Sulfatide role in the sodium pump.
Sodium efflux was studied in 22Na-loaded red blood cells in the presence of arylsulfatase, an enzyme that specifically hydrolyzes sulfatide. Sodium efflux was inhibited in proportion to the amount of arylsulfatase present. Maximum inhibition was almost as high as the efflux obtained in medium with K+ absent. At maximum inhibition 83.2% of the sulfatide content of the fragmented red blood cell membranes was hydrolyzed and ouabain-sensitive (Na+ + K+)-ATPase activity was inhibited by 100%. Sodium efflux, sulfatide content, and (Na+ + K+)-ATPase activity were unaffected with arylsulfatase in the presence of a high concentration of sulfatide. These results indicate that sulfatide plays a specific role in sodium and potassium ion transport. They also suggest that most sulfatide is localized externally in the red blood cell membrane.
D000818:Animals; D001192:Arylsulfatases / Q000494:pharmacology; D001921:Brain; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D010042:Ouabain / Q000494:pharmacology; D051381:Rats; D012964:Sodium / Q000097:blood*; D000254:Sodium-Potassium-Exchanging ATPase / Q000097:blood*; D013433:Sulfoglycosphingolipids / Q000097:blood* / Q000494:pharmacology
D013433:Sulfoglycosphingolipids; D010042:Ouabain; D012964:Sodium; D001192:Arylsulfatases; D000254:Sodium-Potassium-Exchanging ATPase