title: Prorenin Receptor Homologue VHA-20 is Critical for Intestinal pH Regulation, Ion and Water Management and Larval Development in C. elegans.
abstract: The prorenin receptor (ATP6AP2) is a multifunctional transmembrane protein; it is a constituent of proton-translocating V-ATPase, a non-proteolytic activator of renin and an adaptor in the Wnt/β-catenin pathway. Here, we studied vha-20, one of the two prorenin receptor homologues that are identified by sequence similarity in the C. elegans genome. We show that vha-20 (R03E1.2) is prominently expressed in the intestine, in the excretory cell and in amphid neurons, tissues critical for regulation of ion and water management. The expression of vha-20 in the intestine is dependent on NHR-31, a nuclear receptor related to HNF4. VHA-20 is indispensable for normal larval development, acidification of the intestine, and is required for nutrient uptake. Inhibition of vha-20 by RNAi leads to complex deterioration of water and pH gradients at the level of the whole organism including distention of pseudocoelome cavity. This suggests new roles of prorenin receptor in the regulation of body ion and water management and in acidification of intestinal lumen in nematodes.
authors.affiliation: Institute of Cellular Biology and Pathology, First Faculty of Medicine, Charles University in Prague, Czech Republic.
authors.forename: V
authors.initials: V
authors.lastname: Zima
authors.affiliation: Institute of Cellular Biology and Pathology, First Faculty of Medicine, Charles University in Prague, Czech Republic.
authors.forename: K
authors.initials: K
authors.lastname: Šebková
authors.affiliation: Institute of Cellular Biology and Pathology, First Faculty of Medicine, Charles University in Prague, Czech Republic.
authors.forename: K
authors.initials: K
authors.lastname: Šimečková
authors.affiliation: Institute of Cellular Biology and Pathology, First Faculty of Medicine, Charles University in Prague, Czech Republic.
authors.forename: T
authors.initials: T
authors.lastname: Dvořák
authors.affiliation: University of Cambridge Metabolic Research Laboratories, Wellcome Trust-Medical Research Council Institute of Metabolic Science, Cambridge, United Kingdom.
authors.forename: V
authors.initials: V
authors.lastname: Saudek
authors.affiliation: Institute of Cellular Biology and Pathology, First Faculty of Medicine, Charles University in Prague, Czech Republic.
authors.forename: M
authors.initials: M
authors.lastname: Kostrouchová
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D020869:Gene Expression Profiling; D006706:Homeostasis / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D007814:Larva / Q000502:physiology; D016133:Polymerase Chain Reaction; D059467:Transcriptome; D025262:Vacuolar Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D014867:Water / Q000378:metabolism*
chemical_list: D029742:Caenorhabditis elegans Proteins; D014867:Water; D025262:Vacuolar Proton-Translocating ATPases