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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 3. Force measurements in donor cardiomyocytes after exchange with recombinant troponin without PKA treatment.

Donor cardiomyocytes exchanged with 42D/44D, 23D/24D and Wt troponin complex (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) increased at 2.2 μm compared to 1.8 μm for all complexes, however, the difference was only significant in 23D/24D. Stretching of cardiomyocytes from 1.8 to 2.2 μm increased maximal (Fmax) and passive force (Fpas) in all groups. There was no significant effect of sarcomere length on nHill (steepness of the force-pCa curves). Compared to Wt, 42D/44D and 23D/24D significantly decreased Ca2+-sensitivity at both sarcomere lengths (#P<0.05). 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.

Without PKA Wt 42D/44D 23D/24D

Fmax (kN.m−2) 1.8 μm 12.4±0.5 10.3±1.9 11.7±1.1
2.2 μm 16.2±0.5* 16.3±0.8* 16.3±0.9*

Fpas (kN.m−2) 1.8 μm 2.2±0.3 2.1±0.5 2.9±0.3
2.2 μm 3.9±0.6* 3.0±0.7* 4.0±0.3*

pCa50 1.8 μm 5.55±0.05 5.26±0.01# 5.37±0.01#
2.2 μm 5.57±0.05 5.28±0.01# 5.46±0.01*,#

nHill 1.8 μm 1.9±0.1 2.0±0.2 2.0±0.1
2.2 μm 1.9±0.1 2.1±0.3 1.7±0.1