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. Author manuscript; available in PMC: 2015 Jul 15.
Published in final edited form as: Arch Biochem Biophys. 2014 May 9;554:11–21. doi: 10.1016/j.abb.2014.04.017

Table 4. Force measurements in donor cardiomyocytes after exchange with recombinant troponin and subsequent PKA treatment.

Donor cardiomyocytes exchanged with 42D/44D, 23D/24D and Wt troponin complex with PKA treatment (4–5 myocytes per complex). Myofilament force was measured at sarcomere lengths of 1.8 and 2.2 μm at different Ca2+-concentrations. Ca2+-sensitivity derived from the midpoint of the force–pCa relationship (pCa50) significantly increased at 2.2 μm compared to 1.8 μm for all complexes, however, significantly less in 42D/44D compared with Wt and 23D/24D. Stretching of cardiomyocytes from 1.8 to 2.2 μm increased maximal (Fmax) and passive force (Fpas) in all groups, without affecting nHill (steepness of the force-pCa curves). Compared to Wt, 42D/44D decreased Ca2+-sensitivity, reaching significance at sarcomere length 2.2 μm (#P<0.05). pCa50 of Wt did not significantly differ from 23D/24D after PKA treatment. No significant differences between the 3 cTn complexes for Fmax, Fpas and nHill were found. When two-way ANOVA revealed a significant effect for sarcomere length (P<0.05), paired t-tests were performed to compare cell measurements at two different sarcomere lengths in each cTn-exchange group (*P<0.05, 1.8 vs 2.2 μm). Wt and 23D/24D data have been published before.23 Values are means ± SEM.

With PKA Wt 42D/44D 23D/24D

Fmax (kN.m−2) 1.8 μm 12.8±1.1 12.5±1.2 11.1±1.9
2.2 μm 14.9±1.6* 16.3±0.7* 16.2±2.2*

Fpas (kN.m−2) 1.8 μm 2.0±0.2 2.1±0.2 2.6±0.1
2.2 μm 2.9±0.2* 3.3±0.5* 3.6±0.3*

pCa50 1.8 μm 5.34±0.06 5.25±0.01 5.37±0.01
2.2 μm 5.44±0.08* 5.28±0.01*,# 5.48±0.01*

nHill 1.8 μm 2.1±0.1 1.9±0.1 1.7±0.1
2.2 μm 2.1±0.1 1.9±0.3 1.7±0.2