title: Interleukin-1beta induces the novel adipokine chemerin in adipocytes in vitro.
abstract: Chemerin has recently been characterized as a novel adipokine playing a crucial role in adipocyte differentiation and insulin signalling. In the current study, the impact of insulin resistance-inducing and proinflammatory interleukin (IL)-1beta on chemerin protein secretion and mRNA expression was determined in 3T3-L1 adipocytes. Interestingly, IL-1beta significantly induced chemerin protein secretion almost 1.3-fold from 5.89 ng/ml (basal) to 7.52 ng/ml. Furthermore, chemerin mRNA synthesis was significantly stimulated by IL-1beta in a dose-dependent fashion with 1.5-fold induction seen at IL-1beta concentrations as low as 0.07 ng/ml and maximal 2.6-fold upregulation found at 2 ng/ml effector. Induction of chemerin mRNA by IL-1beta was time-dependent in both 3T3-L1 adipocytes and brown fat cells. Signalling studies suggested that Janus kinase 2, nuclear factor kappa B, p44/42 mitogen-activated protein kinase, and phosphatidylinositol 3-kinase are involved in IL-1beta-induced chemerin mRNA expression. Furthermore, recombinant chemerin downregulated insulin-stimulated glucose uptake. Taken together, we show that chemerin is upregulated in fat cells by IL-1beta and might modulate the effects of IL-1beta on adipocyte metabolism and insulin sensitivity.
authors.affiliation: University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany.
authors.forename: Susan
authors.initials: S
authors.lastname: Kralisch
authors.forename: Sebastian
authors.initials: S
authors.lastname: Weise
authors.forename: Grit
authors.initials: G
authors.lastname: Sommer
authors.forename: Jana
authors.initials: J
authors.lastname: Lipfert
authors.forename: Ulrike
authors.initials: U
authors.lastname: Lossner
authors.forename: Matthias
authors.initials: M
authors.lastname: Bluher
authors.forename: Michael
authors.initials: M
authors.lastname: Stumvoll
authors.forename: Mathias
authors.initials: M
authors.lastname: Fasshauer
mesh_terms: D041721:3T3-L1 Cells; D052437:Adipocytes, Brown / Q000187:drug effects* / Q000378:metabolism*; D054392:Adipokines / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002454:Cell Differentiation / Q000187:drug effects / Q000502:physiology; D002478:Cells, Cultured; D018925:Chemokines; D002630:Chemotactic Factors; D016895:Culture Media, Serum-Free; D004305:Dose-Response Relationship, Drug; D005786:Gene Expression Regulation / Q000187:drug effects* / Q000502:physiology; D005947:Glucose / Q000378:metabolism; D007004:Hypoglycemic Agents / Q000494:pharmacology; D007328:Insulin / Q000494:pharmacology; D007333:Insulin Resistance / Q000502:physiology; D036341:Intercellular Signaling Peptides and Proteins; D053583:Interleukin-1beta / Q000494:pharmacology*; D053614:Janus Kinase 2 / Q000378:metabolism; D051379:Mice; D019950:Mitogen-Activated Protein Kinase 1 / Q000378:metabolism; D008954:Models, Biological; D016328:NF-kappa B / Q000378:metabolism; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism; D012333:RNA, Messenger / Q000032:analysis / Q000096:biosynthesis; D011994:Recombinant Proteins / Q000378:metabolism; D013997:Time Factors
chemical_list: D054392:Adipokines; D018925:Chemokines; D002630:Chemotactic Factors; D016895:Culture Media, Serum-Free; D007004:Hypoglycemic Agents; D007328:Insulin; D036341:Intercellular Signaling Peptides and Proteins; D053583:Interleukin-1beta; D016328:NF-kappa B; D012333:RNA, Messenger; D011994:Recombinant Proteins; C523686:chemerin protein, mouse; D019869:Phosphatidylinositol 3-Kinases; C507926:Jak2 protein, mouse; D053614:Janus Kinase 2; D019950:Mitogen-Activated Protein Kinase 1; D005947:Glucose