Effect of different troponin T-tropomyosin combinations on thin filament activation.
Effect of different troponin T-tropomyosin combinations on thin filament activation.
复制标题
不同肌钙蛋白 T-原肌球蛋白组合对细丝激活的影响。
DOI：
10.1016/0022-2836(87)90300-7
复制
发表时间：
1987
影响因子：
5.6
通讯作者：
P. Brandt
中科院分区：
文献类型：
--
作者：
F. Schachat;Michael S. Diamond;P. Brandt
透化兔快骨骼肌纤维对钙的反应由它们表达的肌钙蛋白T（TnT）和原肌球蛋白（Tm）亚型决定。主要表达TnT 2f和α 2 Tm的纤维比TnT 1、TnT 3f和αβ Tm占优势的纤维表现出更陡的pCa/张力关系。肌钙蛋白C提取研究表明，较低的斜率并不是由细丝上不太协调的过渡引起的：在所有快纤维中，Tn → Tm调节链作为一个单位激活。由于TnT变体在其N-末端区段中不同，并且该区域在调节链上与相邻的TMS重叠，我们提出Tm的端到端重叠和TnT对该相互作用的影响是调节链向在钙存在下发生的活性状态的协调过渡的基础。此外，不同的Tn-Tm组合对松弛和活动状态下TnC对钙的亲和力的比率的影响似乎是体内快纤维收缩特性的重要决定因素。
The response of permeabilized rabbit fast skeletal muscle fibers to calcium is determined by the troponin T (TnT) and tropomyosin (Tm) isoforms they express. Fibers expressing primarily TnT2fandα2Tm exhibit steeper pCa/tension relations than those in which either TnT1for TnT3fand αβ Tm predominate. Troponin C extraction studies show that lower slopes do not result from a less concerted transition on the thin filament: the TnTm regulatory strand activates as a unit in all fast fibers. Because the TnT variants differ in their N-terminal segments, and this region overlaps adjacent Tms on the regulatory strand, we propose that both the end-to-end overlap of Tm and the effect of TnT on that interaction are the basis of the concerted transition of the regulatory strand to the active state that occurs in the presence of calcium. Moreover, the effect of different Tn-Tm combinations on the ratio of the affinities of TnC for calcium in the relaxed and active states appears to be a significant determinant of the contractile properties of fast fibersin vivo.
DOI：
10.1016/s0021-9258(17)43827-0
发表时间：
1983-12
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Z. Grabarek;J. Grabarek;Paul C. LeavisS;J. Gergely
通讯作者：
Z. Grabarek;J. Grabarek;Paul C. LeavisS;J. Gergely
DOI：
--
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Schachat,FH;Bronson,DD;McDonald,OB
通讯作者：
McDonald,OB