| Huang B |
------>authors3_c= ------>paper_class1=1 ------>Impact_Factor=5.947 ------>paper_class3=2 ------>paper_class2=1 ------>vol= ------>confirm_bywho=ncchang ------>insert_bywho=chung2 ------>Jurnal_Rank=7.7 ------>authors4_c= ------>comm_author= ------>patent_EDate=None ------>authors5_c= ------>publish_day=1 ------>paper_class2Letter=None ------>page2= ------>medlineContent= ------>unit=E0109 ------>insert_date=20091017 ------>iam=2 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN= ------>authors_c= ------>score=500 ------>journal_name=Cardiovasc Res ------>paper_name=Shear flow increases S-nitrosylation of proteins in endothelial cells. ------>confirm_date=20091019 ------>tch_id=096107 ------>pmid=19447776 ------>page1= ------>fullAbstract=AIMS: Endothelial cells (ECs) constantly exposed to shear flow increase nitric oxide production via the activation of endothelial nitric oxide synthase. Nitric oxide-mediated S-nitrosylation has recently been identified as an important post-translational modification that may alter signalling and/or protein function. S-nitrosylation of endothelial proteins after shear flow treatment has not been fully explored. In this study, the CyDye switch method was utilized to examine S-nitrosylated proteins in ECs after exposure to shear flow. METHODS AND RESULTS: Human umbilical vein ECs were subjected to shear flow for 30 min, and S-nitrosylated proteins were detected by the CyDye switch method. In principle, free thiols in proteins become blocked by alkylation, the S-nitrosylated bond is reduced by ascorbate, and then CyDye labels proteins. Proteins that separately labelled with Cy3 or Cy5 were mixed and subjected to two-dimensional gel electrophoresis for further analysis. More than 100 S-nitrosoproteins were detected in static and shear-treated ECs. Among these, 12 major proteins of heterogeneous function showed a significant increase in S-nitrosylation following shear flow. The S-nitrosylated residues in tropomyosin and vimentin, which were localized in the hydrophobic motif of each protein, were identified as Cys170 and Cys328, respectively. CONCLUSION: Post-translational S-nitrosylation of proteins in ECs can be detected by a reliable CyDye switch method. This flow-induced S-nitrosylation of endothelial proteins may be essential for the adaptation and remodelling of ECs under flow conditions. ------>tmu_sno=None ------>sno=22749 ------>authors2=Chen SC ------>authors3=Wang DL ------>authors4= ------>authors5= ------>authors6= ------>authors6_c= ------>authors=Huang B ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c= ------>publish_area=0 ------>updateTitle=Shear flow increases S-nitrosylation of proteins in endothelial cells. ------>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=1 |