کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10954752 | 1097918 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A non-equilibrium isoelectric focusing method to determine states of phosphorylation of cardiac troponin I: Identification of Ser-23 and Ser-24 as significant sites of phosphorylation by protein kinase C
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کلمات کلیدی
PSDcTnTOFIEFcTNTPKCcTnIElectrophoresis - الکتروفورز THAP - باشهTroponin - تروپونینcardiac troponin T - تروپونین T قلبCardiac troponin - تروپونین قلبیTime-of-Flight - زمان پروازMALDI-TOF mass spectrometry - طیف سنجی جرمی MALDI-TOFPost-source decay - فروپاشی پست منبعPhosphorylation - فسفریلاسیونPhosphopeptide - فسفوپپتیدcardiac troponin I - قلب تروپونین IMALDI - مالدیProtein kinase C - پروتئین کیناز سیmatrix-assisted laser desorption ionization - یونیزاسیون لیزر جذب ماتریس
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A non-equilibrium isoelectric focusing method to determine states of phosphorylation of cardiac troponin I: Identification of Ser-23 and Ser-24 as significant sites of phosphorylation by protein kinase C A non-equilibrium isoelectric focusing method to determine states of phosphorylation of cardiac troponin I: Identification of Ser-23 and Ser-24 as significant sites of phosphorylation by protein kinase C](/preview/png/10954752.png)
چکیده انگلیسی
Phosphorylation of cardiac troponin I (cTnI) by cAMP-dependent kinase (PKA), protein kinase C (PKC) and potentially other kinases modulates the activity of myofilaments. To elucidate the signaling mechanisms involving this modulation, it is important to determine the phosphorylation states of cTnI and its phosphorylation sites in a simple and efficient manner. In this report, we describe a method to determine the phosphorylation states of cTnI with non-equilibrium isoelectric focusing gel electrophoresis (NEIEF). Our method easily separates cTnI species with a single-charge difference. To further establish a role of PKC-dependent phosphorylation of cTnI, we have applied this approach to analysis of cTnI phosphorylation in the Tn complex following treatment with recombinant PKC, and in heart samples treated with a phorbol ester. Using mass spectrometry analysis of Tn and thin filaments, we identified Ser-23 and Ser-24 (normally considered to be PKA-dependent sites) as substrates for phosphorylation by PKC-β and PKC-ε.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular and Cellular Cardiology - Volume 38, Issue 1, January 2005, Pages 213-218
Journal: Journal of Molecular and Cellular Cardiology - Volume 38, Issue 1, January 2005, Pages 213-218
نویسندگان
Tomoyoshi Kobayashi, Xiaofeng Yang, Lori A. Walker, Richard B. Van Breemen, R. John Solaro,