کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10739652 | 1046883 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Protein phosphatase 1α is tyrosine-phosphorylated and inactivated by peroxynitrite in erythrocytes through the src family kinase fgr
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کلمات کلیدی
DTPAKCCPP1PMSFMOPSSIN-1FGRN-ethylmaleimideK-Cl cotransportDTTSrc family tyrosine kinase3-morpholinosydnonimine - 3-مورفولینویدونیمینیمDMSO - DMSOONOO− - ONOO-p-NPP - P-NPPpara-nitrophenyl phosphate - para-nitrofenyl phosphateOxidative stress - تنش اکسیداتیوDiethylenetriaminepentaacetic acid - دی اتیلنتریمین پنتا اسیدهای اسیدdithiothreitol - دیتیوتریتولDimethyl sulfoxide - دیمتیل سولفواکسیدphosphotyrosine - فسفاتیزینTyrosine phosphorylation - فسفوریلاسیون تروفوزینphenylmethylsulfonyl fluoride - فنیل متیل سولفونیل فلورایدLyn - لاینNEM - نهNitric oxide - نیتریک اکسیدHck - هکPeroxynitrite - پروکسی نیتریتSerine/threonine protein phosphatase - پروین فسفاتاز سریین / ترئونینhematopoietic cell kinase - کیناز سلولی خونریزیred blood cell - گلبول قرمز، اریتروسیت
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Protein serine/threonine phosphorylation is a significant component of the intracellular signal that together with tyrosine phosphorylation regulates several processes, including cell-cycle progression, muscle contraction, transcription, and neuronal signaling. Cross-talk between phosphoserine/threonine- and phosphotyrosine-mediated pathways is not yet well understood. In this study we found that peroxynitrite, a physiological oxidant formed by the fast radical-radical reaction between the nitric oxide and the superoxide anion, induced tyrosine phosphorylation of the serine/threonine protein phosphatase 1α (PP1α) in human erythrocytes through activation of src family kinases. We have previously shown in mouse red cells that upregulation of the src kinase fgr phosphorylates PP1α, acting as an upstream negative regulator of PP1α, and downregulates K-Cl cotransport. Here we found that PP1α is a selective substrate of peroxynitrite-activated fgr and that tyrosine phosphorylation of PP1α corresponds to an inhibition of its enzymatic activity. Despite fgr activation and PP1α downregulation, peroxynitrite stimulated in a dose-dependent fashion the function of the K-Cl cotransporter. In an attempt to understand the mechanism of K-Cl cotransport activation, we found that the effect of peroxynitrite is completely reversed by dithriothreitol, suggesting that peroxynitrite acts as an oxidizing agent by an SH-dependent and PP1α-independent mechanism. These findings highlight a novel function of peroxynitrite in regulating the intracellular signal transduction pathways involving serine/threonine phosphorylation and the functional role of proteins that are targets of these phosphatases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 38, Issue 12, 15 June 2005, Pages 1625-1636
Journal: Free Radical Biology and Medicine - Volume 38, Issue 12, 15 June 2005, Pages 1625-1636
نویسندگان
Cinzia Mallozzi, Lucia De Franceschi, Carlo Brugnara, A.M. Michela Di Stasi,