首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Effects of divalent cations on bovine testicular hyaluronidase catalyzed transglycosylation of chondroitin sulfates
Authors:Kakizaki Ikuko  Nukatsuka Isoshi  Takagaki Keiichi  Majima Mitsuo  Iwafune Mito  Suto Shinichiro  Endo Masahiko
Institution:aBeijing Institute of Genomics, Chinese Academy of Sciences, Shunyi Airport Industrial Zone B-6, Beijing 101318, China;bXiangya Hospital, Central South University, Changsha 410078, China;cBeijing Protein Innovation, Beijing 101318, China
Abstract:Two tyrosine residues (Tyr4 and Tyr76) of succinyl-CoA:3-oxoacid CoA transferase (SCOT) are sensitive to nitric oxide (NO) stress, as assessed by mass spectrometry and site-direct mutagenesis. However, monitoring the SCOT nitration in tissue or cells is challenging. Herein, we describe the development of an assay to detect nitrated SCOT directly using site-specific antibodies; the monoclonal antibodies were generated and screened against nitrated peptides of SCOT. After stringent filtration, two antibodies, anti-SCOT4N and anti-SCOT76N, which specifically recognise Tyr4 or Tyr76 of SCOT, respectively, were successfully selected. In a cell model over-expressing iNOS in the mitochondria, nitrated SCOT was significantly increased compared with control cells. In addition, in a mouse model of diabetes, nitrated Tyr4 and Tyr76 in the heart and kidney were higher compared to the control animals. Our results using monoclonal antibodies against nitrated SCOT peptides are in good agreement with the proteomic data.
Keywords:Abbreviations: SCOT  succinyl-CoA:3-oxoacid CoA transferase  NO  nitric oxide  Tyr  tyrosine  3NT  3-nitrotyrosine
本文献已被 ScienceDirect PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号