Source:http://linkedlifedata.com/resource/pubmed/id/15161751
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2004-5-26
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pubmed:abstractText |
A number of factors have been reported to affect insulin synthesis in beta-cells. Although glucose is the most important regulator of insulin gene expression in pancreatic beta-cells, the mechanisms whereby glucose stimulates insulin gene transcription in response to changes in glucose concentration have not been clarified yet. In this study, we examined the role of the Ca(2+)/calmodulin (CaM)-dependent protein kinase (CaM-K) cascade in transcriptional activation of insulin. RT-PCR, Western blotting, and immunohistochemical staining analysis revealed that CaM-K kinase-alpha (CaM-KKalpha) and CaM-KIV were localized in rat pancreatic beta-cells and their cell line, INS-1. Exposure of INS-1 cells to 11.2 mmol/l glucose elicited an increase of insulin promoter activity as well as upregulation of CaM-KIV activity within 2 min after stimulation. We investigated the influence on insulin promoter activity of the constitutively active form (CaM-KIVc) or dominant-negative mutant (CaM-KIVdn) of CaM-KIV in transfected INS-1 cells. CaM-KIVc alone was sufficient, and the upstream kinase, CaM-KK, was enhanced to upregulate the insulin promoter activity in INS-1 cells. Furthermore, cotransfection of CaM-KIVdn suppressed to a significant degree the glucose-upregulated activity of the insulin promoter. Taken together, these results indicated that the CaM-KK/CaM-KIV cascade might play an important role in glucose-upregulated transcriptional activation of the insulin gene.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Camkk1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0012-1797
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pubmed:author |
pubmed-author:CaoWen MWM,
pubmed-author:ImachiHitomiH,
pubmed-author:InuzukaHiroyukiH,
pubmed-author:IshidaToshihikoT,
pubmed-author:KobayashiRyojiR,
pubmed-author:MuraoKojiK,
pubmed-author:NiimiMichioM,
pubmed-author:OhtsukaShoujiS,
pubmed-author:SayoYoshitakaY,
pubmed-author:TokumitsuHiroshiH,
pubmed-author:WongNorman C WNC,
pubmed-author:YuXiaoX
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pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1475-81
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15161751-Animals,
pubmed-meshheading:15161751-Calcium-Calmodulin-Dependent Protein Kinase Kinase,
pubmed-meshheading:15161751-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:15161751-Cell Line, Tumor,
pubmed-meshheading:15161751-Gene Expression,
pubmed-meshheading:15161751-Genes, Dominant,
pubmed-meshheading:15161751-Glucose,
pubmed-meshheading:15161751-Insulin,
pubmed-meshheading:15161751-Islets of Langerhans,
pubmed-meshheading:15161751-Isoenzymes,
pubmed-meshheading:15161751-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15161751-Rats,
pubmed-meshheading:15161751-Rats, Sprague-Dawley,
pubmed-meshheading:15161751-Transcription, Genetic,
pubmed-meshheading:15161751-Up-Regulation
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pubmed:year |
2004
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pubmed:articleTitle |
The role of calcium/calmodulin-dependent protein kinase cascade in glucose upregulation of insulin gene expression.
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pubmed:affiliation |
First Department of Internal Medicine, Kagawa Medical University, 1750-1, Miki-cho, Kita-gun, Kagawa, 761-0793, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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