Expression of the non-erythroid Rh glycoproteins in mammalian tissues.
A novel family of proteins, the Mep/AMT/Rh glycoprotein family may mediate important roles in transmembrane ammonia transport in a wide variety of single-celled and multicellular organisms. Results from our laboratory have examined the expression of the non-erythroid proteins, Rh B Glycoprotein (Rhbg) and Rh C glycoprotein (Rhcg), in a wide variety of mammalian tissues. In the kidney, Rhbg and Rhcg are present in distal nephron sites responsible for ammonia secretion. In the mouse kidney, Rhbg immunoreactivity is exclusively basolateral and Rhcg immunoreactivity is exclusively apical, whereas in the rat kidney Rhcg exhibits both apical and basolateral expression. Chronic metabolic acidosis increases Rhcg expression in the outer and inner medulla of the rat kidney; these changes, at least in the outer medullary collecting duct, involve changes in total cellular protein expression in both principal and intercalated cell and changes in its subcellular localization. In the liver, Rhbg is present in the basolateral plasma membrane of the perivenous hepatocyte and Rhcg is present in bile duct epithelia. In the gastrointestinal tract, Rhbg and Rhcg exhibit cell-specific, axially heterogeneous, and polarized expression. These patterns of expression are consistent with Rhbg and Rhcg mediating important roles in mammalian ammonia biology. The lack of the effect of chronic metabolic acidosis on Rhbg expression raises the possibility that Rhbg may function either as ammonia sensing-protein or that it may mediate roles other than ammonia transport.
Weiner
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Nephrology and Hypertension Section, North Florida/South Georgia Veterans Health System, Gainesville, FL, USA. weineid@ufl.edu
D000138:Acidosis / Q000378:metabolism; D000641:Ammonia / Q000378:metabolism*; D000818:Animals; D001652:Bile Ducts / Q000378:metabolism; D027682:Cation Transport Proteins / Q000096:biosynthesis* / Q000235:genetics; D016764:Cell Polarity; D004847:Epithelial Cells / Q000378:metabolism; D005260:Female; D041981:Gastrointestinal Tract / Q000166:cytology / Q000378:metabolism; D005786:Gene Expression Regulation; D006023:Glycoproteins / Q000096:biosynthesis* / Q000235:genetics; D022781:Hepatocytes / Q000378:metabolism*; D007685:Kidney Tubules, Collecting / Q000378:metabolism*; D007686:Kidney Tubules, Distal / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000096:biosynthesis* / Q000235:genetics; D026901:Membrane Transport Proteins / Q000096:biosynthesis* / Q000235:genetics; D051379:Mice; D018345:Mice, Knockout; D009928:Organ Specificity; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D013045:Species Specificity; D013347:Subcellular Fractions / Q000378:metabolism
D027682:Cation Transport Proteins; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D012333:RNA, Messenger; C508142:Rh type B glycoprotein, rat; C508143:Rh type C glycoprotein, rat; C486033:RhBG protein, mouse; C485880:Rhcg protein, mouse; D000641:Ammonia