title: Localization of cytoskeletal filaments during membrane rearrangement in rat parietal cells stimulated with gastrin.
abstract: When stomachs are stimulated to secrete acid, the intracellular canaliculi of the parietal cell increase and there is a concomitant depletion of the cytoplasmic tubulovesicular system. This change is believed to occur through the transformation of tubulovesicular membranes into intracellular canaliculi. This study was undertaken to examine the distribution of the cytoskeletons in rat gastric parietal cells during this process. In the resting parietal cells, actin filaments decorated with heavy meromyosin (HMM) were found in the cores of microvilli, extending from the apex of microvilli into the pericanalicular cytoplasm and forming radial networks. In some cases, these actin filaments were also associated with the tubulovesicles. Moreover, tubulovesicular membranes were rare in the 300 nm zone around intracellular canaliculi but numerous actin filaments were seen in this region. Soon after stimulation of the parietal cells by gastrin, tubulovesicles were closely associated with the intracellular canaliculi, while actin filaments networks adjacent to the canaliculi diminished and their labeling with HMM seemed less orderly. By immunocytochemistry, immunogold particles indicating ezrin were associated with microvillous membranes in the resting as well as stimulated parietal cells but were absent on the tubulovesicular membranes. When intermediate filaments were immunocytochemically investigated using anti-cytokeratin immunogold particles clearly labeled filamentous bundles present around the intracellular canaliculi, perinuclear spaces and under the basolateral cell membrane. Their localization was not changed after stimulation. These results suggest that actin filaments in the cytoplasm around the intracellular canaliculi may play a key role in the translocation of the tubulovesicles toward the intracellular canaliculi during the acid secreting process.
authors.affiliation: Department of Surgery, Kochi Medical School, Nankoku, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Namikawa
authors.forename: K
authors.initials: K
authors.lastname: Araki
authors.forename: T
authors.initials: T
authors.lastname: Ogata
mesh_terms: D000199:Actins / Q000648:ultrastructure; D000818:Animals; D003598:Cytoskeletal Proteins; D003599:Cytoskeleton / Q000648:ultrastructure*; D005456:Fluorescent Dyes; D005755:Gastrins / Q000494:pharmacology*; D007150:Immunohistochemistry; D007633:Keratins / Q000648:ultrastructure; D008297:Male; D016253:Microscopy, Immunoelectron; D015879:Myosin Subfragments / Q000032:analysis; D010295:Parietal Cells, Gastric / Q000187:drug effects / Q000648:ultrastructure*; D010590:Phalloidine; D010750:Phosphoproteins / Q000648:ultrastructure; D051381:Rats; D017208:Rats, Wistar; D012235:Rhodamines; D000099149:Ezrin
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D005456:Fluorescent Dyes; D005755:Gastrins; D007633:Keratins; D015879:Myosin Subfragments; D010590:Phalloidine; D010750:Phosphoproteins; D012235:Rhodamines; D000099149:Ezrin