Lens sodium channels are inactivated by anti-MIP26 antibodies.
Sodium-specific channels can be functionally identified in phosphatidylcholine liposomes incorporating detergent-solubilized membrane proteins from pig lens epithelium and outer cortex. The transport of sodium is saturable, specific and protease-sensitive. MIP26 was identified in the solubilized membrane fraction and in the liposomes by means of Western blot analysis. Pre-treatment of liposomes with anti-MIP26 antiserum abolished the transport of sodium. These data indicate that MIP26 is associated to a sodium selective transport activity.
Alberti
G
G
Istituto di Oftalmologia, University of Parma, Italy.
Gandolfi
S A
SA
Maraini
G
G
D000818:Animals; D020346:Aquaporins; D015153:Blotting, Western; D005136:Eye Proteins / Q000276:immunology / Q000502:physiology*; D005614:Freeze Fracturing; D007106:Immune Sera / Q000276:immunology; D007908:Lens, Crystalline / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000502:physiology; D012964:Sodium / Q000378:metabolism; D015222:Sodium Channels / Q000502:physiology*; D013552:Swine
D020346:Aquaporins; D005136:Eye Proteins; D007106:Immune Sera; D008081:Liposomes; D008562:Membrane Glycoproteins; D015222:Sodium Channels; C030328:aquaporin 0; D012964:Sodium