title: Ammonia excretion in the Atlantic hagfish (Myxine glutinosa) and responses of an Rhc glycoprotein.
abstract: Hagfishes, the most ancient of the extant craniates, demonstrate a high tolerance for a number of unfavorable environmental conditions, including elevated ammonia. Proposed mechanisms of ammonia excretion in aquatic organisms include vesicular NH(4)(+) transport and release by exocytosis in marine crabs, and passive NH(3) diffusion, active NH(4)(+) transport, and paracellular leakage of NH3 or NH(4)(+) across the gills of fishes. Recently, an emerging paradigm suggests that Rhesus glycoproteins play a vital role in ammonia transport in both aquatic invertebrates and vertebrates. This study has identified an Rh glycoprotein ortholog from the gills of Atlantic hagfish. The hagfish Rhcg shares a 56-60% amino acid identity to other vertebrate Rhcg cDNAs. Sequence information was used to produce an anti-hagfish Rhcg (hRhcg) antibody. We have used hRhcg to localize protein expression to epithelial cells of the gill and the skin. In addition, we have quantified hRhcg expression following exposure to elevated plasma ammonia levels. Animals exposed to a 3 mmol/kg NH(4)Cl load resulted in significantly elevated plasma ammonia concentrations compared with controls for up to 4 h postinjection. This correlated with net ammonia excretion rates that were also significantly elevated for up to 4 h postinjection. Rhcg mRNA expression in both the gill and skin was significantly elevated by 15 min and 1 h, respectively, and hRhcg protein expression in gills was significantly elevated at 2, 4, and 8 h postinjection. These results demonstrate a potential role for Rhcg in the excretion of ammonia in the Atlantic hagfish.
authors.affiliation: Department of Biology, Appalachian State University, Boone, North Carolina; Mount Desert Island Biological Laboratory, Salisbury Cove, Maine; and edwardssl@appstate.edu.
authors.forename: Susan L
authors.initials: SL
authors.lastname: Edwards
authors.affiliation: Department of Biology, Appalachian State University, Boone, North Carolina; Mount Desert Island Biological Laboratory, Salisbury Cove, Maine; and.
authors.forename: Justin
authors.initials: J
authors.lastname: Arnold
authors.affiliation: Department of Biology, Appalachian State University, Boone, North Carolina; Mount Desert Island Biological Laboratory, Salisbury Cove, Maine; and.
authors.forename: Salvatore D
authors.initials: SD
authors.lastname: Blair
authors.affiliation: Department of Biology, Appalachian State University, Boone, North Carolina; Mount Desert Island Biological Laboratory, Salisbury Cove, Maine; and.
authors.forename: Margaret
authors.initials: M
authors.lastname: Pray
authors.affiliation: Department of Biology, Appalachian State University, Boone, North Carolina; Mount Desert Island Biological Laboratory, Salisbury Cove, Maine; and.
authors.forename: Rachel
authors.initials: R
authors.lastname: Bradley
authors.affiliation: Mount Desert Island Biological Laboratory, Salisbury Cove, Maine; and.
authors.forename: Olivia
authors.initials: O
authors.lastname: Erikson
authors.affiliation: Department of Biology, University of Ottawa, Ottawa, Ontario, Canada.
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Walsh
mesh_terms: D000641:Ammonia / Q000378:metabolism*; D000818:Animals; D027682:Cation Transport Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D005786:Gene Expression Regulation / Q000502:physiology; D005880:Gills / Q000378:metabolism; D006196:Hagfishes / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D014867:Water / Q000737:chemistry
chemical_list: D027682:Cation Transport Proteins; D008562:Membrane Glycoproteins; D012333:RNA, Messenger; D014867:Water; D000641:Ammonia