dcm-related tropomyosin mutants e40ke54k over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridgesdcm-related原肌球蛋白突变体e40ke54k over-inhibit肌动球蛋白的相互作用,导致自行车横桥的数量减少.pdfVIP

DCM-Related Tropomyosin Mutants E40K/E54K Over- Inhibit the Actomyosin Interaction and Lead to a Decrease in the Number of Cycling Cross-Bridges Fan Bai, Heather L. Groth, Masataka Kawai* Departments of Anatomy and Cell Biology, and Internal Medicine, University of Iowa, Iowa City, Iowa, United States of America Abstract Two DCM mutants (E40K and E54K) of tropomyosin (Tm) were examined using the thin-filament extraction/reconstitu-tion technique. The effects of the Ca2+, ATP, phos-phate (Pi), and ADP concentrations on isometric tension and its transients were studied at 25uC, and the results were com-pared to those for the WT protein. Our results indicate that both E40K and E54K have a significantly lower T (high Ca2+ ten-sion at pCa 4.66) (E40K: 1.21 60.06 T , 6SEM, N = 34; E54K: 1.2460.07 T , HC a a N = 28), a significantly lower T (low- Ca2+ tension at pCa 7.0) (E40K: 0.07 60.02 T , N = 34; E54K: 0.06 60.02 T , N = 28), and a LC a a significantly lower T (Ca2+ activatable tension) (T = T –T E40K: 1.1560.08 T , N = 34; E54K: 1.18 60.06 T , N = 28) than act act HC LC, a a WT (T = 1.5360.07 T , T = 0.1260.01 T , T = 1.4060.07 T , N = 25). All tensions were normalized to T ( = 13.960.8 kPa, HC a LC a act a a N = 57), the ten-sion of actin-filament reconstituted cardiac fibers (myocardium) under the standard activating condit