ZFIN ID: ZDB-PUB-100830-2
Cloning and characterization of a zebrafish homologue of human AQP1: A bifunctional water and gas channel
Chen, L.M., Zhao, J., Musa-Aziz, R., Pelletier, M.F., Drummond, I.A., and Boron, W.F.
Date: 2010
Source: American journal of physiology. Regulatory, integrative and comparative physiology   299(5): R1163-R1174 (Journal)
Registered Authors: Drummond, Iain
Keywords: Xenopus oocyte, gas permeability, intracellular pH, surface pH
MeSH Terms:
  • Air Sacs/metabolism
  • Amino Acid Sequence
  • Ammonia/metabolism*
  • Animals
  • Aquaporin 1/chemistry
  • Aquaporin 1/genetics
  • Aquaporin 1/metabolism*
  • Biological Transport
  • Blotting, Western
  • Brain/metabolism
  • Carbon Dioxide/metabolism*
  • Cloning, Molecular
  • Embryo, Nonmammalian/metabolism
  • Eye/metabolism
  • Gases
  • Gene Expression Regulation, Developmental
  • Gills/metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • In Situ Hybridization
  • Molecular Sequence Data
  • Permeability
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • Water/metabolism*
  • Xenopus
  • Zebrafish/embryology
  • Zebrafish/genetics
  • Zebrafish/metabolism*
  • Zebrafish Proteins/chemistry
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 20739606 Full text @ Am. J. Physiol. Regul. Integr. Comp. Physiol.
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ABSTRACT
The mammalian aquaporins AQP1, AQP4, and AQP5 have been shown to function not only as water channels but also as gas channels. Zebrafish have two genes encoding an AQP1 homologue, aqp1a and aqp1b. In the present study, we cloned the cDNA that encodes the zebrafish protein Aqp1a from the 72-hour postfertilization (hpf) embryo of Danio rerio, as well as from the swimbladder of the adult. The deduced amino-acid sequence of aqp1a consists of 260 amino acids and is 59% identical to human AQP1. By analyzing the genomic DNA sequence, we identified four exons in the aqp1a gene. By in-situ hybridization, aqp1a is expressed transiently in the developing vasculature and in erythrocytes from 16 to 48 hours of development. Later, at 72hpf, aqp1a is expressed in dermal ionocytes and in the swimbladder. Western blotting of adult tissues reveals that Aqp1a is most highly expressed in eye and swimbladder. Xenopus oocytes expressing aqp1a have a channel-dependent (*) osmotic water permeability (P(f)(*)) that is indistinguishable from that of human AQP1. Based on the magnitude of the transient change in surface pH (DeltapH(S)) recorded as the oocytes were exposed to either CO(2) or NH(3), we conclude that zebrafish Aqp1a is permeable to both CO(2) and NH(3). The ratio (DeltapH(S)(*))(CO(2))/P(f)(*) is about half that of human AQP1, and the ratio (DeltapHS*)NH(3)/P(f)* is about one quarter that of human AQP1. Thus, compared to human AQP1, zebrafish Aqp1a has about twice the selectivity for CO(2) over NH(3).
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