Redistribution of membranes and cytoskeletal proteins in chicken oxyntic cells during the HCl secretory cycle: ultrastructural and immunofluorescence study.
Changes in ultrastructure and cytoskeletal organization by avian oxyntic cells, at the onset of HCl secretion, were analysed. Cells in resting state, induced by fasting and cimetidine, were compared with histamine stimulated secreting cells. Ultrastructural studies were done by transmission electron microscopy; the distribution of prekeratin, myosin, and filamin-like protein, by immunofluorescence; and that of F-actin using FITC-phalloidin. Resting cells show short pericellular clefts. These are increasingly deepened in secreting cells by a reorganization of the lateral cell borders involving displacement of the junctional complexes toward the cell base and incorporation of the tubular system to the luminal plasma membrane. In secreting cells, the processes of the secretory surface are concentrated in a pericellular groove. Histamine stimulation induces a drastic redistribution of cytoskeletal proteins. In chicken oxyntic cells, in addition to the F-actin cytoskeleton associated with the membranes of the secretory surface, there is a cytoskeletal ring containing F-actin, myosin, and a filamin-like protein, located at the level of the junctional complexes. In resting cells, filaments and masses of cytoskeletal matrix are associated with the zonula adherens. In secreting cells, the junctional complexes maintain their association with the filamentous ring, while the amorphous matrix is replaced by microfilaments that support the processes of the luminal surface. Intermediate filaments form a peripheral ring probably associated with the zonula adherens, and project from the ring toward the cell cytoplasm. Thus, with the onset of HCl secretion, the apical cytoskeletal ring of resting cells displaces toward the cell base. A role for this cytoskeletal ring in the changes in shape parallel to HCl secretion is discussed.
Koenig
C S
CS
Departamento de Biología Celular, Pontificia Universidad Católica de Chile, Alameda Santiago.
Dabiké
M
M
D000199:Actins / Q000378:metabolism; D000818:Animals; D002645:Chickens; D003285:Contractile Proteins / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000648:ultrastructure*; D064448:Filamins; D005455:Fluorescent Antibody Technique; D006851:Hydrochloric Acid / Q000378:metabolism*; D007425:Intracellular Membranes / Q000648:ultrastructure*; D007633:Keratins / Q000378:metabolism; D008840:Microfilament Proteins / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D010295:Parietal Cells, Gastric / Q000378:metabolism / Q000648:ultrastructure*; D014018:Tissue Distribution
D000199:Actins; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D064448:Filamins; D008840:Microfilament Proteins; D007633:Keratins; D009218:Myosins; D006851:Hydrochloric Acid