title: SNARE proteins and rab3A contribute to canalicular formation in parietal cells.
abstract: SNARE proteins - rab3A - parietal cells - H+/K+-ATPase When stimulated by histamine, acetylcholine, or gastrin the luminal compartments of oxyntic parietal cells display conspicuous morphological changes. The luminal plasma membrane surface becomes greatly expanded, while the cytoplasmic tubulovesicles are decreased in parallel. Due to these membrane rearrangements the H+/K(+)-ATPase obtains access to the luminal surface, where proton secretion occurs. The stimulation-induced translocation of H+/K(+)-ATPase involves a fusion process. Exocytotic membrane fusion in neurons is achieved by the highly regulated interaction of mainly three proteins, the vesicle protein synaptobrevin and the plasma membrane proteins syntaxin and SNAP25 (synaptosomal-associated protein of 25 kDa), also referred to as SNARE proteins. Using immunofluorescence microscopy we analysed the subcellular distribution of neuronal synaptic proteins and rab3A in resting and stimulated parietal cells from pig and rat. In resting cells all synaptic proteins colocalized with the H+/ K(+)-ATPase trapped in the tubulovesicular compartment. After stimulation, translocated H+/K(+)-ATPase showed a typical canalicular distribution. Syntaxin, synaptobrevin, SNAP25 and rab3A underwent a similar redistribution in stimulated cells and consequently localized to the canalicular compartment. Using immunoprecipitation we found that the SNARE complex consisting of synaptobrevin, syntaxin and SNAP25, which is a prerequisite for membrane fusion in neurons, is also assembled in parietal cells. In addition the parietal cell-derived synaptobrevin could be proteolytically cleaved by tetanus toxin light chain. These data may provide evidence that SNARE proteins and rab3A are functionally involved in the stimulation-induced translocation of the H+/K(+)-ATPase.
authors.affiliation: Institut für Anatomie der Charité, Humboldt-Universität zu Berlin, Germany. thomas.joens@charite.de
authors.forename: T
authors.initials: T
authors.lastname: Jöns
authors.forename: S
authors.initials: S
authors.lastname: Lehnardt
authors.forename: H
authors.initials: H
authors.lastname: Bigalke
authors.forename: H K
authors.initials: HK
authors.lastname: Heim
authors.forename: G
authors.initials: G
authors.lastname: Ahnert-Hilger
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D002352:Carrier Proteins / Q000378:metabolism*; D005753:Gastric Mucosa / Q000166:cytology / Q000378:metabolism; D005755:Gastrins / Q000494:pharmacology; D017506:H(+)-K(+)-Exchanging ATPase / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D005810:Multigene Family; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010295:Parietal Cells, Gastric / Q000378:metabolism*; D011233:Precipitin Tests; D050683:R-SNARE Proteins; D051381:Rats; D017208:Rats, Wistar; D013552:Swine; D050825:Synaptosomal-Associated Protein 25; D020826:rab3A GTP-Binding Protein / Q000378:metabolism*
chemical_list: D000911:Antibodies, Monoclonal; D002352:Carrier Proteins; D005755:Gastrins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins; C494210:Snap25 protein, rat; D050825:Synaptosomal-Associated Protein 25; D017506:H(+)-K(+)-Exchanging ATPase; D020826:rab3A GTP-Binding Protein