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Colocalization of the (Pro)renin Receptor/Atp6ap2 with H+-ATPases in Mouse Kidney but Prorenin Does Not Acutely Regulate Intercalated Cell H+-ATPase Activity

Daryadel, Arezoo ; Bourgeois, Soline ; Figueiredo, Marta F L ; Gomes Moreira, Ana ; Kampik, Nicole B ; Oberli, Lisa ; Mohebbi, Nilufar ; Lu, Xifeng ; Meima, Marcel E ; Danser, A H Jan ; Wagner, Carsten A Fotiadis, Dimitrios

PloS one, 2016, Vol.11 (1), p.e0147831-e0147831 [Revista revisada por pares]

United States: Public Library of Science

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Colocalization of the (Pro)renin Receptor/Atp6ap2 with H+-ATPases in Mouse Kidney but Prorenin Does Not Acutely Regulate Intercalated Cell H+-ATPase Activity
Autor: Daryadel, Arezoo ; Bourgeois, Soline ; Figueiredo, Marta F L ; Gomes Moreira, Ana ; Kampik, Nicole B ; Oberli, Lisa ; Mohebbi, Nilufar ; Lu, Xifeng ; Meima, Marcel E ; Danser, A H Jan ; Wagner, Carsten A
Fotiadis, Dimitrios
Materias: Acidification ; Adenosine triphosphatase ; Ammonium Chloride - pharmacology ; Animals ; Anion Transport Proteins - genetics ; Anion Transport Proteins - metabolism ; Aquaporin 2 - genetics ; Aquaporin 2 - metabolism ; Bicarbonates ; Biology and Life Sciences ; Carbonates ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell surface ; Dogs ; Drinking water ; Endocytosis ; Experiments ; Gene Expression Regulation ; H+-transporting ATPase ; Hydrogen ; Hypertension ; Immunohistochemistry ; Internal medicine ; Kidney Cortex - cytology ; Kidney Cortex - drug effects ; Kidney Cortex - metabolism ; Kidney Medulla - cytology ; Kidney Medulla - drug effects ; Kidney Medulla - metabolism ; Kidney Tubules, Collecting - cytology ; Kidney Tubules, Collecting - drug effects ; Kidney Tubules, Collecting - metabolism ; Kidney Tubules, Proximal - cytology ; Kidney Tubules, Proximal - drug effects ; Kidney Tubules, Proximal - metabolism ; Kidneys ; Kinases ; Localization ; Madin Darby Canine Kidney Cells ; Male ; Medicine ; Medicine and Health Sciences ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Membrane proteins ; Membranes ; Metabolism ; Mice ; Mice, Inbred C57BL ; mRNA ; Pharmacology ; Phosphorylation ; Physiology ; Plasma ; Protein turnover ; Proteins ; Proton-Translocating ATPases - genetics ; Proton-Translocating ATPases - metabolism ; Proximal tubules ; Reabsorption ; Receptors, Cell Surface - genetics ; Receptors, Cell Surface - metabolism ; Renin ; Renin - pharmacology ; Renin-Angiotensin System - drug effects ; Research and Analysis Methods ; Rodents ; Salts ; Signal Transduction ; Signaling ; Sodium Bicarbonate - pharmacology ; Sodium chloride ; Sodium Chloride - pharmacology ; Sodium-Phosphate Cotransporter Proteins, Type IIa - genetics ; Sodium-Phosphate Cotransporter Proteins, Type IIa - metabolism ; Solute Carrier Family 12, Member 1 - genetics ; Solute Carrier Family 12, Member 1 - metabolism ; Solute Carrier Family 12, Member 3 - genetics ; Solute Carrier Family 12, Member 3 - metabolism ; Sulfate Transporters ; Wnt protein
Es parte de: PloS one, 2016, Vol.11 (1), p.e0147831-e0147831
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Competing Interests: The authors have declared that no competing interests exist.
Conceived and designed the experiments: AD NM AHJD CAW. Performed the experiments: AD SB MFLF AGM NBK LO NM XL MEM. Analyzed the data: AD SB NBK CAW. Contributed reagents/materials/analysis tools: XL MEM AHJD. Wrote the paper: AD SB MFLF NBK AHJD CAW.
Descripción: The (Pro)renin receptor (P)RR/Atp6ap2 is a cell surface protein capable of binding and non-proteolytically activate prorenin. Additionally, (P)RR is associated with H(+)-ATPases and alternative functions in H(+)-ATPase regulation as well as in Wnt 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 coregulated with other H(+)-ATPase subunits, and whether acute stimulation of the (P)RR/Atp6ap2 with prorenin regulates H(+)-ATPase activity in intercalated cells in freshly isolated collecting ducts. We localized (P)PR/Atp6ap2 along the murine nephron by qPCR and immunohistochemistry. (P)RR/Atp6ap2 mRNA was detected in all nephron segments with highest levels in the collecting system coinciding with H(+)-ATPases. Further experiments demonstrated expression at the brush border membrane of proximal tubules and in all types of intercalated cells colocalizing with H(+)-ATPases. In mice treated with NH4Cl, NaHCO3, KHCO3, NaCl, or the mineralocorticoid DOCA for 7 days, (P)RR/Atp6ap2 and H(+)-ATPase subunits were regulated but not co-regulated at protein and mRNA levels. Immunolocalization in kidneys from control, NH4Cl or NaHCO3 treated mice demonstrated always colocalization of PRR/Atp6ap2 with H(+)-ATPase subunits at the brush border membrane of proximal tubules, the apical pole of type A intercalated cells, and at basolateral and/or apical membranes of non-type A intercalated cells. Microperfusion of isolated cortical collecting ducts and luminal application of prorenin did not acutely stimulate H(+)-ATPase activity. However, incubation of isolated collecting ducts with prorenin non-significantly increased ERK1/2 phosphorylation. Our results suggest that the PRR/Atp6ap2 may form a complex with H(+)-ATPases in proximal tubule and intercalated cells but that prorenin has no acute effect on H(+)-ATPase activity in intercalated cells.
Editor: United States: Public Library of Science
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Colocalization of the (Pro)renin Receptor/Atp6ap2 with H+-ATPases in Mouse Kidney but Prorenin Does Not Acutely Regulate Intercalated Cell H+-ATPase Activity

Daryadel, Arezoo ; Bourgeois, Soline ; Figueiredo, Marta F L ; Gomes Moreira, Ana ; Kampik, Nicole B ; Oberli, Lisa ; Mohebbi, Nilufar ; Lu, Xifeng ; Meima, Marcel E ; Danser, A H Jan ; Wagner, Carsten A Fotiadis, Dimitrios

United States: Public Library of Science

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