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Atp6v0a4  -  ATPase, H+ transporting, lysosomal V0...

Mus musculus

Synonyms: Atp6n1b, V-ATPase 116 kDa isoform a4, V-ATPase alpha 4, V-type proton ATPase 116 kDa subunit a isoform 4, Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4, ...
 
 
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Disease relevance of Atp6v0a4

 

High impact information on Atp6v0a4

  • We have shown that a3, one of the four subunit a isoforms (a1, a2, a3, and a4), is a component of the plasma membrane V-ATPase (Toyomura, T., Oka, T., Yamaguchi, C., Wada, Y., and Futai, M. (2000) J. Biol. Chem. 275, 8760-8765) [2].
  • These results suggest that the V-ATPase, with the a4 isoform, is important for renal acid/base homeostasis [3].
  • The human and murine genes have similar genomic organization; furthermore, Atp6n1b maps to a region of mouse chromosome 6 that is syntenic with the segment of human 7q33-34 containing ATP6N1B [4].
  • Northern blot analysis of Atp6n1b reveals a 3.7-kilobase a4 transcript in kidney but not other major organs, and a reverse transcription polymerase chain reaction in 12 mouse tissues detects expression in kidney alone [4].
  • Subcellular fractionation showed that in both fetal and mature (cortex and medulla) kidneys, E1 and a4 were located in endosomes [5].
 

Anatomical context of Atp6v0a4

  • Moreover, histochemical studies show that a4 is localized in the apical and basolateral plasma membranes of cortical alpha- and beta-intercalated cells, respectively [3].
  • Taken together, these results demonstrate a4 expression in the proximal tubule, loop of Henle, distal tubule, and collecting duct and suggest that under conditions in which increased V-H(+)-ATPase activity is required, a4 is regulated by trafficking but not protein expression [1].
 

Associations of Atp6v0a4 with chemical compounds

  • These patterns contrasted with the later (from E15.5) and progressive expression of IC-specific a4, B1, G3, and C2 subunits, after the induction of the forkhead transcription factor Foxi1 [5].
  • As for the distal nephron, the majority of observations suggest that the regulation of H+-ATPase activity in response to acid-base status is mediated by the trafficking of pumps or pump sub-units, especially for the a4 subunit, rather than changes in subunit expression levels [6].
 

Analytical, diagnostic and therapeutic context of Atp6v0a4

  • Molecular cloning and characterization of Atp6n1b: a novel fourth murine vacuolar H+-ATPase a-subunit gene [4].
  • Immunofluorescence studies in murine kidney demonstrate high intensity a4 staining at the surface of intercalated cells, with additional expression in the proximal tubule (not previously reported in human kidney) [4].
  • Immunoprecipitation experiments, together with sequence similarities for other isoforms (a1, a2, and a3), indicate that the a4 isoform is a component of V-ATPase [3].
  • Immunohistochemistry, however, demonstrated a subcellular redistribution of a4 in response to the different stimuli [1].
  • NH(4)Cl or NaHCO(3) loading for 24 h, 48 h, or 7 d as well as K(+) depletion for 7 and 14 d had no influence on a4 protein expression levels in either cortex or medulla as determined by Western blotting [1].

References

  1. Localization and regulation of the ATP6V0A4 (a4) vacuolar H+-ATPase subunit defective in an inherited form of distal renal tubular acidosis. Stehberger, P.A., Schulz, N., Finberg, K.E., Karet, F.E., Giebisch, G., Lifton, R.P., Geibel, J.P., Wagner, C.A. J. Am. Soc. Nephrol. (2003) [Pubmed]
  2. From lysosomes to the plasma membrane: localization of vacuolar-type H+ -ATPase with the a3 isoform during osteoclast differentiation. Toyomura, T., Murata, Y., Yamamoto, A., Oka, T., Sun-Wada, G.H., Wada, Y., Futai, M. J. Biol. Chem. (2003) [Pubmed]
  3. a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a. Oka, T., Murata, Y., Namba, M., Yoshimizu, T., Toyomura, T., Yamamoto, A., Sun-Wada, G.H., Hamasaki, N., Wada, Y., Futai, M. J. Biol. Chem. (2001) [Pubmed]
  4. Molecular cloning and characterization of Atp6n1b: a novel fourth murine vacuolar H+-ATPase a-subunit gene. Smith, A.N., Finberg, K.E., Wagner, C.A., Lifton, R.P., Devonald, M.A., Su, Y., Karet, F.E. J. Biol. Chem. (2001) [Pubmed]
  5. Ubiquitous and kidney-specific subunits of vacuolar H+-ATPase are differentially expressed during nephrogenesis. Jouret, F., Auzanneau, C., Debaix, H., Wada, G.H., Pretto, C., Marbaix, E., Karet, F.E., Courtoy, P.J., Devuyst, O. J. Am. Soc. Nephrol. (2005) [Pubmed]
  6. Use of transgenic mice in acid-base balance studies. Cantone, A., Wang, T., Pica, A., Simeoni, M., Capasso, G. J. Nephrol. (2006) [Pubmed]
 
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