کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10738695 | 1046725 | 2011 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mass spectrometric identification of tryptophan nitration sites on proteins in peroxynitrite-treated lysates from PC12 cells
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کلمات کلیدی
PBS6-nitrotryptophanNGFIEFRNSPVDF3-nitrotyrosine - 3-نیتروتیروستینBSA - BSAbovine serum albumin - آلبومین سرم گاوPolyclonal antibody - آنتی بادی های پلی کلونالTryptophan residue - باقی مانده تریپتوفانisoelectric focusing - تمرکز ذره ای الکتریکیpolyvinylidene difluoride - دی فلوئورید پلی وینیلیدینFree radicals - رادیکال آزادSOD - سدSuperoxide dismutase - سوکسوکس دیسموتازnerve growth factor - فاکتور رشد عصبNitration - نیتروژن Proteomics - پروتئومیکسPeroxynitrite - پروکسی نیتریتreactive nitrogen species - گونه های واکنش پذیر نیتروژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Mass spectrometric identification of tryptophan nitration sites on proteins in peroxynitrite-treated lysates from PC12 cells Mass spectrometric identification of tryptophan nitration sites on proteins in peroxynitrite-treated lysates from PC12 cells](/preview/png/10738695.png)
چکیده انگلیسی
One of the important sites of peroxynitrite action that affects cellular function is known to be nitration of tyrosine residues. However, tryptophan residues could be another target of peroxynitrite-dependent modification of protein function, as we have shown previously using a model protein (F. Yamakura et al., J. Biochem. 138:57-69; 2005). Here, we report the identification of several proteins that allowed us to determine the position of nitrotryptophan in their amino acid sequences in a more complex system. We modified lysates from PC12 cells with and without nerve growth factor (NGF) by treatment with peroxynitrite (0.98 or 4.9 mM). Western blot analyses using anti-6-nitrotryptophan antibody showed several immunoreactive bands and spots, which were subsequently subjected to trypsin digestion and LC-ESI-MS-MS analysis. We identified several tryptic peptides including nitrotryptophan residues, which were derived from l-lactate dehydrogenase A, malate dehydrogenase 1, M2 pyruvate kinase, and heat-shock protein 90α, in peroxynitrite-treated lysates from PC12 cells, and l-lactate dehydrogenase A, malate dehydrogenase 1, transaldorase, and lactoylglutathione lyase, in peroxynitrite-treated lysates from NGF/PC12 cells. The molar ratio of 3-nitrotyrosine to 6-nitrotryptophan in protease-digested PC12 cell lysates treated with peroxynitrite was determined to be 5.8 to 1 by using an HPLC-CoulArray system. This is the first report to identify several specific sites of nitrated tryptophan on proteins in a complex system treated with peroxynitrite and to compare the susceptibility of nitration between tryptophan and tyrosine residues of the proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 50, Issue 3, 1 February 2011, Pages 419-427
Journal: Free Radical Biology and Medicine - Volume 50, Issue 3, 1 February 2011, Pages 419-427
نویسندگان
Hiroaki Kawasaki, Keiichi Ikeda, Ayako Shigenaga, Takeshi Baba, Kenji Takamori, Hideoki Ogawa, Fumiyuki Yamakura,