Vacuolar‐type H<sup>+</sup>‐ATPase in mouse bladder epithelium is responsible for urinary acidification

Tomochika, Ken Ichi; Shinoda, Sumió; Kumon, Hiromi; Mori, Masaharu; Moriyama, Yoshinori; Futai, Masamitsu

doi:10.1016/s0014-5793(97)00090-2

Cited by 16 publications

(9 citation statements)

References 25 publications

(22 reference statements)

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“…Five minutes after application of foliomycin, the REC pH i was effectively reduced by 0.19 Ϯ 0.03 pH units. This pH i change is in the order (Ϫ0.08 to Ϫ0.26 pH units) of results from other authors who studied nonpigmented ciliary epithelium, mouse bladder epithelium, and macrophages by use of specific vH ϩ -ATPase inhibitors (21,23,34,43). In part of the experiments, a time-dependent attenuation of the foliomycininduced pH i decrease occurred, leading to a stronger variability of the foliomycin effect (Ϫ0.18 Ϯ 0.07 pH units) observed at the end of the measuring period.…”

Section: Fig 8 Products From Rt-pcr Experiments To Detect Vhsupporting

confidence: 62%

A vH⁺-ATPase is present in cultured sheep ruminal epithelial cells

Etschmann¹,

Heipertz²,

Schulenburg³

et al. 2006

American Journal of Physiology-Gastrointestinal and Liver Physi

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Section: Fig 8 Products From Rt-pcr Experiments To Detect Vhsupporting

confidence: 62%

A vH⁺-ATPase is present in cultured sheep ruminal epithelial cells

Etschmann¹,

Heipertz²,

Schulenburg³

et al. 2006

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…These antibodies cross-reacted with the corresponding subunits of plants and animal origin. The specificity of the antibodies was extensively characterized previously (31)(32)(33)(34).…”

Section: Methodsmentioning

confidence: 99%

Vacuolar H+-ATPase Localized in Plasma Membranes of Malaria Parasite Cells, Plasmodium falciparum, Is Involved in Regional Acidification of Parasitized Erythrocytes

Hayashi

Yamada

Mitamura

et al. 2000

Journal of Biological Chemistry

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111

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“…The organellar acidic pH generated by V-ATPase is responsible for various processes including zymogen activation, receptor-mediated endocytosis, macromolecule degradation, and protein sorting. The enzyme is also found in plasma membranes, where it transports protons outside cells such as osteoclasts (6,7), renal-intercalated cells (8), and epithelial cells of the seminal duct and bladder (9,10).…”

Section: A Ubiquitous Vacuolar-type Hmentioning

confidence: 99%

a4, a Unique Kidney-specific Isoform of Mouse Vacuolar H+-ATPase Subunit a

Oka¹,

Murata²,

Namba³

et al. 2001

Journal of Biological Chemistry

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125

136

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The vacuolar-type H؉ -ATPase (V-ATPase) translocates protons across membranes. Here, we have identified a mouse cDNA coding for a fourth isoform (a4) of the membrane sector subunit a of V-ATPase. This isoform was specifically expressed in kidney, but not in the heart, brain, spleen, lung, liver, muscle, or testis. Immunoprecipitation experiments, together with sequence similarities for other isoforms (a1, a2, and a3), indicate that the a4 isoform is a component of V-ATPase. Moreover, histochemical studies show that a4 is localized in the apical and basolateral plasma membranes of cortical ␣-and ␤-intercalated cells, respectively. These results suggest that the V-ATPase, with the a4 isoform, is important for renal acid/base homeostasis. A ubiquitous vacuolar-type Hϩ -ATPase (V-ATPase) 1 translocates protons across membranes utilizing the energy of ATP hydrolysis (for reviews, see Refs. 1-5). The organellar acidic pH generated by V-ATPase is responsible for various processes including zymogen activation, receptor-mediated endocytosis, macromolecule degradation, and protein sorting. The enzyme is also found in plasma membranes, where it transports protons outside cells such as osteoclasts (6, 7), renal-intercalated cells (8), and epithelial cells of the seminal duct and bladder (9, 10).V-ATPase has a membrane peripheral V 1 sector for ATP hydrolysis and an integral V o for proton translocation (1-5). The V o sector consists of at least five subunits (a, c, cЈ, cЉ, and d) (11). Subunit a is the largest (116 kDa) of the V-ATPase subunits, and its isoforms have been found in yeast (12), chicken (13), mouse (7, 14, 15), cow (16, 17), and human (18). These isoforms exhibit different distributions in organelles and tissues. Yeast isoforms (Vph1p and Stv1p) are localized in vacuoles and Golgi/endosomes, respectively (12). Three isoforms (a1, a2, and a3) have been found previously in mammals (7, 14 -18). These isoforms may be important for the localization of V-ATPase in various organelles or plasma membranes.In this study, we have isolated a mouse cDNA coding for a fourth isoform (a4) of V-ATPase subunit a. Isoform a4 exhibits high similarities with the a1, a2, and a3 isoforms and is expressed exclusively in kidney. Furthermore, a4 was localized immunochemically in the apical and basolateral plasma membranes of cortical ␣-and ␤-intercalated cells, respectively. These results suggest that the V-ATPase with the a4 isoform is a kidney-specific proton pump important for acid/base homeostasis.

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Vacuolar‐type H⁺‐ATPase in mouse bladder epithelium is responsible for urinary acidification

Abstract: The urine in the mouse bladder was found to be acidic, ranging from pH 5.3 to 5.5 in the daytime and pH 6.0 to 6.

Cited by 16 publications

References 25 publications

A vH⁺-ATPase is present in cultured sheep ruminal epithelial cells

A vH⁺-ATPase is present in cultured sheep ruminal epithelial cells

Vacuolar H+-ATPase Localized in Plasma Membranes of Malaria Parasite Cells, Plasmodium falciparum, Is Involved in Regional Acidification of Parasitized Erythrocytes

a4, a Unique Kidney-specific Isoform of Mouse Vacuolar H+-ATPase Subunit a

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Vacuolar‐type H+‐ATPase in mouse bladder epithelium is responsible for urinary acidification

Abstract: The urine in the mouse bladder was found to be acidic, ranging from pH 5.3 to 5.5 in the daytime and pH 6.0 to 6.

Cited by 16 publications

References 25 publications

A vH+-ATPase is present in cultured sheep ruminal epithelial cells

A vH+-ATPase is present in cultured sheep ruminal epithelial cells

Vacuolar H+-ATPase Localized in Plasma Membranes of Malaria Parasite Cells, Plasmodium falciparum, Is Involved in Regional Acidification of Parasitized Erythrocytes

a4, a Unique Kidney-specific Isoform of Mouse Vacuolar H+-ATPase Subunit a

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Vacuolar‐type H⁺‐ATPase in mouse bladder epithelium is responsible for urinary acidification

A vH⁺-ATPase is present in cultured sheep ruminal epithelial cells

A vH⁺-ATPase is present in cultured sheep ruminal epithelial cells