کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8289320 | 1536302 | 2016 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The effect of cardiomyopathy mutation (R97L) in mouse cardiac troponin T on the muscle length-mediated recruitment of crossbridges is modified divergently by α- and β-myosin heavy chain
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کلمات کلیدی
NRDLSDCrossbridgeTNCHCMNTGTnI - TNILeast significant differences - اختلافات جزئی کمترanalysis of variance - تحلیل واریانسANOVA - تحلیل واریانس Analysis of varianceTransgenic - تراریختهTropomyosin - تروپومیوسینTroponin - تروپونینTroponin C - تروپونین CTroponin I - تروپونین ITroponin T - تروپونین Tcardiac troponin T - تروپونین T قلبTnT - تی ان تیstandard error - خطای استانداردMyosin heavy chain - زنجیره سنگین میوزینmuscle length - طول عضلهnon-transgenic - غیر ترانس ژنیکMHC - مجموعه سازگاری بافتی اصلیSudden cardiac death - مرگ ناگهانی قلبیCentral region - منطقه مرکزیwild-type - نوع وحشیHypertrophic cardiomyopathy - کاردیومیوپاتی هایپرتروفیک
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Hypertrophic cardiomyopathy mutations in cardiac troponin T (TnT) lead to sudden cardiac death. Augmented myofilament Ca2+ sensitivity is a common feature in TnT mutants, but such observations fail to provide a rational explanation for severe cardiac phenotypes. To better understand the mutation-induced effect on the cardiac phenotype, it is imperative to determine the effects on dynamic contractile features such as the muscle length (ML)-mediated activation against α- and β-myosin heavy chain (MHC) isoforms. α- and β-MHC are not only differentially expressed in rodent and human hearts, but they also modify ML-mediated activation differently. Mouse analog of human TnTR94L (TnTR97L) or wild-type TnT was reconstituted into de-membranated muscle fibers from normal (α-MHC) and transgenic (β-MHC) mouse hearts. TnTR97L augmented myofilament Ca2+ sensitivity by a similar amount in α- and β-MHC fibers. However, TnTR97L augmented the negative impact of strained crossbridges on other crossbridges (γ) by 22% in α-MHC fibers, but attenuated γ by 21% in β-MHC fibers. TnTR97L decreased the magnitude of ML-mediated recruitment of crossbridges (ER) by 37% in α-MHC fibers, but increased ER by 35% in β-MHC fibers. We provide a mechanistic basis for the TnTR97L-induced effects in α- and β-MHC fibers and discuss the relevance to human hearts.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 601, 1 July 2016, Pages 105-112
Journal: Archives of Biochemistry and Biophysics - Volume 601, 1 July 2016, Pages 105-112
نویسندگان
Sampath K. Gollapudi, Murali Chandra,