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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Giebisch, Gerhard Finberg, Karin E. Paunescu, Teodor G. Bailey, Matthew A. Breton, Sylvie Brown, Dennis Geibel, John P. Wagner, Carsten A. Lifton, Richard P. |
| Description | Author Affiliation: Finberg KE ( Departments of Genetics, Cellular and Molecular Physiology, Surgery, and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.); |
| Abstract | The multisubunit vacuolar-type H(+)ATPases mediate acidification of various intracellular organelles and in some tissues mediate H(+) secretion across the plasma membrane. Mutations in the B1-subunit of the apical H(+)ATPase that secretes protons in the distal nephron cause distal renal tubular acidosis in humans, a condition characterized by metabolic acidosis with an inappropriately alkaline urine. To examine the detailed cellular and organismal physiology resulting from this mutation, we have generated mice deficient in the B1-subunit (Atp6v1b1(-/-) mice). Urine pH is more alkaline and metabolic acidosis is more severe in Atp6v1b1(-/-) mice after oral acid challenge, demonstrating a failure of normal urinary acidification. In Atp6v1b1(-/-) mice, the normal urinary acidification induced by a lumen-negative potential in response to furosemide infusion is abolished. After an acute intracellular acidification, Na(+)-independent pH recovery rates of individual Atp6v1b1(-/-) intercalated cells of the cortical collecting duct are markedly reduced and show no further decrease after treatment with the selective H(+)ATPase inhibitor concanamycin. Apical expression of the alternative B-subunit isoform, B2, is increased in Atp6v1b1(-/-) medulla and colocalizes with the H(+)ATPase E-subunit; however, the greater severity of metabolic acidosis in Atp6v1b1(-/-) mice after oral acid challenge indicates that the B2-subunit cannot fully functionally compensate for the loss of B1. Our results indicate that the B1 isoform is the major B-subunit isoform that incorporates into functional, plasma membrane H(+)ATPases in intercalated cells of the cortical collecting duct and is required for maximal urinary acidification. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 38 |
| Volume Number | 102 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2005-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Acidosis, Renal Tubular Enzymology Acids Urine Cell Membrane Kidney Tubules, Collecting Vacuolar Proton-Translocating ATPases Metabolism Genetics Administration & Dosage Animals Hydrogen-Ion Concentration Kidney Medulla Mice Mice, Knockout Protein Subunits Protons Deficiency Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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