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Papers In Press, published online ahead of print August 11, 2005
Department of Integrative Biology, University of Guelph, Guelph, ON N1G 2W1
Corresponding Author: dlingwoo{at}uoguelph.ca
Na+-K+-ATPase is arguably the most important enzyme in the animal cell plasma membrane, but the role of the membrane in its regulation is poorly understood. We investigated the relationship between Na+-K+-ATPase and membrane microdomains or lipid rafts enriched in sulfatide (sulfogalactosyl ceramide/SGC), a glycosphingolipid implicated as a cofactor for this enzyme, in the basolateral membrane (BLM) of rainbow trout gill epithelium. Our studies demonstrated that when trout adapt to seawater (33ppt), Na+-K+-ATPase relocates to these structures. Arylsulfatase-induced desulfation of BLM SGC prevented this relocation and significantly reduced Na+-K+-ATPase activity in seawater but not freshwater trout. We contend that Na+-K+-ATPase partitions into SGC-enriched rafts to help facilitate the up-regulation of its activity during seawater adaptation. We also suggest that differential partitioning of Na+-K+-ATPase between these novel SGC-enriched regulatory platforms results in two distinct, physiological Na+ transport modes. In addition, we extend the working definition of cholesterol-dependent raft integrity to structural dependence on the sulfate moiety of SGC in this membrane.
J. Biol. Chem, 10.1074/jbc.M506670200
Submitted on June 20, 2005
Revised on July 13, 2005
Accepted on August 11, 2005
Regulation of fish gill Na+-K+-ATPase by selective sulfatide-enriched raft partitioning during seawater adaptation
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