Luminal flow modulates H<sup>+</sup>-ATPase activity in the cortical collecting duct (CCD)

Li, Wen; Pastor-Soler, Núria M.; Schreck, Carlos; Zavilowitz, Beth; Kleyman, Thomas R.; Satlin, Lisa M.

doi:10.1152/ajprenal.00179.2011

Cited by 15 publications

(10 citation statements)

References 82 publications

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“…Statistics were then performed on n ϭ 5 mice/group. For images of ENaC-␤, freshly harvested kidneys were cut into 5-mm slices, fixed using 4% paraformaldehyde, and processed as previously described (23,37). Tissues were embedded in Tissue Tek OCT (Sakura, Torrance, CA).…”

Section: Methodsmentioning

confidence: 99%

AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1

Fraser

Choy

Pastor-Soler

et al. 2013

American Journal of Physiology-Renal Physiology

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Salt reabsorption is the major energy-requiring process in the kidney, and AMP-activated protein kinase (AMPK) is an important regulator of cellular metabolism. Mice with targeted deletion of the β1-subunit of AMPK (AMPK-β1(-/-) mice) had significantly increased urinary Na(+) excretion on a normal salt diet. This was associated with reduced expression of the β-subunit of the epithelial Na(+) channel (ENaC) and increased subapical tubular expression of kidney-specific Na(+)-K(+)-2Cl(-) cotransporter 2 (NKCC2) in the medullary thick ascending limb of Henle. AMPK-β1(-/-) mice fed a salt-deficient diet were able to conserve Na(+), but renin secretion increased 180% compared with control mice. Cyclooxygenase-2 mRNA also increased in the kidney cortex, indicating greater signaling through the macula densa tubular salt-sensing pathway. To determine whether the increase in renin secretion was due to a change in regulation of fatty acid metabolism by AMPK, mice with a mutation of the inhibitory AMPK phosphosite in acetyl-CoA carboxylase 1 [ACC1-knockin (KI)(S79A) mice] were examined. ACC1-KI(S79A) mice on a normal salt diet had no increase in salt loss or renin secretion, and expression of NKCC2, Na(+)-Cl(-) cotransporter, and ENaC-β were similar to those in control mice. When mice were placed on a salt-deficient diet, however, renin secretion and cortical expression of cyclooxygenase-2 mRNA increased significantly in ACC1-KI(S79A) mice compared with control mice. In summary, our data suggest that renin synthesis and secretion are regulated by AMPK and coupled to metabolism by phosphorylation of ACC1.

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Section: Methodsmentioning

confidence: 99%

AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1

Fraser

Choy

Pastor-Soler

et al. 2013

American Journal of Physiology-Renal Physiology

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“…BCECF-loaded cells in the OMCDs were visualized under epifluorescence illumination using a ϫ40 water-immersion objective (Nikon S Fluor 40; numeric aperture 0.9, working distance 0.3) (9,27). OMCDs were alternately excited at 490 and 440 nm using a wavelength switcher (DG-4 or LAMBDA 10 -2; Sutter).…”

Section: Microperfusion Of Isolated Rabbit Tubules and Measurement Ofmentioning

confidence: 99%

AMP-activated protein kinase regulates the vacuolar H⁺-ATPase via direct phosphorylation of the A subunit (ATP6V1A) in the kidney

Alzamora

Al‐bataineh

Liu

et al. 2013

American Journal of Physiology-Renal Physiology

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(28 -30, 49). We have demonstrated that in kidney intercalated cells and in epididymal clear cells, which share a common developmental origin in the Wolffian duct, the V-ATPase redistributes from the apical membrane to the cytosol with stimulation of the metabolic sensor AMPK (16,18). In our previous studies we first identified the V-ATPase A subunit as an AMPK substrate using the unbiased "MudSeeK" proteomic screening method and subsequently showed that the V-ATPase A subunit is phosphorylated directly by AMPK in kidney cells (18,52). AMPK is an important cell energy-sensing kinase that has been shown to downregulate several kidney membrane transport proteins (17,39). We have shown that AMPK reduces apical V-ATPase accumulation acutely in kidney intercalated cells, and that AMPK activation antagonizes the ability of PKA to increase V-ATPase localization at the apical pole of type A intercalated cells (16).Phosphatidylinositol 3-kinase and PKA are additional kinases that regulate the function of the V-ATPase in the mammalian kidney (16,41,43). PKA agonists also regulate the V-ATPase in other animal models (42, 54). However, it was not until recently that work by our group linked the direct phosphorylation of the V-ATPase by PKA at Ser-175 to increases in V-ATPase plasma membrane activity in mammalian cells (2). Ser-175 A subunit phosphorylation is likely to occur downstream of acid-base-sensing pathways, which require the presence of active carbonic anhydrase, the soluble

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“…Although neonates with loss of function ROMK mutations may exhibit early hyperkalemia (10), this likely reflects a delay in BK channel expression in the immediate postnatal period. Finally, identification of a luminal H + -ATPase in principal cells, although modest compared with intercalated cell H + -ATPase, raises the possibility that these cells may contribute to renal H + secretion (11).…”

Section: Challenging Traditionmentioning

confidence: 99%