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Am J Physiol Cell Physiol 282: C1454-C1460, 2002; doi:10.1152/ajpcell.00319.2001
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Vol. 282, Issue 6, C1454-C1460, June 2002

V-type H+-ATPase in the human eccrine sweat duct: immunolocalization and functional demonstration

D. Granger1, M. Marsolais1, J. Burry2, and R. Laprade1

1 Groupe de Recherche en Transport Membranaire, Université de Montréal, Montreal, Quebec, Canada H3C 3J7; and 2 Unilever Research, Port Sunlight, UK CH63 3JW

We investigated for the presence of a vacuolar-type H+-ATPase (V-ATPase) in the human eccrine sweat duct (SD). With the use of immunocytochemistry, an anti-V- ATPase antibody showed a strong staining at the apical membrane and a weaker one in the cytoplasm. Cold preservation followed by rewarming did not alter this staining pattern. With the use of the pH-sensitive dye 2',7'-bis(2-carboxyethyl)-5(6)-carboxyfluorescein on isolated and perfused straight SD under HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>-free conditions and in the absence of Na+, proton extrusion was determined from the recovery rate of intracellular pH (dpHi/dt) following an acid load. Oligomycin (25 µM), an inhibitor of F-type ATPases, decreased dpHi/dt by 88 ± 6%, suggesting a role for an ATP-dependent process involved in pHi recovery. Moreover, dpHi/dt was inhibited at 95 ± 3% by 100 nM luminal concanamycin A, a specific inhibitor of V-ATPases, whereas 10 µM bafilomycin A1, another specific inhibitor of V-ATPases, was required to decrease dpHi/dt by 73%. These results strongly suggest that a V-ATPase is involved in proton secretion in the human eccrine SD.

proton pump; intracellular pH measurement; concanamycin A; bafilomycin A1; oligomycin


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