Colocalization of the (Pro)renin receptor/Atp6ap2 with H+-AT pases in mouse kidney but prorenin does not acutely regulate intercalated cell H+-ATPase activity
- Daryadel, A. (Arezoo)
- Bourgeois, S. (Soline)
- Figueiredo, M.F.L. (Marta F. L.)
- Moreira, A.G. (Ana Gomes)
- Kampik, N.B. (Nicole B.)
- Oberli, L. (Lisa)
- Mohebbi, N. (Nilufar)
- Lu, X. (Xifeng)
- Meima, M.E. (Marcel)
- Danser, A.H.J. (Jan)
- Wagner, C.A. (Carsten)
Publication date
January 2016
DOI Publisher
Public Library of Science (PLoS)Abstract
The (Pro)renin receptor (P)RR/Atp6ap2 is a cell surface protein capable of binding and nonproteolytically activate prorenin. Additionally, (P)RR is associated with H+-ATPases and alternative functions in H+-ATPase regulation as well as inWnt signalling have been reported. Kidneys express very high levels of H+-ATPases which are involved in multiple functions such as endocytosis, membrane protein recycling as well as urinary acidification, bicarbonate reabsorption, and salt absorption. Here, we wanted to localize the (P)RR/Atp6ap2 along the murine nephron, exmaine whether the (P)RR/Atp6ap2 is co
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