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Your search keyword '"Lifton, Richard P"' showing total 10 results
Start Over Author "Lifton, Richard P" Journal kidney international
10 results on '"Lifton, Richard P"'

1. Whole exome sequencing identified ATP6V1C2 as a novel candidate gene for recessive distal renal tubular acidosis

Author

Jobst-Schwan, Tilman, primary, Klämbt, Verena, additional, Tarsio, Maureen, additional, Heneghan, John F., additional, Majmundar, Amar J., additional, Shril, Shirlee, additional, Buerger, Florian, additional, Ottlewski, Isabel, additional, Shmukler, Boris E., additional, Topaloglu, Rezan, additional, Hashmi, Seema, additional, Hafeez, Farkhanda, additional, Emma, Francesco, additional, Greco, Marcella, additional, Laube, Guido F., additional, Fathy, Hanan M., additional, Pohl, Martin, additional, Gellermann, Jutta, additional, Milosevic, Danko, additional, Baum, Michelle A., additional, Mane, Shrikant, additional, Lifton, Richard P., additional, Kane, Patricia M., additional, Alper, Seth L., additional, and Hildebrandt, Friedhelm, additional

Published
2020
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4. Monogenic causes of chronic kidney disease in adults

Author

Connaughton, Dervla M., primary, Kennedy, Claire, additional, Shril, Shirlee, additional, Mann, Nina, additional, Murray, Susan L., additional, Williams, Patrick A., additional, Conlon, Eoin, additional, Nakayama, Makiko, additional, van der Ven, Amelie T., additional, Ityel, Hadas, additional, Kause, Franziska, additional, Kolvenbach, Caroline M., additional, Dai, Rufeng, additional, Vivante, Asaf, additional, Braun, Daniela A., additional, Schneider, Ronen, additional, Kitzler, Thomas M., additional, Moloney, Brona, additional, Moran, Conor P., additional, Smyth, John S., additional, Kennedy, Alan, additional, Benson, Katherine, additional, Stapleton, Caragh, additional, Denton, Mark, additional, Magee, Colm, additional, O’Seaghdha, Conall M., additional, Plant, William D., additional, Griffin, Matthew D., additional, Awan, Atif, additional, Sweeney, Clodagh, additional, Mane, Shrikant M., additional, Lifton, Richard P., additional, Griffin, Brenda, additional, Leavey, Sean, additional, Casserly, Liam, additional, de Freitas, Declan G., additional, Holian, John, additional, Dorman, Anthony, additional, Doyle, Brendan, additional, Lavin, Peter J., additional, Little, Mark A., additional, Conlon, Peter J., additional, and Hildebrandt, Friedhelm, additional

Published
2019
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6. Whole exome sequencing frequently detects a monogenic cause in early onset nephrolithiasis and nephrocalcinosis

Author

Daga, Ankana, primary, Majmundar, Amar J., additional, Braun, Daniela A., additional, Gee, Heon Yung, additional, Lawson, Jennifer A., additional, Shril, Shirlee, additional, Jobst-Schwan, Tilman, additional, Vivante, Asaf, additional, Schapiro, David, additional, Tan, Weizhen, additional, Warejko, Jillian K., additional, Widmeier, Eugen, additional, Nelson, Caleb P., additional, Fathy, Hanan M., additional, Gucev, Zoran, additional, Soliman, Neveen A., additional, Hashmi, Seema, additional, Halbritter, Jan, additional, Halty, Margarita, additional, Kari, Jameela A., additional, El-Desoky, Sherif, additional, Ferguson, Michael A., additional, Somers, Michael J.G., additional, Traum, Avram Z., additional, Stein, Deborah R., additional, Daouk, Ghaleb H., additional, Rodig, Nancy M., additional, Katz, Avi, additional, Hanna, Christian, additional, Schwaderer, Andrew L., additional, Sayer, John A., additional, Wassner, Ari J., additional, Mane, Shrikant, additional, Lifton, Richard P., additional, Milosevic, Danko, additional, Tasic, Velibor, additional, Baum, Michelle A., additional, and Hildebrandt, Friedhelm, additional

Published
2018
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7. Whole exome sequencing identified ATP6V1C2as a novel candidate gene for recessive distal renal tubular acidosis

Author

Jobst-Schwan, Tilman, Klämbt, Verena, Tarsio, Maureen, Heneghan, John F., Majmundar, Amar J., Shril, Shirlee, Buerger, Florian, Ottlewski, Isabel, Shmukler, Boris E., Topaloglu, Rezan, Hashmi, Seema, Hafeez, Farkhanda, Emma, Francesco, Greco, Marcella, Laube, Guido F., Fathy, Hanan M., Pohl, Martin, Gellermann, Jutta, Milosevic, Danko, Baum, Michelle A., Mane, Shrikant, Lifton, Richard P., Kane, Patricia M., Alper, Seth L., and Hildebrandt, Friedhelm

