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  A Brush Border Membrane-Bound H+ -ATPase from the Dog Proximal Tubule

Noël, J., Laprade, R., Burckhardt, G., Gougoux, A., & Vinay, P. (1992). A Brush Border Membrane-Bound H+ -ATPase from the Dog Proximal Tubule. Cellular Physiology and Biochemistry, 2(1), 18-36. doi:10.1159/000154623.

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Genre: Journal Article

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 Creators:
Noël, J.1, Author
Laprade, R.1, Author
Burckhardt, Gerhard2, Author              
Gougoux, A.1, 3, Author
Vinay, P.1, 3, Author
Affiliations:
1Groupe de Recherche en Transport Membranaire Départements de Médecine et Physiologie, ou_persistent22              
2Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              
3Hôpital Notre-Dame de Montréal, Université de Montréal, Montréal Québec, Canada, ou_persistent22              

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Free keywords: H+ secretion; Acridine orange; Oxygen consumption; Rabbit; Ecto-ATPase
 Abstract: We have characterized the H+-ATPase activity (ATP hydrolysis and proton transport) of brush border membranes (BBMs) isolated from the dog kidney cortex. In solubilized BBMs, two thirds of total ATPase activity is insensitive to 10–3 M ouabain and 10–5M oligomycin, but sensitive to 10–6M NN’-dicyclohexylcarbodiimide (DCCD), N-ethyl-maleimide (NEM) and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole. The NEM- and DCCD-sensitive ATPase activity is not affected by 2–20 mM potassium, 10–3M omeprazole or 10–3M vanadate. A comparable enrichment was observed in solubilized BBMs for this ATPase activity and BBM enzyme markers. The NEM-sensitive ATPase activity of intact BBMs is increased 6.6-fold upon solubilization with 0.1 % deoxycholate, indicating the localization of most of the ATP-binding sites inside the native vesicles. Addition of ATP to BBM vesicles resulted in a large intravesicular acidification (acridine orange) only in vesicles pretreated with cholate which reverses the polarity of the H+ pump. Both proton transport and H+-ATPase activity were optimal around pH 7.0–7.5, and presented a comparable sensitivity to inhibitors. In intact dog cortical tubules, the large ouabain-insensitive but oligomycin-sensitive respiration suggests that this pump may represent a major energy-consuming process. In contrast, rabbit cortical tubules present a lower H+-ATPase activity and specific respiration. We therefore propose that an ATP-driven H+ transport may contribute significantly to H+ secretion in dog proximal tubules.

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Language(s): eng - English
 Dates: 1991-09-231991-10-102008-09-041992
 Publication Status: Published in print
 Pages: 19
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1159/000154623
 Degree: -

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Title: Cellular Physiology and Biochemistry
Source Genre: Journal
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Publ. Info: Basel : S. Karger
Pages: - Volume / Issue: 2 (1) Sequence Number: - Start / End Page: 18 - 36 Identifier: ISSN: 1015-8987
CoNE: https://pure.mpg.de/cone/journals/resource/954925585261