Peroxisome Proliferator-Activated Receptor-γ Increases Adiponectin Secretion via Transcriptional Repression of Endoplasmic Reticulum Chaperone Protein ERp44

• DOI: 10.1210/en.2009-1501
• Publication Date: 2010-05-20T02:12:24Z
• Authors: Qinqiang Long; Ting Lei; Bin Feng; Changjun Yin; Dan Jin; Yanling Wu; Xiaoyue Zhu; Xiaodong Chen; Li Gan; Zaiqing Yang
• Keywords: Chaperone (clinical)

Adiponectin, an adipocyte-derived hormone, is a versatile player involved in the regulation of energy homeostasis, cardiovascular disease, and diabetes. Within adipocytes, adiponectin retained lumen endoplasmic reticulum (ER) by binding to thiol protein ER resident 44 kDa (ERp44), which apparently regulated activation nuclear receptor peroxisome proliferator-activated (PPAR)-γ. However, precise role ERp44 secretion remains elusive. In present study, we investigated functional correlation between pig model. The transcription porcine was PPARγ, consistent with finding putative proliferator response element sites within promoter. Using chromatin immunoprecipitation luciferase reporter assays, demonstrated that repressed through PPARγ site located positions −981 −1004 its 5′-flanking region. human embryonic kidney 293 cells stably transfected cDNA encoding adiponectin, significantly up-regulated mRNA down-regulated observably, either treatment agonist rosiglitazone or overexpression these cells. Taken together, our results indicated essential regulatory factor for transcriptional activity ERp44, turn controls adiponectin.