Regulation of renal aquaporin water channels in acute pyelonephritis

This study aimed to investigate if AQP2 expression in host cells increases UPEC infection efficiency and to identify specific bacterial components that mediate AQP2 plasma membrane insertion. Since the transepithelial water permeability in the collecting duct is co-determined by AQP3 and AQP4, we also investigated whether AQP3 and AQP4 localization is altered in the APN mouse model. We show that AQP2 expression does not increase UPEC infection efficiency and that AQP2 was targeted to the plasma membrane in AQP2 expressing cells in response to the two pathogen-associated molecular patterns (PAMPs), lipopolysaccharide and peptidoglycan. In contrast to AQP2, the subcellular localizations of AQP1, AQP3, and AQP4 were unaffected both in lysate-incubated cell cultures and in the APN mouse model. Our finding demonstrated that cellular exposure to lipopolysaccharide and peptidoglycan can trigger the insertion of AQP2 in the plasma membrane revealing a new regulatory pathway for AQP2 plasma membrane translocation, which may potentially be exploited in intervention strategies.PMID:38525539 | DOI:10.1152/ajpcell.00308.2023

Source: Am J Physiol Cell Ph... - March 25, 2024 Category: Cytology Authors: Christina V Ernstsen Marianna Ranieri Fr édéric H Login Isra K Mahmoud Jacob R Therkildsen Giovanna Valenti Helle Praetorius Rikke N ørregaard Lene N Nejsum Source Type: research