title: Feeding induces translocation of vacuolar proton ATPase and pendrin to the membrane of leopard shark (Triakis semifasciata) mitochondrion-rich gill cells.
abstract: In this study we characterized mitochondrion-rich (MR) cells and regulation of acid/base (A/B) relevant ion-transporting proteins in leopard shark (Triakis semifasciata) gills. Immunohistochemistry revealed that leopard shark gills posses two separate cell populations that abundantly express either Na⁺/K⁺-ATPase (NKA) or V-H⁺-ATPase (VHA), but not both ATPases together. Co-immunolocalization with mitochondrial Complex IV demonstrated, for the first time in shark gills, that both NKA- and VHA-rich cells are also MR cells, and that all MR cells are either NKA- or VHA-rich cells. Additionally we localized the anion exchanger pendrin to VHA-rich cells, but not NKA-rich cells. In starved sharks, VHA was localized throughout the cell cytoplasm and pendrin was present at the apical pole (but not in the membrane). However, in a significant number of gill cells from fed leopard sharks, VHA translocated to the basolateral membrane (as previously described in dogfish), and pendrin translocated to the apical membrane. Our results highlight the importance of translocation of ion-transporting proteins to the cell membrane as a regulatory mechanism for A/B regulation.
authors.affiliation: Marine Biology Research Division, Scripps Institution of Oceanography, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 93092-0202, USA.
authors.forename: Jinae N
authors.initials: JN
authors.lastname: Roa
authors.affiliation: Marine Biology Research Division, Scripps Institution of Oceanography, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 93092-0202, USA.
authors.forename: Christian L
authors.initials: CL
authors.lastname: Munévar
authors.affiliation: Marine Biology Research Division, Scripps Institution of Oceanography, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 93092-0202, USA. Electronic address: mtresguerres@ucsd.edu.
authors.forename: Martin
authors.initials: M
authors.lastname: Tresguerres
mesh_terms: D000136:Acid-Base Equilibrium; D000818:Animals; D000836:Animals, Zoo / Q000502:physiology; D002140:California; D002462:Cell Membrane / Q000378:metabolism*; D016764:Cell Polarity; D027963:Chloride-Bicarbonate Antiporters / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology / Q000378:metabolism; D004435:Eating / Q000502:physiology*; D003576:Electron Transport Complex IV / Q000378:metabolism; D005260:Female; D029941:Fish Proteins / Q000378:metabolism*; D005880:Gills / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D010140:Pacific Ocean; D020033:Protein Isoforms / Q000378:metabolism; D021381:Protein Transport; D012754:Sharks / Q000502:physiology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D025262:Vacuolar Proton-Translocating ATPases / Q000378:metabolism*
chemical_list: D027963:Chloride-Bicarbonate Antiporters; D029941:Fish Proteins; D020033:Protein Isoforms; D003576:Electron Transport Complex IV; D025262:Vacuolar Proton-Translocating ATPases; D000254:Sodium-Potassium-Exchanging ATPase
keywords: Alkaline tide; Elasmobranch; Na(+)/K(+)-ATPase; Pendrin; Proton pump; Sodium pump; V-H(+)-ATPase; slc26a4
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