Aquaporin molecular characterization in the sea-bass (Dicentrarchus labrax): the effect of salinity on AQP1 and AQP3 expression

Comp Biochem Physiol A Mol Integr Physiol. 2007 Oct;148(2):430-44. doi: 10.1016/j.cbpa.2007.06.002. Epub 2007 Jun 12.

Abstract

Euryhaline fish possess the ability to compensate for environmental salinity changes through hydro-mineral regulation. A number of proteins have been studied in order to understand water and ion exchanges, known as fish osmoregulation. Sea-bass (Dicentrarchus labrax) cDNA sequences encoding a homologue of mammalian aquaporin (termed AQP1) and a homologue of mammalian aquaglyceroporin (termed AQP3) have been isolated and sequenced. The aquaporin amino acid sequences share respectively more than 60% and 65% identity with other known aquaporins. We have shown that salinity influences aquaporin expression levels in the gill, kidney and digestive tract, the main osmoregulatory organs. AQP1 may have a major osmoregulatory role in water transport in kidney and gut in SW-acclimated fish, whereas AQP3 could be implicated in gill water transport in FW-acclimated fish.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological
  • Animals
  • Aquaporin 1 / chemistry
  • Aquaporin 1 / genetics
  • Aquaporin 1 / metabolism*
  • Aquaporin 3 / chemistry
  • Aquaporin 3 / genetics
  • Aquaporin 3 / metabolism*
  • Bass / metabolism*
  • Brain / metabolism
  • Evolution, Molecular
  • Fish Proteins / chemistry
  • Fish Proteins / genetics
  • Fish Proteins / metabolism*
  • Gastrointestinal Tract / metabolism
  • Gene Expression Regulation
  • Gills / metabolism
  • Humans
  • Kidney / metabolism
  • Molecular Sequence Data
  • Phylogeny
  • RNA, Messenger / metabolism
  • Sequence Homology, Amino Acid
  • Sodium Chloride / metabolism*
  • Water-Electrolyte Balance*

Substances

  • Fish Proteins
  • RNA, Messenger
  • Aquaporin 1
  • Aquaporin 3
  • Sodium Chloride