pubmed-article:18445652 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C0030281 | lld:lifeskim |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C0061355 | lld:lifeskim |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C1256369 | lld:lifeskim |
pubmed-article:18445652 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:18445652 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:18445652 | pubmed:dateCreated | 2008-5-7 | lld:pubmed |
pubmed-article:18445652 | pubmed:abstractText | Glucagon-like peptide-1 (GLP-1) is a polypeptide hormone secreted from enteroendocrine L cells and potentiates glucose-dependent insulin secretion in pancreatic beta cells. Recently the GLP-1 receptor (GLP-1 R) has been a focus for new anti-diabetic therapy with the introduction of GLP-1 analogues and DPP-IV inhibitors, and this has stimulated additional interest in the mechanisms of GLP-1 signaling. Here we identify a mechanism for GLP-1 action, showing that the scaffold protein beta-arrestin-1 mediates the effects of GLP-1 to stimulate cAMP production and insulin secretion in beta cells. Using a coimmunoprecipitation technique, we also found a physical association between the GLP-1 R and beta-arrestin-1 in cultured INS-1 pancreatic beta cells. beta-Arrestin-1 knockdown broadly attenuated GLP-1 signaling, causing decreased ERK and CREB activation and IRS-2 expression as well as reduced cAMP levels and impaired insulin secretion. However, beta-arrestin-1 knockdown did not affect GLP-1 R surface expression and ligand-induced GLP-1 R internalization/desensitization. Taken together, these studies indicate that beta-arrestin-1 plays a role in GLP-1 signaling leading to insulin secretion, defining a previously undescribed mechanism for GLP-1 action. | lld:pubmed |
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pubmed-article:18445652 | pubmed:language | eng | lld:pubmed |
pubmed-article:18445652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18445652 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18445652 | pubmed:month | May | lld:pubmed |
pubmed-article:18445652 | pubmed:issn | 1091-6490 | lld:pubmed |
pubmed-article:18445652 | pubmed:author | pubmed-author:OlefskyJerrol... | lld:pubmed |
pubmed-article:18445652 | pubmed:author | pubmed-author:ImamuraTakesh... | lld:pubmed |
pubmed-article:18445652 | pubmed:author | pubmed-author:YoshizakiTake... | lld:pubmed |
pubmed-article:18445652 | pubmed:author | pubmed-author:LuJuu-ChinJC | lld:pubmed |
pubmed-article:18445652 | pubmed:author | pubmed-author:SonodaNoriyuk... | lld:pubmed |
pubmed-article:18445652 | pubmed:author | pubmed-author:BabendureJenn... | lld:pubmed |
pubmed-article:18445652 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18445652 | pubmed:day | 6 | lld:pubmed |
pubmed-article:18445652 | pubmed:volume | 105 | lld:pubmed |
pubmed-article:18445652 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18445652 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18445652 | pubmed:pagination | 6614-9 | lld:pubmed |
pubmed-article:18445652 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:18445652 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18445652 | pubmed:articleTitle | Beta-Arrestin-1 mediates glucagon-like peptide-1 signaling to insulin secretion in cultured pancreatic beta cells. | lld:pubmed |
pubmed-article:18445652 | pubmed:affiliation | Department of Medicine, Division of Endocrinology and Metabolism, University of California at San Diego, La Jolla, CA 92093, USA. | lld:pubmed |
pubmed-article:18445652 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18445652 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:18445652 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |