Source:http://linkedlifedata.com/resource/pubmed/id/17536021
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2007-10-23
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| pubmed:abstractText |
Gastric enterochromaffin-like (ECL) cells release histamine in response to food because of elevation of gastrin and neural release of pituitary adenylate cyclase-activating peptide (PACAP). Acid secretion is at a basal level in the absence of food but is rapidly stimulated with feeding. Rats fasted for 24 h showed a significant decrease of mucosal histamine despite steady-state expression of the histamine-synthesizing enzyme histidine decarboxylase (HDC). Comparative transcriptomal analysis using gene expression oligonucleotide microarrays of 95% pure ECL cells from fed and 24-h fasted rats, thereby eliminating mRNA contamination from other gastric mucosal cell types, identified significantly increased gene expression of the enzymes histidase and urocanase catabolizing the HDC substrate L-histidine but significantly decreased expression of the cellular L-histidine uptake transporter SN2 and of the vesicular monoamine transporter 2 (VMAT-2) responsible for histamine uptake into secretory vesicles. This was confirmed by reverse transcriptase-quantitative polymerase chain reaction of gastric fundic mucosal samples from fed and 24-h fasted rats. The decrease of VMAT-2 gene expression was also shown by a decrease in VMAT-2 protein content in protein extracts from fed and 24-h fasted rats compared with equal amounts of HDC protein and Na-K-ATPase alpha(1)-subunit protein content. These results indicate that rat gastric ECL cells regulate their histamine content during 24-h fasting not by a change in HDC gene or protein expression but by regulation of substrate concentration for HDC and a decreased histamine secretory pool.
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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/Amino Acid Transport Systems...,
http://linkedlifedata.com/resource/pubmed/chemical/Atp1a1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Histamine,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine Ammonia-Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SLC38A5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Slc18a2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Urocanate Hydratase,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Monoamine Transport...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
1531-2267
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
22
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| pubmed:volume |
31
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
183-92
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| pubmed:meshHeading |
pubmed-meshheading:17536021-Amino Acid Transport Systems, Neutral,
pubmed-meshheading:17536021-Animals,
pubmed-meshheading:17536021-Cell Count,
pubmed-meshheading:17536021-Enterochromaffin Cells,
pubmed-meshheading:17536021-Enzyme Induction,
pubmed-meshheading:17536021-Fasting,
pubmed-meshheading:17536021-Gene Expression Profiling,
pubmed-meshheading:17536021-Gene Expression Regulation,
pubmed-meshheading:17536021-Histamine,
pubmed-meshheading:17536021-Histamine Release,
pubmed-meshheading:17536021-Histidine Ammonia-Lyase,
pubmed-meshheading:17536021-Histidine Decarboxylase,
pubmed-meshheading:17536021-Male,
pubmed-meshheading:17536021-RNA, Messenger,
pubmed-meshheading:17536021-Rats,
pubmed-meshheading:17536021-Rats, Sprague-Dawley,
pubmed-meshheading:17536021-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:17536021-Transcription, Genetic,
pubmed-meshheading:17536021-Urocanate Hydratase,
pubmed-meshheading:17536021-Vesicular Monoamine Transport Proteins
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| pubmed:year |
2007
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| pubmed:articleTitle |
Fasting-induced changes in ECL cell gene expression.
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| pubmed:affiliation |
Departments of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California-Los Angeles, Los Angeles, California, USA. nilslam@ucla.edu
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| pubmed:publicationType |
Journal Article
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