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Article: Gastric adenosine triphosphatases: a review of their possible role in HCl secretion

TitleGastric adenosine triphosphatases: a review of their possible role in HCl secretion
Authors
Issue Date1977
PublisherWB Saunders Co. The Journal's web site is located at http://www.elsevier.com/locate/gastro
Citation
Gastroenterology, 1977, v. 73 n. 4 II, p. 921-926 How to Cite?
AbstractIn the search for gastric ATPases that might be related to the mechanism of HCl secretion, an interesting and rather unique K +-stimulated ATPase has been discovered. This enzyme is isolated from oxyntic cells and has been associated with the apical plasma membrane and/or tubulovesicular system. Membrane vesicles containing the K +-stimulated ATPase transport H + into the vesicular lumen under the appropriate conditions of ATP, Mg 2+, and KCl. This process can be measured by pH electrode, binding of certain metachromatic dyes to 'energized' sites, or accumulation ratios of substances with appropriate pK values. Vesicular interior can be acidified to pH 3.5 or below. At the present time, it is difficult to distinguish between an electrogenic H + pump and an electroneutral H +/K + exchange mechanism. A hypothetical scheme for the gastric H + secretory mechanism is proposed which fits much of the data from studies on the K +-ATPase, vesicular transport, and intact gastric mucosa.
Persistent Identifierhttp://hdl.handle.net/10722/171466
ISSN
2015 Impact Factor: 18.187
2015 SCImago Journal Rankings: 7.170
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorForte, JGen_US
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:15:18Z-
dc.date.available2012-10-30T06:15:18Z-
dc.date.issued1977en_US
dc.identifier.citationGastroenterology, 1977, v. 73 n. 4 II, p. 921-926en_US
dc.identifier.issn0016-5085en_US
dc.identifier.urihttp://hdl.handle.net/10722/171466-
dc.description.abstractIn the search for gastric ATPases that might be related to the mechanism of HCl secretion, an interesting and rather unique K +-stimulated ATPase has been discovered. This enzyme is isolated from oxyntic cells and has been associated with the apical plasma membrane and/or tubulovesicular system. Membrane vesicles containing the K +-stimulated ATPase transport H + into the vesicular lumen under the appropriate conditions of ATP, Mg 2+, and KCl. This process can be measured by pH electrode, binding of certain metachromatic dyes to 'energized' sites, or accumulation ratios of substances with appropriate pK values. Vesicular interior can be acidified to pH 3.5 or below. At the present time, it is difficult to distinguish between an electrogenic H + pump and an electroneutral H +/K + exchange mechanism. A hypothetical scheme for the gastric H + secretory mechanism is proposed which fits much of the data from studies on the K +-ATPase, vesicular transport, and intact gastric mucosa.en_US
dc.languageengen_US
dc.publisherWB Saunders Co. The Journal's web site is located at http://www.elsevier.com/locate/gastroen_US
dc.relation.ispartofGastroenterologyen_US
dc.subject.meshAcridinesen_US
dc.subject.meshAdenosine Triphosphatases - Physiologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBicarbonates - Pharmacologyen_US
dc.subject.meshBiological Transport, Activeen_US
dc.subject.meshCell Membrane - Enzymologyen_US
dc.subject.meshGastric Juice - Secretionen_US
dc.subject.meshGastric Mucosa - Enzymology - Secretionen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen - Metabolismen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMagnesium - Pharmacologyen_US
dc.subject.meshPotassium - Metabolismen_US
dc.subject.meshSodium - Metabolismen_US
dc.titleGastric adenosine triphosphatases: a review of their possible role in HCl secretionen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid20386-
dc.identifier.scopuseid_2-s2.0-0017705261en_US
dc.identifier.volume73en_US
dc.identifier.issue4 IIen_US
dc.identifier.spage921en_US
dc.identifier.epage926en_US
dc.identifier.isiWOS:A1977DY03500011-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridForte, JG=26425932500en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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