Aggregation of intramembrane particles in erythrocyte membranes treated with diamide.
Treatment of erythrocytes with diamide (diazene dicarboxylic acid bis-(N,N-dimethylamide)) results in oxidation of sulfhydryl groups of the membrane, and cross-linking of membrane proteins into high molecular weight complexes. Concomitant freeze-etching studies show aggregation of intramembrane particles on the protoplasmic fracture face of erythrocyte ghost membranes treated with the oxidant. Furthermore, after a 3 h incubation of erythrocytes with 10 mM diamide at 37 degrees C, cellular energy levels declined to about 70% of control values. The data suggest that disulfide cross-linking of the major membrane proteins releases the apparent physical occlusion of the band 3 proteins within the interstices of the cytoskeletal shell. This results in the translational mobility of band 3 proteins which is reflected ultra-structurally in the freeze-etch images.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001391:Azo Compounds / Q000494:pharmacology*; D003958:Diamide / Q000494:pharmacology*; D004229:Dithiothreitol / Q000494:pharmacology; D004587:Electrophoresis, Agar Gel; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D004912:Erythrocytes / Q000187:drug effects*; D005613:Freeze Etching; D006801:Humans; D008854:Microscopy, Electron
D001391:Azo Compounds; D003958:Diamide; D000255:Adenosine Triphosphate; D004229:Dithiothreitol