pubmed-article:17916654 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17916654 | lifeskim:mentions | umls-concept:C0015350 | lld:lifeskim |
pubmed-article:17916654 | lifeskim:mentions | umls-concept:C0022131 | lld:lifeskim |
pubmed-article:17916654 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:17916654 | lifeskim:mentions | umls-concept:C0016026 | lld:lifeskim |
pubmed-article:17916654 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:17916654 | lifeskim:mentions | umls-concept:C0443264 | lld:lifeskim |
pubmed-article:17916654 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:17916654 | pubmed:dateCreated | 2007-12-31 | lld:pubmed |
pubmed-article:17916654 | pubmed:abstractText | Maintenance of pancreatic beta-cell mass depends on extracellular stimuli that promote survival and proliferation. In the islet, these stimuli come from the beta-cell microenvironment and include extracellular matrix deposited by associated vascular endothelial cells. Fibroblast growth factor receptor-1 (FGFR1) has recently been implicated as a signaling pathway that is important for normal beta-cell function. We would like to understand how extracellular matrix and FGFR1 signaling interact to promote beta-cell survival and proliferation. To examine beta-cell-specific receptor responses, we created lentiviral vectors with rat insulin promoter-driven expression of Venus fluorescent protein-tagged full-length (R1betav) and kinase-deficient (KDR1betav) FGFR1. Significant FGF-1-dependent activation of ERK1/2 was observed in betaTC3 cells, dispersed beta-cells, and beta-cells in intact islets. This response was enhanced by R1betav expression and reduced by KDR1betav expression. Plating-dispersed beta-cells on collagen type IV resulted in enhanced expression of endogenous FGFR1 that was associated with sustained activation of ERK1/2. Conversely, plating cells on laminin reduced expression of FGFR1, and this reduction was associated with transient activation of ERK1/2. Addition of neutralizing antibodies to inhibit beta-cell attachment to laminin via alpha(6)-integrin increased high-affinity FGF-1-binding at the plasma membrane and resulted in sustained ERK1/2 activity similar to cells plated on collagen type IV. These data show that the FGF-stimulated beta-cell response is negatively affected by alpha(6)-integrin binding to laminin and suggest regulation associated with vascular endothelial cell remodeling. | lld:pubmed |
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pubmed-article:17916654 | pubmed:language | eng | lld:pubmed |
pubmed-article:17916654 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17916654 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17916654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17916654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17916654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17916654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17916654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17916654 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17916654 | pubmed:month | Jan | lld:pubmed |
pubmed-article:17916654 | pubmed:issn | 0888-8809 | lld:pubmed |
pubmed-article:17916654 | pubmed:author | pubmed-author:RocheleauJona... | lld:pubmed |
pubmed-article:17916654 | pubmed:author | pubmed-author:KilkennyDawn... | lld:pubmed |
pubmed-article:17916654 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17916654 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:17916654 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17916654 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17916654 | pubmed:pagination | 196-205 | lld:pubmed |
pubmed-article:17916654 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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pubmed-article:17916654 | pubmed:year | 2008 | lld:pubmed |