کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8474063 | 1550418 | 2015 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Comprehensive assessment of chamber-specific and transmural heterogeneity in myofilament protein phosphorylation by top-down mass spectrometry
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کلمات کلیدی
MLC2vMLC1myofilamentPTMsMyosin light chain 1cTNTMLC2cTnIFT-ICREPITPMLTQMS/MS - MS / MSendo - اندوright ventricle - بطن راستleft ventricle - بطن چپTandem MS - تاندوم MSTropomyosin - تروپومیوسینcardiac troponin T - تروپونین T قلبpost-translational modifications - تغییرات پس از ترجمه، پیرایش پساترجمهLinear ion trap - تله یونی خطیLeft atrium - دهان چپRight atrium - دهلیز راستFourier transform ion cyclotron resonance - رزونانس سیکلوترون یون تبدیل تبدیل فوریهMyosin light chain 2 - زنجیره سبک Myosin 2Mass spectrometry - طیف سنجی جرمیPhosphorylation - فسفریلاسیونmyo - فیبروئیدcardiac troponin I - قلب تروپونین ITransmural heterogeneity - ناهمگونی انتقالliquid chromatography - کروماتوگرافی مایع
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Comprehensive assessment of chamber-specific and transmural heterogeneity in myofilament protein phosphorylation by top-down mass spectrometry Comprehensive assessment of chamber-specific and transmural heterogeneity in myofilament protein phosphorylation by top-down mass spectrometry](/preview/png/8474063.png)
چکیده انگلیسی
The heart is characterized by a remarkable degree of heterogeneity, the basis of which is a subject of active investigation. Myofilament protein post-translational modifications (PTMs) represent a critical mechanism regulating cardiac contractility, and emerging evidence shows that pathological cardiac conditions induce contractile heterogeneity that correlates with transmural variations in the modification status of myofilament proteins. Nevertheless, whether there exists basal heterogeneity in myofilament protein PTMs in the heart remains unclear. Here we have systematically assessed chamber-specific and transmural variations in myofilament protein PTMs, specifically, the phosphorylation of cardiac troponin I (cTnI), cardiac troponin T (cTnT), tropomyosin (Tpm), and myosin light chain 2 (MLC2). We show that the phosphorylation of cTnI and αTm vary in the different chambers of the heart, whereas the phosphorylation of MLC2 and cTnT does not. In contrast, no significant transmural differences were observed in the phosphorylation of any of the myofilament proteins analyzed. These results highlight the importance of appropriate tissue sampling-particularly for studies aimed at elucidating disease mechanisms and biomarker discovery-in order to minimize potential variations arising from basal heterogeneity in myofilament PTMs in the heart.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular and Cellular Cardiology - Volume 87, October 2015, Pages 102-112
Journal: Journal of Molecular and Cellular Cardiology - Volume 87, October 2015, Pages 102-112
نویسندگان
Zachery R. Gregorich, Ying Peng, Nicole M. Lane, Jeremy J. Wolff, Sijian Wang, Wei Guo, Huseyin Guner, Justin Doop, Timothy A. Hacker, Ying Ge,