Muscle proteins and the changes in shape of avian oxynticopeptic cells in relation to secretion.
A combined ultrastructural and biochemical study of the avian oxynticopeptic cell was performed. Scanning electron microscopy demonstrates that this cell undergoes great changes in the shape of its apical pole in relation to secretory activity. These changes are confirmed by transmission electron microscopy and by freeze-fracture images. The biochemical finding of actin- and myosin-like proteins in high-speed supernatants of homogenates of these cells as well as the ultrastructural and cytochemical localization of actin-like filaments in their apical poles suggest a possible participation of these proteins in the above-mentioned changes. Thus, the study of cytoplasmic matrix elements and of their organization may be highly relevant in the search for a correlation between structure and function in these cells.
D000199:Actins / Q000378:metabolism; D000818:Animals; D010856:Columbidae / Q000033:anatomy & histology*; D004140:Dinitrophenols / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005753:Gastric Mucosa / Q000378:metabolism / Q000648:ultrastructure*; D006651:Histocytochemistry; D009124:Muscle Proteins / Q000378:metabolism*
D000199:Actins; D004140:Dinitrophenols; D009124:Muscle Proteins