Major organ-specific glycoproteins in isolated brain and kidney membranes identified as Na,K-ATPase subunits by combined glycan-, lectin-, and immunoblotting.
In the present work combined glycan-, lectin-, and immunoblotting of isolated brain and kidney membranes shows that the alpha and beta subunits of Na,K-ATPase are the most abundant glycoproteins. Further, Datura stramonium and Galanthus nivalis agglutinins recognize the Na,K-ATPase subunits in a mutually exclusive manner in membranes from human, rabbit and rat brain or human, rabbit, rat, pig and dog kidney indicating the presence of species-independent organ-typical glycoforms. The glycosylation status is not related to the ouabain-sensitivity. Taken together, the data reveals organ-specific glycoforms of Na,K-ATPase which might have roles for organ identification and recognition.
Benallal
M
M
Laboratory of Experimental Cell Therapeutics, Geneva University Medical School, Switzerland.
Anner
B M
BM
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D003208:Concanavalin A / Q000378:metabolism; D004285:Dogs; D027801:Galanthus; D006001:Glycoconjugates / Q000032:analysis; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D015151:Immunoblotting; D007668:Kidney / Q000201:enzymology*; D037102:Lectins / Q000378:metabolism; D009928:Organ Specificity; D010042:Ouabain / Q000494:pharmacology; D037121:Plant Lectins; D011817:Rabbits; D051381:Rats; D012756:Sheep; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D014909:Wheat Germ Agglutinins / Q000378:metabolism
D006001:Glycoconjugates; D006023:Glycoproteins; D037102:Lectins; D037121:Plant Lectins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase