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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 574 (1989), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 65 (2003), S. 103-131 
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Notes: Abstract Acid secretion by the gastric parietal cell is regulated by paracrine, endocrine, and neural pathways. The physiological stimuli include histamine, acetylcholine, and gastrin via their receptors located on the basolateral plasma membranes. Stimulation of acid secretion typically involves an initial elevation of intracellular calcium and/or cAMP followed by activation of a cAMP-dependent protein kinase cascade that triggers the translocation and insertion of the proton pump enzyme, H,K-ATPase, into the apical plasma membrane of parietal cells. Whereas the H,K-ATPase contains a plasma membrane targeting motif, the stimulation-mediated relocation of the H,K-ATPase from the cytoplasmic membrane compartment to the apical plasma membrane is mediated by a SNARE protein complex and its regulatory proteins. This review summarizes the progress made toward an understanding of the cell biology of gastric acid secretion. In particular we have reviewed the early signaling events following histaminergic and cholinergic activation, the identification of multiple factors participating in the trafficking and recycling of the proton pump, and the role of the cytoskeleton in supporting the apical pole remodeling, which appears to be necessary for active acid secretion by the parietal cell. Emphasis is placed on identifying protein factors that serve as effectors for the mechanistic changes associated with cellular activation and the secretory response.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 242 (1974), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 341 (1980), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 71 (1983), S. 195-207 
    ISSN: 1432-1424
    Keywords: HCl secretion ; cotransport ; oxantic cell ; (H++K+)-ATPase ; apical membrane ; membrane transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We have previously reported marked structural and functional differencces between (H+/K+)-ATPase-rich vesicles obtained from resting fundic gastric mucosa and those obtained from secreting tissue. The functional differences seem to arise from activation of a permeability pathway for K+ salts in the vesicles originating from stimulated tissue. By providing the intravesicular K+ needed for the ATPase-mediated H+/K+ exchange, this pathway facilitates formation of large pH gradients (J.M. Wolosin & J.G. Forte.FEBS Lett. 125:208–212, 1981). We have now expanded our observations on the characteristics of the K-salt transport. The dependence of intravesicular acidification on the concentration of various anions or of K+ was monitored using the rate of fluorescence quenching of the pH probe, acridine orange. Rates of acid accumulation followed the series I−〉Br−〉Cl−〉NO 3 − 〉CH3SO 3 − 〉isethionate〉gluconate. The effects of exogenous ionophores on pH gradients suggested that K+-salt transport is electroneutral. On the basis of the known properties of the H+/K+ pump, we devised a method by which the rates of unidirectional K+ salt influx can be monitored via the resulting rates of H+ accumulation. Accordingly, the dependence of these rates on the concentration of K+ and Cl− was studied and subjected to a kinetic analysis. It was found that the dependence follows that expected for an electroneutral K+ and Cl− transport system with apparent Michaelis constants equal to 15±2mm for K+ and 46±5mm for Cl−. It is concluded that intravesicular acid accumulation, believed to represent HCl secretion in whole tissue, results from the combined action of a KCl symport and the well known (H++K+)-ATPase. Though the calculated maximal transport capacity of the symport exceeds by several times the maximal transport capacity of the pump, at physiological concentrations of the ions both transport systems are expected to transport K+ in opposite directions at similar rates. Implications of these observations to HCl secretion by intact tissue are discussed.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 159 (1997), S. 99 -111 
    ISSN: 1432-1424
    Keywords: Key words: Parietal cell—Acid secretion—Signal transduction—Cytoskeleton—Protein phosphorylation—Membrane fusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 61 (1981), S. 55-60 
    ISSN: 1432-1424
    Keywords: (K++H+)-ATPase ; H+/ATP stoichiometry ; gastric microsomes ; proton transport ; HCl secretion ; membrane transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The initial rate of ATP-dependent proton uptake by hog gastric vesicles was measured at pH's between 6.1 and 6.9 by measuring the loss of protons from the external space with a glass electrode. The apparent rates of proton loss were corrected for scalar proton production due to ATP hydrolysis. For vesicles in 150mm KCl and pH 6.1, corrected rates of proton uptake and ATP hydrolysis were 639±84 and 619±65 nmol/min×mg protein, respectively, giving an H+/ATP ratio of 1.03±0.7. Furthermore, at all pH's tested the ratio of the rate of proton uptake to the rate of ATP hydrolysis was not significantly different than 1.0. No proton uptake (〈10 nmol/min×mg protein) was exhibited by vesicles in 150mm NaCl at pH 6.1 despite ATP hydrolysis of 187±46 nmol/min×mg (nonproductive hydrolysis). Comparison of the rates of proton transport and ATP hydrolysis in various mixture of KCl and NaCl showed that the H+/ATP stoichiometries were not significantly different than 1.0 at all concentrations of K+ greater than 10mm. This fact suggests that the nonproductive rate is vanishingly small at these concentrations, implying that the measured H+/ATP stoichiometry is equal to the enzymatic stoichiometry. This result shows that the isolated gastric (K++H+)-ATPase is thermodynamically capable of forming the observed proton gradient of the stomach.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 83 (1985), S. 261-272 
    ISSN: 1432-1424
    Keywords: K+ and Cl− channels ; ion transport ; gastric secretion ; apical membranes ; (H++K+)-ATPase ; oxyntic cell stimulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary This study concerns the properties of rapid K+ and Cl transport pathways that are present in the (H++K+)-ATPase membrane from stimulated, and secreting, gastric oxyntic cells. Ion permeabilities in the isolated stimulation-associated vesicles were monitored via the rates of H+ efflux under conditions of exclusive H+/K+ counterflux or H+−Cl co-efflux, as well as by comparison of equilibration rates for86Rb and36Cl under conditions of equilibrium exchange and unidirectional salt flux. These latter studies suggest that Rb+ and Cl pathways are conductive and independent. In spite of the functional independence of the ion pathways, several divalent cations inhibit Rb+ and Cl isotopic exchange as well as the H+ efflux that is dependent on either K+ or anion (Cl, SCN, NO2) fluxes. Zn2+ is the more potent inhibitor, reducing by 50% the sensitive component of K+, Cl, and NO2 fluxes at about 20 μm; Mn2+ has a similar effect at 200 μm. Ni2+ and Co2+ were roughly equipotent to Mn2+ while Mg2+ and Ca2+ had not inhibitory effect. These results suggest that the stimulation-induced permeabilities, while functioning independently, may be physically linked, i.e., residing within a single entity. In similar studies carried out in (H++K+)-ATPase vesicles obtained from nonstimulated cells, no vestiges of sensitivity to the inhibitory divalent cations could be detected. The implications of these findings for the physiology of the oxyntic cell in the context of a model for membrane fusion are discussed.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 59 (1981), S. 135-142 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A procedure is described for the preparation of a membrane fraction enriched in basal-lateral plasma membranes from gastric mucosa. Gastric glands isolated from rabbit were employed as starting material, greatly reducing contamination from nonglandular cell types. The distribution of cellular components during the fractionation procedure was monitored with specific marker enzymes. (Na++K+)-ATPase, ouabain-sensitive K+-stimulatedp-nitrophenyl-phosphatase and histamine-stimulated adenylate cyclase were used as markers for basal-lateral membranes. These three markers were similarly distributed during both differential and equilibrium density gradient centrifugation. The enriched membrane fraction contained more than 30% of the total initial activities of the three basal-lateral membrane markers which were purified better than 11-fold with respect to protein. (Na++K+)-ATPase activity was resolved from the activities of acid phosphatase, pepsin, Mg2+-ATPase, cytochromec oxidase, NADPH-cytochromec reductase, glucose-6-phosphatase, (K++H+)-ATPase, DNA and RNA.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 196 (1980), S. 163-172 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The density and distribution of membrane associated particles of piglet oxyntic cell tubulovesicular and apical surface membranes were investigated during resting (nonsecreting) and secreting conditions. For the resting oxyntic cell, the abundant tubulovesicles showed a highly asymmetrical distribution of particles between fracture faces, with the P face heavily studded by particles and the E face particle deficient. The apical surface, however, had a relatively symmetrical distribution of particles on both membrane fracture faces. In contrast to the resting state, the apical surface of the stimulated oxyntic cell showed a marked asymmetry of membrane particles; the P face had a high density of particles, while there was a scarcity of particles on the E face. The observed changes in apical surface membrane particle distribution support the hypothesis that, following the initiation of acid secretion, the tubulovesicles fuse with and become an integral part of the apical surface. Thus, the apical membrane P face of the stimulated cell is enriched and the E face is diluted by the incorporation of tubulovesicular membranes.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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