Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Changes in V-ATPase subunits of human urinary exosomes reflect the renal response to acute acid/alkali loading and the defects in distal renal tubular acidosis.

Kidney international - 1 Apr 2018

Pathare Ganesh, Dhayat Nasser A, Mohebbi Nilufar, Wagner Carsten A, Bobulescu Ion A, Moe Orson W, Fuster Daniel G

Abstract excerpt

In the kidney, final urinary acidification is achieved by V-ATPases expressed in type A intercalated cells. The B1 subunit of the V-ATPase is required for maximal urinary acidification, while the role of the homologous B2 subunit is less clear. Here we examined the effect of acute acid/alkali loading in humans on B1 and B2 subunit abundance in urinary exosomes in normal individuals and of acid loading in patients...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acidosis, Renal Tubular
Share to Ammonium Chloride

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bicarbonates

Share to Exosomes

Share to Hydrogen-Ion Concentration

Share to Kidney Tubules

Share to Vacuolar Proton-Translocating ATPases

Share to Water-Electrolyte Balance

Source

Open in PubMed Open full text

Identifiers

PMID: 29310826
DOI: 10.1016/j.kint.2017.10.018
PMCID: PMC6508879

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Changes in V-ATPase subunits of human urinary exosomes reflect the renal response to acute acid/alkali loading and the defects in distal renal tubular acidosis.PMID 29310826Read ↗

Hypokalemic Distal Renal Tubular Acidosis.Semantic proximity Read ↗

Renal tubular acidosisSemantic proximity Read ↗

Kidney-specific <i>Wdr72</i> deletion leads to incomplete distal renal tubular acidosis through impaired V-ATPase B1 subunit localizationSemantic proximity Read ↗

Regulation of luminal acidification by the V-ATPase.Semantic proximity Read ↗

The lysosomal V-ATPase B1 subunit in renal proximal tubule is linked to nephropathic cystinosisSemantic proximity Read ↗

Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness.Semantic proximity Read ↗

Differential localization of vacuolar H+-ATPases containing a1, a2, a3, or a4 (ATP6V0A1-4) subunit isoforms along the nephron.Semantic proximity Read ↗

Proteomic analysis of V-ATPase-rich cells harvested from the kidney and epididymis by fluorescence-activated cell sorting.Semantic proximity Read ↗

SLC4A1 mutations that cause distal renal tubular acidosis alter cytoplasmic pH and cellular autophagy.Semantic proximity Read ↗

Incomplete distal renal tubular acidosis from a heterozygous mutation of the V-ATPase B1 subunit.Semantic proximity Read ↗

<i>SLC4A1</i> MUTATIONS THAT CAUSE DISTAL RENAL TUBULAR ACIDOSIS ALTER CYTOPLASMIC PH AND CELLULAR AUTOPHAGYSemantic proximity Read ↗

A pH imbalance is linked to autophagic dysregulation of inner ear hair cells in Atp6v1ba-deficient zebrafish.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.