Association of syntaxin 3 and vesicle-associated membrane protein (VAMP) with H+/K(+)-ATPase-containing tubulovesicles in gastric parietal cells.
H+/K(+)-ATPase is the proton pump in the gastric parietal cell that is responsible for gastric acid secretion. Stimulation of acid secretion is associated with a reorganization of the parietal cells resulting in the incorporation of H+/K(+)-ATPase from a cytoplasmic membrane pool, the tubulovesicle compartment, into the apical canalicular membrane. To better characterize the role of membrane trafficking events in the morphological and physiological changes associated with acid secretion from parietal cells, we have characterized the expression and localization of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) in these cells. Each of the six different SNARE proteins examined [syntaxins 1 through 4 of 25-kDa synaptosome-associated protein, and vesicle-associated membrane protein] were found to be expressed in parietal cells. Furthermore, two of these SNAREs, vesicle-associated membrane protein and syntaxin 3, were associated with H+/K(+)-ATPase-containing tubulovesicles while the remainder were excluded from this compartment. The expression of syntaxin 1 and synaptosome-associated protein of 25 kDa in parietal cells, two SNAREs previously thought to be restricted to neuroendocrine tissues, suggests that parietal cells may utilize membrane trafficking machinery that is similar to that utilized for regulated exocytosis in neurons. Furthermore, the localization of syntaxin 3, a putative target membrane SNARE, to the tubulovesicle compartment indicates that syntaxin 3 may have an alternative function. These observations support a role for intracellular membrane trafficking events in the regulated recruitment of H+/K(+)-ATPase to the plasma membrane after parietal cell stimulation.
Peng
X R
XR
Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
Yao
X
X
Chow
D C
DC
Forte
J G
JG
Bennett
M K
MK
D000818:Animals; D000954:Antigens, Surface / Q000737:chemistry; D017506:H(+)-K(+)-Exchanging ATPase / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D006868:Hydrolysis; D018189:Immunomagnetic Separation; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism; D010295:Parietal Cells, Gastric / Q000166:cytology* / Q000201:enzymology*; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D011817:Rabbits; D051381:Rats; D017207:Rats, Sprague-Dawley; D050600:SNARE Proteins; D013347:Subcellular Fractions / Q000737:chemistry; D050825:Synaptosomal-Associated Protein 25; D050827:Syntaxin 1; D014357:Trypsin / Q000378:metabolism; D033921:Vesicular Transport Proteins
D000954:Antigens, Surface; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D050600:SNARE Proteins; C494210:Snap25 protein, rat; C494213:Stx1a protein, rat; D050825:Synaptosomal-Associated Protein 25; D050827:Syntaxin 1; D033921:Vesicular Transport Proteins; D014357:Trypsin; D017506:H(+)-K(+)-Exchanging ATPase