Detection and ultrastructural localization of human smooth muscle myosin-like molecules in human non-muscle cells by specific antibodies.
Spectrin, a protein complex which is peripherally attached to the cytoplasmic surface of the human erythrocyte membrane, cannot be detected (by complement fixation with anti-spectrin antibodies) in homogenates of several different human non-muscle cells studied. On the other hand, a protein antigenically identical or similar to human smooth muscle myosin was detected (by complement fixation with antibodies to uterine smooth muscle myosin) in these cells. In the case of human fibroblast line WI38, this smooth muscle myosin like component was shown (by ferritin-antibody experiments in electron microscopy) to be at least partly associated with cytoplasmic surface of the plasma membrane of the cell. It is proposed that the spectrin complex of the erythrocyte membrane and the smooth muscle myosin-like component of the fibroblast membrane play similar roles in regulating the translational mobilities of integral proteins in their respective membranes.
D000937:Antigen-Antibody Reactions; D001792:Blood Platelets / Q000032:analysis / Q000276:immunology; D002460:Cell Line; D006367:HeLa Cells / Q000032:analysis / Q000276:immunology / Q000648:ultrastructure; D006801:Humans; D008168:Lung / Q000196:embryology; D008214:Lymphocytes / Q000032:analysis / Q000276:immunology / Q000648:ultrastructure; D008854:Microscopy, Electron; D009130:Muscle, Smooth / Q000032:analysis*; D009218:Myosins / Q000276:immunology*; D011487:Protein Conformation
D009218:Myosins