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. 2004 Aug;263(1):73-80.
doi: 10.1023/B:MCBI.0000041849.60591.45.

Reduced cross-bridge dependent stiffness of skinned myocardium from mice lacking cardiac myosin binding protein-C

Bradley M Palmer  1 , Bradley K McConnell  2 , Guo Hua Li  2 , Christine E Seidman  1 , J G Seidman  1 , Thomas C Irving  3 , Norman R Alpert  1 , David W Maughan  1
Affiliations

Reduced cross-bridge dependent stiffness of skinned myocardium from mice lacking cardiac myosin binding protein-C

Bradley M Palmer et al. Mol Cell Biochem. 2004 Aug.

Abstract

The role of cardiac myosin binding protein-C (MyBP-C) on myocardial stiffness was examined in skinned papillary muscles of wild-type (WT(+/+)) and homozygous truncated cardiac MyBP-C (MyBP-C(t/t)) male mice. No MyBP-C was detected by gel electrophoresis or by Western blots in the MyBP-C(t/t) myocardium. Rigor-bridge dependent myofilament stiffness, i.e., rigor minus relaxed stiffness, in the MyBP-C(t/t) myocardium (281 ± 44 kN/m(2)) was 44% that in WT(+/+) (633 ± 141 kN/m(2)). The center-to-center spacing between thick filaments as determined by X-ray diffraction in MyBP-C(t/t) (45.0 ± 1.2 nm) was not significantly different from that in WT(+/+) (43.2 ± 0.9 nm). The fraction of cross-sectional area comprised of myofibrils, as determined by electron microscopy, was reduced in the MyBP-C(t/t) (39.9%) by 10% compared to WT(+/+) (44.5%). These data suggest that the 56% reduction in rigor-bridge dependent stiffness of the skinned MyBP-C(t/t) myocardium could not be due solely to a 10% reduction in the number of thick filaments per cross-sectional area and must also be due to approximately 50% reduction in the stiffness of the rigor-bridge attached thick filaments lacking MyBP-C. (Mol Cell Biochem 263: 73-80, 2004).

Keywords: C-protein; compliance; homozygous; isometric tension; truncated protein.

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