| Shao-chun Lu |
------>authors3_c= ------>paper_class1=1 ------>Impact_Factor=4.230 ------>paper_class3=2 ------>paper_class2=1 ------>vol=296 ------>confirm_bywho=wslee ------>insert_bywho=cmbsfc21 ------>Jurnal_Rank=11.5 ------>authors4_c= ------>comm_author=1 ------>patent_EDate=None ------>authors5_c= ------>publish_day=11 ------>paper_class2Letter=None ------>page2=1139 ------>medlineContent= ------>unit=E1300 ------>insert_date=20090225 ------>iam=4 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN= ------>authors_c= ------>score=500 ------>journal_name=American Journal of Physiology - Cell Physiology ------>paper_name=The essential role of Oct-2 in LPS-induced expression of iNOS in Raw 264.7 macrophages and its regulation by Trichostatin A ------>confirm_date=20090508 ------>tch_id=083008 ------>pmid=19279235 ------>page1=1133 ------>fullAbstract=This article reports on a study of the effect of trichostatin A (TSA), an inhibitor of histone deacetylase, on lipopolysaccharide (LPS)-induced expression of inducible nitric oxide synthase (iNOS) in RAW 264.7 macrophages and its underlying mechanisms. TSA pretreatment potently diminishes LPS-stimulated nitric oxide (NO) release and both mRNA and protein levels of iNOS in macrophages. The effects of TSA and LPS on transcription factors binding to two LPS-responsive elements within the iNOS promoter, one binding the NF-kappaB site and the other the octamer element, were investigated. Results show that TSA did not alter the LPS-activated NF-kappaB activity demonstrated by the nuclear translocation of p50 and p65 and by a NF-kappaB-driven reporter gene expression system. In addition, neither TSA nor LPS changed the expression of Oct-1, a ubiquitously expressed octamer binding protein. However, TSA suppressed the LPS-induced expression of Oct-2, another octamer binding protein, at both mRNA and protein levels. Chromatin immunoprecipitation assays revealed that binding of Oct-2 to the iNOS promoter was enhanced by LPS treatment; however, pretreatment with TSA resulted in loss of this binding. Moreover, forced expression of Oct-2 by transfection of pCG-Oct-2 plasmid restored the TSA-suppressed iNOS expression elevated by LPS stimulation, further indicating that Oct-2 activation is a crucial step for transcriptional activation of the iNOS gene in response to LPS stimulation in macrophages. This study demonstrates that TSA diminishes iNOS expression in LPS-treated macrophages by inhibiting Oct-2 expression and thus reducing the production of NO. ------>tmu_sno=None ------>sno=21154 ------>authors2=Hsiao-Wen Wu ------>authors3=Yen-Jen Lin ------>authors4=Shwu-Fen Chang ------>authors5= ------>authors6= ------>authors6_c= ------>authors=Shao-chun Lu ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c= ------>publish_area=0 ------>updateTitle=The essential role of Oct-2 in LPS-induced expression of iNOS in RAW 264.7 macrophages and its regulation by trichostatin A. ------>language=2 ------>check_flag=None ------>submit_date=None ------>country=None ------>no= ------>patent_SDate=None ------>update_bywho=None ------>publish_year=2009 ------>submit_flag=None ------>publish_month=5 |