Abstract

Distal renal tubular acidosis is a rare renal tubular disorder characterized by hyperchloremic metabolic acidosis and impaired urinary acidification. Mutations in three genes (ATP6V0A4, ATP6V1B1and SLC4A1)constitute a monogenic causation in 58-70% of familial cases of distal renal tubular acidosis. Recently, mutations in FOXI1have been identified as an additional cause. Therefore, we hypothesized that further monogenic causes of distal renal tubular acidosis remain to be discovered. Panel sequencing and/or whole exome sequencing was performed in a cohort of 17 families with 19 affected individuals with pediatric onset distal renal tubular acidosis. A causative mutation was detected in one of the three “classical” known distal renal tubular acidosis genes in 10 of 17 families. The seven unsolved families were then subjected to candidate whole exome sequencing analysis. Potential disease causing mutations in three genes were detected: ATP6V1C2, which encodes another kidney specific subunit of the V-type proton ATPase (1 family); WDR72(2 families), previously implicated in V-ATPase trafficking in cells; and SLC4A2(1 family),a paralog of the known distal renal tubular acidosis gene SLC4A1.Two of these mutations were assessed for deleteriousness through functional studies. Yeast growth assays for ATP6V1C2revealed loss-of-function for the patient mutation, strongly supporting ATP6V1C2as a novel distal renal tubular acidosis gene. Thus, we provided a molecular diagnosis in a known distal renal tubular acidosis gene in 10 of 17 families (59%) with this disease, identified mutations in ATP6V1C2as a novel human candidate gene, and provided further evidence for phenotypic expansion in WDR72mutations from amelogenesis imperfecta to distal renal tubular acidosis.

Published
2020
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8. Whole exome sequencing identifies causative mutations in the majority of consanguineous or familial cases with childhood-onset increased renal echogenicity

Author

Braun, Daniela A., primary, Schueler, Markus, additional, Halbritter, Jan, additional, Gee, Heon Yung, additional, Porath, Jonathan D., additional, Lawson, Jennifer A., additional, Airik, Rannar, additional, Shril, Shirlee, additional, Allen, Susan J., additional, Stein, Deborah, additional, Al Kindy, Adila, additional, Beck, Bodo B., additional, Cengiz, Nurcan, additional, Moorani, Khemchand N., additional, Ozaltin, Fatih, additional, Hashmi, Seema, additional, Sayer, John A., additional, Bockenhauer, Detlef, additional, Soliman, Neveen A., additional, Otto, Edgar A., additional, Lifton, Richard P., additional, and Hildebrandt, Friedhelm, additional

Published
2016
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10. Regulation of the expression of the Cl- /anion exchanger pendrin in mouse kidney by acid-base status.

Author

Wagner, Carsten A., Finberg, Karin E., Stehberger, Paul A., Lifton, Richard P., Giebisch, Gerhard H., Aronson, Peter S., and Geibel, John P.

Subjects
*ION exchange (Chemistry), *KIDNEY physiology
Abstract

Regulation of the expression of the Cl- /anion exchanger pendrin in mouse kidney by acid-base status. Background. Pendrin belongs to a superfamily of Cl- /anion exchangers and is expressed in the inner ear, the thyroid gland, and the kidney. In humans, mutations in pendrin cause Pendred syndrome characterized by sensorineural deafness and goiter. Recently pendrin has been localized to the apical side of non-type A intercalated cells of the cortical collecting duct, and reduced bicarbonate secretion was demonstrated in a pendrin knockout mouse model. To investigate a possible role of pendrin in modulating acid-base transport in the cortical collecting duct, we examined the regulation of expression of pendrin by acid-base status in mouse kidney. Methods. Mice were treated orally either with an acid or bicarbonate load (0.28 mol/L NH4 Cl or NaHCO3 ) or received a K+ -deficient diet for one week. Immunohistochemistry and Western blotting was performed. Results. Acid-loading caused a reduction in pendrin protein expression levels within one day and decreased expression to 23% of control levels after one week. Concomitantly, pendrin protein was shifted from the apical membrane to the cytosol, and the relative abundance of pendrin positive cells declined. Similarly, in chronic K+ -depletion, known to elicit a metabolic alkalosis, pendrin protein levels decreased and pendrin expression was shifted to an intracellular pool with the relative number of pendrin positive cells reduced. In contrast, following oral bicarbonate loading pendrin was found exclusively in the apical membrane and the relative number of pendrin positive cells increased. Conclusions. These results are in agreement with a potential role of pendrin in bicarbonate secretion and regulation of acid-base transport in the cortical collecting duct. [ABSTRACT FROM AUTHOR]

Published
2002
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