pubmed-article:16514645 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0029418 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0037907 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0600138 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C1333928 | lld:lifeskim |
pubmed-article:16514645 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:16514645 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:16514645 | pubmed:dateCreated | 2006-8-25 | lld:pubmed |
pubmed-article:16514645 | pubmed:abstractText | We previously reported that p38 mitogen-activated protein (MAP) kinase plays a part in sphingosine 1-phosphate-stimulated heat shock protein 27 (HSP27) induction in osteoblast-like MC3T3-E1 cells. In the present study, we investigated whether phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt) is involved in the induction of HSP27 in these cells. Sphingosine 1-phosphate time dependently induced the phosphorylation of Akt. Akt inhibitor, 1L-6-hydroxymethyl-chiro-inositol 2-(R)-2-O-methyl-3-O-octadecylcarbonate, reduced the HSP27 induction stimulated by sphingosine 1-phosphate. The sphingosine 1-phosphate-induced phosphorylation of GSK-3beta was suppressed by Akt inhibitor. The sphingosine 1-phosphate-induced HSP27 levels were attenuated by LY294002 or wortmannin, PI3K inhibitors. Furthermore, LY294002 or Akt inhibitor did not affect the sphingosine 1-phosphate-induced phosphorylation of p38 MAP kinase and SB203580, a p38 MAP kinase inhibitor, had little effect on the phosphorylation of Akt. These results suggest that PI3K/Akt plays a part in the sphingosine 1-phosphate-stimulated induction of HSP27, maybe independently of p38 MAP kinase, in osteoblasts. | lld:pubmed |
pubmed-article:16514645 | pubmed:language | eng | lld:pubmed |
pubmed-article:16514645 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16514645 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16514645 | pubmed:month | Aug | lld:pubmed |
pubmed-article:16514645 | pubmed:issn | 0730-2312 | lld:pubmed |
pubmed-article:16514645 | pubmed:author | pubmed-author:Matsushima-Ni... | lld:pubmed |
pubmed-article:16514645 | pubmed:author | pubmed-author:KozawaOsamuO | lld:pubmed |
pubmed-article:16514645 | pubmed:author | pubmed-author:TakaiShinjiS | lld:pubmed |
pubmed-article:16514645 | pubmed:author | pubmed-author:TokudaHaruhik... | lld:pubmed |
pubmed-article:16514645 | pubmed:author | pubmed-author:KatoKanefusaK | lld:pubmed |
pubmed-article:16514645 | pubmed:author | pubmed-author:HanaiYoshiter... | lld:pubmed |
pubmed-article:16514645 | pubmed:copyrightInfo | (c) 2006 Wiley-Liss, Inc. | lld:pubmed |
pubmed-article:16514645 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16514645 | pubmed:day | 1 | lld:pubmed |
pubmed-article:16514645 | pubmed:volume | 98 | lld:pubmed |
pubmed-article:16514645 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16514645 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16514645 | pubmed:pagination | 1249-56 | lld:pubmed |
pubmed-article:16514645 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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pubmed-article:16514645 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16514645 | pubmed:articleTitle | Phosphatidylinositol 3-kinase/Akt plays a role in sphingosine 1-phosphate-stimulated HSP27 induction in osteoblasts. | lld:pubmed |
pubmed-article:16514645 | pubmed:affiliation | Department of Pharmacology, Gifu University Graduate School of Medicine, Gifu 501-1194, Japan. | lld:pubmed |
pubmed-article:16514645 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16514645 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:69253 | entrezgene:pubmed | pubmed-article:16514645 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16514645 | lld:entrezgene |