to perform these functions requires that various cell types throughout the nephron respond to changes in acid-base chemistry by modulating specific ion transport and/or metabolic processes in a coordinated fashion such that the urine and renal vein chemistry is altered appropriately. The purpose of the article is to provide the interested reader with a broad review of a field that began historically ~ 60 years ago with whole animal studies, and has evolved to where we are currently addressing questions related to kidney acid-base regulation at the single protein structure/function level.

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Long-term regulation of vacuolar H+-ATPase by angiotensin II in proximal tubule cells

Cited by 19 publications

References 42 publications

New insights and perspectives on intrarenal renin-angiotensin system: Focus on intracrine/intracellular angiotensin II

New insights and perspectives on intrarenal renin-angiotensin system: Focus on intracrine/intracellular angiotensin II

Interaction between V-ATPase B2 and (Pro) renin Receptors in Promoting the progression of Renal Tubulointerstitial Fibrosis

Molecular Mechanisms and Regulation of Urinary Acidification

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