4.4 Article

Feeding induces translocation of vacuolar proton ATPase and pendrin to the membrane of leopard shark (Triakis semifasciata) mitochondrion-rich gill cells

出版社

ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpa.2014.04.003

关键词

Alkaline tide; Elasmobranch; Na+/K+-ATPase; Pendrin; Proton pump; slc26a4; Sodium pump; V-H+-ATPase

资金

  1. Alfred P. Sloan Foundation Research Fellowship [BR2013-103]
  2. American Physiological Society Undergraduate Summer Research Fellowship
  3. California State University Sally Casanova Pre-Doctoral scholarship
  4. San Diego Fellowship
  5. NIH Training Grant in Marine Biotechnology [GM067550]
  6. SIO funds

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In this study we characterized mitochondrion-rich (MR) cells and regulation of acid/base (A/B) relevant iontransporting 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. (C) 2014 Elsevier Inc. All rights reserved.

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