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First published online July 17, 2009
Journal of Experimental Biology 212, 2303-2312 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.023085

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Review

A new paradigm for ammonia excretion in aquatic animals: role of Rhesus (Rh) glycoproteins

Patricia A. Wright^1,* and Chris M. Wood^2,3

¹ Department of Integrative Biology, University of Guelph, Guelph, ON, N1G 2W1, Canada
² Department of Biology, McMaster University, Hamilton, ON, L8S 4K1, Canada
³ Division of Marine Biology and Fisheries, Rosenstiel School of Marine Atmospheric Science, University of Miami, Miami, FL 33149, USA

^* Author for correspondence (e-mail: patwrigh{at}uoguelph.ca)

Accepted 6 May 2009

Ammonia excretion at the gills of fish has been studied for 80 years, but the mechanism(s) involved remain controversial. The relatively recent discovery of the ammonia-transporting function of the Rhesus (Rh) proteins, a family related to the Mep/Amt family of methyl ammonia and ammonia transporters in bacteria, yeast and plants, and the occurrence of these genes and glycosylated proteins in fish gills has opened a new paradigm. We provide background on the evolution and function of the Rh proteins, and review recent studies employing molecular physiology which demonstrate their important contribution to branchial ammonia efflux. Rhag occurs in red blood cells, whereas several isoforms of both Rhbg and Rhcg occur in many tissues. In the branchial epithelium, Rhcg appears to be localized in apical membranes and Rhbg in basolateral membranes. Their gene expression is upregulated during exposure to high environmental ammonia or internal ammonia infusion, and may be sensitive to synergistic stimulation by ammonia and cortisol. Rhcg in particular appears to be coupled to H⁺ excretion and Na⁺ uptake mechanisms. We propose a new model for ammonia excretion in freshwater fish and its variable linkage to Na⁺ uptake and acid excretion. In this model, Rhag facilitates NH₃ flux out of the erythrocyte, Rhbg moves it across the basolateral membrane of the branchial ionocyte, and an apical "Na⁺/NH ⁺₄ exchange complex" consisting of several membrane transporters (Rhcg, V-type H⁺-ATPase, Na⁺/H⁺ exchanger NHE-2 and/or NHE-3, Na⁺ channel) working together as a metabolon provides an acid trapping mechanism for apical excretion. Intracellular carbonic anhydrase (CA-2) and basolateral Na⁺/HCO ^–₃ cotransporter (NBC-1) and Na⁺/K⁺-ATPase play indirect roles. These mechanisms are normally superimposed on a substantial outward movement of NH₃ by simple diffusion, which is probably dependent on acid trapping in boundary layer water by H⁺ ions created by the catalysed or non-catalysed hydration of expired metabolic CO₂. Profitable areas for future investigation of Rh proteins in fish are highlighted: their involvement in the mechanism of ammonia excretion across the gills in seawater fish, their possible importance in ammonia excretion across the skin, their potential dual role as CO₂ transporters, their responses to feeding, and their roles in early life stages prior to the full development of gills.

Key words: gill, ammonia transport, early life stages, skin, H⁺-ATPase, Rhcg, Rhbg, Rhg

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