{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T15:41:58Z","timestamp":1791128518212,"version":"4.1.0"},"reference-count":44,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,10,12]],"date-time":"2004-10-12T00:00:00Z","timestamp":1097539200000},"content-version":"vor","delay-in-days":3725,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Glia"],"published-print":{"date-parts":[[1994,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Carbonic anhydrase activity was characterized in freshly dissociated M\u00fcller cells of the salamander retina. Intracellular pH was monitored using ratio imaging of the indicator dye BCECF as extracellular Pco<jats:sub>2<\/jats:sub> was varied. The extracellular solution was switched rapidly (141 ms rise time) from a HEPES buffered to a CO<jats:sub>2<\/jats:sub>\u2010HCO<jats:sup>\u2212<\/jats:sup><jats:sub>3<\/jats:sub> buffered solution (both pH 7.4). Introduction of CO<jats:sub>2<\/jats:sub>\u2010HCO<jats:sup>\u2212<\/jats:sup><jats:sub>3<\/jats:sub> produced a rapid cell acidification. Cell pH dropped from a steady\u2010state pH of 7.02 in HEPES solution to pH 6.81 in CO<jats:sub>2<\/jats:sub>\u2010HCO<jats:sup>\u2212<\/jats:sup><jats:sub>3<\/jats:sub>. Methazolamide, a carbonic anhydrase inhibitor, dramatically reduced the initial rate of acidification, demonstrating that the acidification was produced by the carbonic anhydrase\u2010catalyzed hydration of CO<jats:sub>2<\/jats:sub>. The initial rate of acidification, 52.6 pH units per min (0.88 pH units per s), was reduced \u223c 150\u2010fold to 0.36 pH units per min by 10<jats:sup>\u22123<\/jats:sup> M methazolamide. Half\u2010maximal inhibition occurred at a methazolamide concentration of 5.6. 10<jats:sup>\u22127<\/jats:sup> M. The carbonic anhydrase inhibitor acetazolamide (10<jats:sup>\u22123<\/jats:sup> M) also greatly reduced the rate of cell acidification. The latency to the onset of carbonic anhydrase inhibition was 660 ms for methazolamide and 7.5 s for acetazolamide. The carbonic anhydrase inhibitor benzolamide (10<jats:sup>\u22124<\/jats:sup> M, 4 min exposure), which is poorly membrane permeant, had little effect on the rate of cell acidification, indicating that the site of carbonic anhydrase action was intracellular. The activity of M\u00fcller cell carbonic anhydrase may help to buffer extracellular CO<jats:sub>2<\/jats:sub> variations in the retina. \u00a9 1994 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/glia.440110402","type":"journal-article","created":{"date-parts":[[2005,5,12]],"date-time":"2005-05-12T18:17:54Z","timestamp":1115921874000},"page":"291-299","source":"Crossref","is-referenced-by-count":38,"title":["A physiological measure of carbonic anhydrase in m\u00fcller cells"],"prefix":"10.1002","volume":"11","author":[{"given":"Eric A.","family":"Newman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,10,12]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/glia.440040506"},{"key":"e_1_2_1_3_1","first-page":"3068","article-title":"Intracellular pH regulation in fresh and cultured bovine corneal endothelium. II. 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