Journal of Biological Chemistry
Membrane Transport, Structure, Function, and BiogenesisPutative Re-entrant Loop 1 of AE2 Transmembrane Domain Has a Major Role in Acute Regulation of Anion Exchange by pH*
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The abbreviations used are: pHi, intracellular pH; pHo, extracellular pH; TMD, transmembrane domain; aa, amino acid(s); MES, 4-morpholineethanesulfonic acid; MTSEA, (2-aminoethyl) methanethiosulfonate; MTSET, (2-(trimethylammonium)-ethyl) methanethiosulfonate; MTSES, (2-(trimethylammonium)-ethyl) methanethiosulfonate; PBS, phosphate-buffered saline; BSA, bovine serum albumin; HA, hemagglutinin; GFP, green fluorescent protein; FI, fluorescence intensity; DIDS, 4,4′-di-isothiocyanatostilbene-2,2′ disulfonic acid; WT, wild type; MTS, methanethiosulfonate.
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An alternative method normalized each rate constant to that individual oocyte's rate constant measured at pHo 8.5, which was given a value of 100%. The normalized rate constants at every pHo value were fit with Equation 1. Data calculated by this approach yielded pHo(50) values not significantly different in most cases from those presented. However, application of this alternative method to Equation 1 yielded poor fits (r2 as low as 0.6) for some AE2 mutants.
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A. K. Stewart, P. Papageorgiou, and S. L. Alper, unpublished observations.
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This work was supported, in whole or in part, by National Institutes of Health Grants DK43495 (to S. L. A.) and RR017927 (Shared Instrument Grant) to Beth Israel Deaconess Medical Center. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1–4.
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Supported by a postdoctoral fellowship award from the National Kidney Foundation.