{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,12,15]],"date-time":"2022-12-15T14:28:36Z","timestamp":1671114516477},"reference-count":0,"publisher":"American Physiological Society","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Renal Physiology"],"published-print":{"date-parts":[[1992,2,1]]},"abstract":"<jats:p> We examined the effect of Cl- depletion metabolic alkalosis (CDA) on H(+)-ATPase and band 3 protein localization in intercalated cells (IC) of the rat cortical collecting duct (CCD) and the outer medullary collecting duct (OMCD). After 30 min of peritoneal dialysis against 0.15 M NaHCO3 to produce CDA, or Ringer bicarbonate to serve as controls (CON), both groups were infused intravenously with an 80 mM Cl- solution for 90 min. For CDA vs. CON, physiological parameters were as follows: plasma total CO2, 38.0 +\/- 1.1 vs. 27.8 +\/- 0.6 meq\/l (P less than 0.001); urinary total CO2 excretion, 141 +\/- 89 vs. 20 +\/- 3 neq.min-1.100 g body wt-1; and urinary Cl- excretion, 20 +\/- 10 vs. 486 +\/- 144 neq.min-1.100 g body wt-1 (P less than 0.001). H(+)-ATPase was localized in thin sections using a rabbit polyclonal antibody against the 70-kDa subunit of bovine brain H(+)-ATPase. Band 3 protein was localized using a polyclonal antibody against the 43-kDa subunit of the cytoplasmic domain of human erythrocyte band 3 protein. In CON rats, H(+)-ATPase localized along the apical plasma membrane and over the apical cytoplasmic vesicles of type A ICs in the CCD and ICs of the OMCD. H(+)-ATPase was observed along the basolateral plasma membrane and over cytoplasmic vesicles throughout type B ICs. In CDA rats, H(+)-ATPase was only observed over apical cytoplasmic vesicles in type A ICs and in the majority of OMCD ICs. In type B ICs, H(+)-ATPase staining was intensified along the basal plasma membrane in CDA. Band 3 protein was consistently localized in the basolateral plasma membrane of all type A cells in the CCD and ICs of the OMCD in both CON and CDA. In summary, stimulation of HCO3- secretion in rats caused withdrawal of H(+)-ATPase from the apical plasma membrane and storage in apical cytoplasmic vesicles of ICs of the OMCD and type A ICs of the CCD. H(+)-ATPase appeared to be inserted into the basal plasma membrane of type B ICs. These findings suggest that, during correction of CDA, proton secretion by type A and OMCD ICs is suppressed and proton transport across the basolateral plasma membrane of type B ICs is stimulated. <\/jats:p>","DOI":"10.1152\/ajprenal.1992.262.2.f309","type":"journal-article","created":{"date-parts":[[2017,12,23]],"date-time":"2017-12-23T09:15:07Z","timestamp":1514020507000},"page":"F309-F319","source":"Crossref","is-referenced-by-count":13,"title":["Response of intercalated cells to chloride depletion metabolic alkalosis"],"prefix":"10.1152","volume":"262","author":[{"given":"J. W.","family":"Verlander","sequence":"first","affiliation":[{"name":"Laboratory of Experimental Morphology, University of Florida, Gainesville 32610\u20130224."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K. M.","family":"Madsen","sequence":"additional","affiliation":[{"name":"Laboratory of Experimental Morphology, University of Florida, Gainesville 32610\u20130224."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. H.","family":"Galla","sequence":"additional","affiliation":[{"name":"Laboratory of Experimental Morphology, University of Florida, Gainesville 32610\u20130224."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. G.","family":"Luke","sequence":"additional","affiliation":[{"name":"Laboratory of Experimental Morphology, University of Florida, Gainesville 32610\u20130224."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C. C.","family":"Tisher","sequence":"additional","affiliation":[{"name":"Laboratory of Experimental Morphology, University of Florida, Gainesville 32610\u20130224."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Renal Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.physiology.org\/doi\/pdf\/10.1152\/ajprenal.1992.262.2.F309","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,8]],"date-time":"2019-09-08T20:18:32Z","timestamp":1567973912000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.physiology.org\/doi\/10.1152\/ajprenal.1992.262.2.F309"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,2,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1992,2,1]]}},"alternative-id":["10.1152\/ajprenal.1992.262.2.F309"],"URL":"https:\/\/doi.org\/10.1152\/ajprenal.1992.262.2.f309","relation":{},"ISSN":["1931-857X","1522-1466"],"issn-type":[{"value":"1931-857X","type":"print"},{"value":"1522-1466","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,2,1]]}}}