Source:http://linkedlifedata.com/resource/pubmed/id/10484402
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3 Pt 1
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pubmed:dateCreated |
1999-10-28
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pubmed:abstractText |
We established a beta-escin-permeabilized gland model with the use of rabbit isolated gastric glands. The glands retained an ability to secrete acid, monitored by [14C]aminopyrine accumulation, in response to cAMP, forskolin, and histamine. These responses were all inhibited by cAMP-dependent protein kinase inhibitory peptide. Myosin light-chain kinase inhibitory peptide also suppressed aminopyrine accumulation, whereas the inhibitory peptide of protein kinase C or that of calmodulin kinase II was without effect. Guanosine-5'-O-(3-thiotriphosphate) (GTPgammaS) abolished cAMP-stimulated acid secretion concomitantly, interfering with the redistribution of H+-K+-ATPase from tubulovesicles to the apical membrane. To identify the targets of GTPgammaS, effects of peptide fragments of certain GTP-binding proteins were examined. Although none of the peptides related to Rab proteins showed any effect, the inhibitory peptide of Arf protein inhibited cAMP-stimulated secretion. These results demonstrate that our new model, the beta-escin-permeabilized gland, allows the introduction of relatively large molecules, e.g., peptides, into the cell, and will be quite useful for analyzing signal transduction of parietal cell function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminopyrine,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Escin,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/H( )-K( )-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase inhibitor peptide
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
G736-44
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10484402-Aminopyrine,
pubmed-meshheading:10484402-Animals,
pubmed-meshheading:10484402-Biological Transport,
pubmed-meshheading:10484402-Enzyme Inhibitors,
pubmed-meshheading:10484402-Escin,
pubmed-meshheading:10484402-GTP-Binding Proteins,
pubmed-meshheading:10484402-Gastric Acid,
pubmed-meshheading:10484402-Gastric Mucosa,
pubmed-meshheading:10484402-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:10484402-H(+)-K(+)-Exchanging ATPase,
pubmed-meshheading:10484402-Peptide Fragments,
pubmed-meshheading:10484402-Peptides,
pubmed-meshheading:10484402-Permeability,
pubmed-meshheading:10484402-Protein Kinases,
pubmed-meshheading:10484402-Rabbits
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pubmed:year |
1999
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pubmed:articleTitle |
Responsiveness of beta-escin-permeabilized rabbit gastric gland model: effects of functional peptide fragments.
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pubmed:affiliation |
Laboratory of Pharmacology and Toxicology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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