Acid secretion of parietal cells is paralleled by a redistribution of NSF and alpha, beta-SNAPs and inhibited by tetanus toxin.
Stimulation of parietal cells causes fusion of intracellular tubulovesicles with the canalicular plasma membrane thereby increasing the apical membrane area up to tenfold. The presence of the SNARE proteins synaptobrevin, syntaxin1, and SNAP25 in parietal cells and their intracellular redistribution after stimulation suggest a SNARE-mediated mechanism. Here we show that NSF and alpha, beta-SNAPs which are involved in the dissociation of the SNARE complex in neurons also occur in parietal cells exhibiting subcellular distributions similar to the ones obtained for SNARE proteins and for the H+, K(+)-ATPase. More importantly proteolytic cleavage of synaptobrevin by tetanus neurotoxin completely inhibits the cAMP-dependent increase of acid secretion further supporting the crucial role SNARE proteins play in parietal cells.
Lehnardt
S
S
Institut für Anatomie, Charité Humboldt-Universität zu Berlin, 10117 Berlin, Germany.
Ahnert-Hilger
G
G
Bigalke
H
H
Jöns
T
T
D015153:Blotting, Western; D002352:Carrier Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002469:Cell Separation; D005744:Gastric Acid / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D052066:N-Ethylmaleimide-Sensitive Proteins; D010295:Parietal Cells, Gastric / Q000378:metabolism*; D050683:R-SNARE Proteins; D050600:SNARE Proteins; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D013744:Tetanus Toxin / Q000633:toxicity*; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D008565:Membrane Proteins; D050683:R-SNARE Proteins; D050600:SNARE Proteins; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D013744:Tetanus Toxin; D033921:Vesicular Transport Proteins; D052066:N-Ethylmaleimide-Sensitive Proteins