Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P41181 (collecting duct)
 5,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Response of intercalated cells to chloride depletion metabolic alkalosis. 153 35

Band 3 protein is the major anion transport protein of the erythrocyte cell membrane where it catalyzes the exchange of HCO3- for Cl-. There is evidence that band 3 protein is present in the collecting duct of both the rat and rabbit kidney. We used colloidal-gold immunocytochemistry to determine the ultrastructural location of band 3 protein in the rat cortical (CCD) and outer medullary collecting ducts (OMCD). Kidneys of normal Sprague-Dawley rats were fixed by intravascular perfusion with 1% glutaraldehyde and embedded in Lowicryl K4M. Two polyclonal antibodies raised in rabbits were used as the primary antibody in separate experiments, one against the 43-kDa fragment of the cytoplasmic domain of human erythrocyte band 3 protein and the other against rat erythrocyte band 3 protein. This was followed by exposure to gold-conjugated goat anti-rabbit immunoglobulin G. Transmission electron microscopy revealed gold particles along the basal and lateral plasma membranes of all intercalated cells of the OMCD. In the CCD, the basal and lateral plasma membranes of the type A intercalated cells only were labeled with gold particles. The type B intercalated cells and principal cells were devoid of gold particles, as were all cells of the proximal tubule, the distal convoluted tubule, and the thick ascending limb of the loop of Henle. We conclude that a Cl(-)-HCO3- transporter is present in the basal and lateral plasma membranes of the intercalated cells in the OMCD and the type A intercalated cells in the CCD. These findings provide further evidence that these intercalated cells are involved in H+ secretion in the OMCD and CCD of the rat. We have no evidence for the presence of band 3 protein in the type B intercalated cells of the CCD, which supports the hypothesis that type B cells are functionally and structurally distinct from type A cells.
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PMID:Immunocytochemical localization of band 3 protein in the rat collecting duct. 339 6

Band 3 protein is an anion-exchange protein that in the human kidney is restricted to a subpopulation of collecting duct-intercalated cells; however, it is absent in the metanephric-derived cells of the nephron. We have studied band 3 protein expression in a series of 60 renal tumors that included 10 oncocytomas, 42 renal cell carcinomas, and eight nephroblastomas by using frozen tumors and a monoclonal antibody. We detected band 3 protein expression in nine of 10 oncocytomas but not in any renal cell carcinomas or nephroblastomas. This finding confirms that band 3 protein is a specific marker for oncocytoma and therefore may have a potential diagnostic application. It also supports the contention that renal cell carcinoma and oncocytoma are histogenically unrelated; the former is metanephric blastema derived and the latter is ampullary bud derived.
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PMID:Immunocytochemical analysis of band 3 protein in renal cell carcinoma, nephroblastoma, and oncocytoma. 802 3

Structurally and functionally distinct populations of intercalated cells have been described in the collecting duct of both rat and rabbit. However, little is known about these cells in the mouse kidney. The study presented here examines ultrastructural and immunological characteristics of different types of intercalated cells in the mouse. Kidneys of two strains of normal female mice, C57BL/6 and IBR, were preserved by in vivo perfusion with 1% glutaraldehyde or paraformaldehyde-picric acid fixatives and processed for morphological evaluation or light and electron microscopic immunohistochemistry, respectively. The avidin-biotin-horseradish peroxidase procedure was performed on was sections using antibodies against carbonic anhydrase II, H+ -ATPase and Band 3 protein. Immunogold cytochemistry was performed on Lowicryl sections using antibodies to H+ -ATPase and Band 3 protein. Colocalization of H+ -ATPase and Band 3 protein was performed by double labeling using an immunogold technique with silver enhancement. Intercalated cells identified by positive staining for H+ -ATPase and carbonic anhydrase II constituted 35% to 40% of all cells in the connecting tubule (CNT), cortical collecting duct (CCD), and outer medullary collecting duct (OMCD). Type A intercalated cells identified by positive Band 3 staining constituted 16%, 24%, and 33% of the total cell population in the CNT, CCD, and OMCD, respectively. Electron microscopy and immunogold cytochemistry demonstrated three distinct populations of intercalated cells. Type A intercalated cells with apical H+ -ATPase and basolateral Band 3 immunoreactivity were present in all segments examined, and had prominent apical microprojections and characteristic tubulovesicular structures beneath the apical surface, both coated with studs on the cytoplasmic face. Type B intercalated cells with basolateral and cytoplasmic H+-ATPase and no Band 3 immunoreactivity were most frequently observed in the initial collecting tubule, but were present also in the CNT and early CCD. Type B intercalated cells had a fairly smooth apical surface, a gray zone free of organelles beneath the apical plasma membrane, and small cytoplasmic vesicles without studs throughout the cell. A third type of intercalated cell with apical and cytoplasmic H+-ATPase, but no basolateral Band 3 protein, was observed exclusively in the CNT and the initial collecting tubule. This type of cell was large, with numerous mitochondria, and vesicles coated with studs were present throughout the cell. It resembled a third type of intercalated cell described previously in the rat. It is concluded that three morphologically and immunologically distinct types of intercalated cells are present in the mouse kidney.
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PMID:Identification of distinct subpopulations of intercalated cells in the mouse collecting duct. 878 96