[Identification of the so-called 48 K protein that interacts with illuminated rhodopsin in retinal rods, and the retinal S antigen, inductor of experimental autoimmune uveoretinitis].
In Vertebrate retinal rod outer segments, a soluble "48 K" protein binds to disk membranes upon illumination in presence of ATP or GTP (H. Kühn, Biochemistry, 17, 1978, p. 4389). Its binding to photoexcited rhodopsin implies a probable role of the "48 K" protein in the ATP dependent regulation of the photoinduced enzymatic cascade which controls the hydrolysis of cGMP. The "retinal S antigen" is also a soluble protein located in photoreceptor cells which is known to be an organ-specific auto-antigen inducing experimental autoimmune uveoretinitis. Using extracts of purified cattle and frog rod outer segments, purified bovine S antigen, and monoclonal antibodies against S antigen, we found that both proteins exhibit identical characteristics with respect to: their migration in SD S-gel electrophoresis; their binding to rod disc membranes upon illumination in presence of ATP or GTP; their immunological reactivity with monoclonal antibodies.
D000818:Animals; D000941:Antigens / Q000378:metabolism*; D001001:Anura; D019393:Arrestin; D001327:Autoimmune Diseases / Q000276:immunology; D002417:Cattle; D005136:Eye Proteins / Q000302:isolation & purification*; D010775:Photic Stimulation; D010786:Photoreceptor Cells / Q000378:metabolism*; D011485:Protein Binding; D012168:Retinal Pigments / Q000378:metabolism*; D012173:Retinitis / Q000276:immunology; D012243:Rhodopsin / Q000378:metabolism*; D014605:Uveitis / Q000276:immunology
D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D012168:Retinal Pigments; D012243:Rhodopsin
Identité de la protéine dite "48 K" qui interagit avec la rhodopsineilluminée dans les bâtonnets rétiniens et de l'"antigène s rétinien" inducteur de l'uvéo-rétinite autoimmune expérimentale.