| pubmed-article:20382119 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20382119 | lifeskim:mentions | umls-concept:C0023796 | lld:lifeskim |
| pubmed-article:20382119 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
| pubmed-article:20382119 | lifeskim:mentions | umls-concept:C0052851 | lld:lifeskim |
| pubmed-article:20382119 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20382119 | pubmed:dateCreated | 2010-5-10 | lld:pubmed |
| pubmed-article:20382119 | pubmed:abstractText | Activin B, consisting of two inhibin betaB (INHBB) subunits, is a hormone known to affect gonadal function, reproduction and fetal development. We have reported that INHBB and activin B receptors are highly expressed in adipocytes suggesting that activin B may have local effects in adipose tissue. In this study, we investigate the effect of activin B on lipolysis, measured as release of non-esterified fatty acids and free glycerol. Recombinant activin B decreased lipolysis in a concentration-dependent manner and increased intracellular triglyceride content in 3T3-L1 adipocytes. siRNA-mediated knock-down of INHBB expression increased lipolysis, and this effect was abolished by addition of recombinant activin B. In line with its inhibitory effect on lipolysis, activin B caused a down regulation of the expression of adipose triglyceride lipase and hormone sensitive lipase, key genes involved in lipolysis. In summary, we suggest that activin B is a novel adipokine that inhibits lipolysis in a paracrine or autocrine manner. | lld:pubmed |
| pubmed-article:20382119 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20382119 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20382119 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20382119 | pubmed:month | May | lld:pubmed |
| pubmed-article:20382119 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:20382119 | pubmed:author | pubmed-author:CarlssonLena... | lld:pubmed |
| pubmed-article:20382119 | pubmed:author | pubmed-author:SvenssonPer-A... | lld:pubmed |
| pubmed-article:20382119 | pubmed:author | pubmed-author:MagnussonBjör... | lld:pubmed |
| pubmed-article:20382119 | pubmed:author | pubmed-author:SjöholmKajsaK | lld:pubmed |
| pubmed-article:20382119 | pubmed:copyrightInfo | Copyright (c) 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:20382119 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20382119 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:20382119 | pubmed:volume | 395 | lld:pubmed |
| pubmed-article:20382119 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20382119 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20382119 | pubmed:pagination | 373-6 | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:meshHeading | pubmed-meshheading:20382119... | lld:pubmed |
| pubmed-article:20382119 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20382119 | pubmed:articleTitle | Activin B inhibits lipolysis in 3T3-L1 adipocytes. | lld:pubmed |
| pubmed-article:20382119 | pubmed:affiliation | Department of Molecular and Clinical Medicine, Institute of Medicine, Sahlgrenska Academy, Gothenburg University, Sahlgrenska Center for Cardiovascular and Metabolic Research, Gothenburg, Sweden. | lld:pubmed |
| pubmed-article:20382119 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20382119 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:16324 | entrezgene:pubmed | pubmed-article:20382119 | lld:entrezgene |
