{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:04:22Z","timestamp":1791295462724,"version":"4.1.0"},"reference-count":39,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"5","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["Hypertension"],"published-print":{"date-parts":[[2000,5]]},"abstract":"<jats:p>\n            <jats:italic>Abstract<\/jats:italic>\n            \u2014The aim of the  present study was to demonstrate rapid effects of  aldosterone on the Na\n            <jats:sup>+<\/jats:sup>\n            -H\n            <jats:sup>+<\/jats:sup>\n            exchanger  in strips of human vascular vessels and to determine whether  11\u03b2-hydroxysteroid dehydrogenase enzyme (11\u03b2-HSD) could play a  protective role in this response, such as that described for the  classic type I mineralocorticoid receptor (MR). The activity of  11\u03b2-HSD isoforms 1 and 2 were measured in fetal and adult arteries.  Both isoforms are present in adult and fetal vessels. However, a  significant difference in the proportion of each isoform was found.  Isoform 1 activity (in pmol \u00b7 min\n            <jats:sup>\u22121<\/jats:sup>\n            \u00b7 100  mg\n            <jats:sup>\u22121<\/jats:sup>\n            protein) was 42\u00b15 in fetal vessels and 29\u00b12 in  adult arteries, and isoform 2 activity was 78\u00b17 in fetal and 12\u00b12 in  adult tissue. The nongenomic effect of aldosterone on  Na\n            <jats:sup>+<\/jats:sup>\n            -H\n            <jats:sup>+<\/jats:sup>\n            exchanger activity was measured in  strips of chorionic and radial uterine arteries loaded with the  pH-sensitive dye  2\u2032,7\u2032-bis(2-carboxyethyl)-5,6-carboxyfluorescein.  Recordings of intracellular pH (pH\n            <jats:sub>i<\/jats:sub>\n            ) were made by  videofluorescence microscopy. Aldosterone (0.5  nmol\/L) rapidly increased pH\n            <jats:sub>i<\/jats:sub>\n            , with a half-maximal effect  between 2 and 3 nmol\/L in both fetal and adult vessels.  Ethylisopropylamiloride, a specific inhibitor of the  Na\n            <jats:sup>+<\/jats:sup>\n            -H\n            <jats:sup>+<\/jats:sup>\n            exchanger, inhibited this effect. The  hormone-mediated increase in pH\n            <jats:sub>i<\/jats:sub>\n            was unaffected by  spironolactone, a classic antagonist of MR, but was  completely blocked by RU28318. Cortisol (up to 1 \u03bcmol\/L) had no  effect on pH\n            <jats:sub>i<\/jats:sub>\n            , but when applied in the presence of  carbenoxolone, a dramatic increase in Na\n            <jats:sup>+<\/jats:sup>\n            -H\n            <jats:sup>+<\/jats:sup>\n            exchanger activity was evident. The increments on pH\n            <jats:sub>i<\/jats:sub>\n            for  each cortisol concentration were similar to those observed for  aldosterone. These findings suggest that vascular 11\u03b2-HSD  plays an active role in maintaining the specificity of the rapid  effects of aldosterone.\n          <\/jats:p>","DOI":"10.1161\/01.hyp.35.5.1099","type":"journal-article","created":{"date-parts":[[2012,6,12]],"date-time":"2012-06-12T00:25:31Z","timestamp":1339460731000},"page":"1099-1104","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":134,"title":["Role of 11\u03b2-Hydroxysteroid Dehydrogenase in Nongenomic Aldosterone Effects in Human Arteries"],"prefix":"10.1161","volume":"35","author":[{"given":"Rodrigo","family":"Alzamora","sequence":"first","affiliation":[{"name":"From the Laboratory of Cellular and Molecular Physiology, Faculty of  Medicine, University of Los Andes, Las Condes, Santiago, Chile."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis","family":"Michea","sequence":"additional","affiliation":[{"name":"From the Laboratory of Cellular and Molecular Physiology, Faculty of  Medicine, University of Los Andes, Las Condes, Santiago, Chile."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisa T.","family":"Marusic","sequence":"additional","affiliation":[{"name":"From the Laboratory of Cellular and Molecular Physiology, Faculty of  Medicine, University of Los Andes, Las Condes, Santiago, Chile."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.hyp.10.6.608"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.hyp.11.2.174"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2845584"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0039-128X(96)00033-5"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0922-4106(93)90072-H"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1161\/hyp.32.6.1077"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1161\/hyp.33.6.1369"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1042\/cs0850257"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1210\/edrv.18.1.0288"},{"key":"e_1_3_2_10_2","first-page":"207","volume":"60","year":"1997","unstructured":"Brem AS, Bina RB, Hill N, Alia C, Morris DJ. 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