Myosin Binding Protein C, a Phosphorylation-Dependent
Force Regulator in Muscle That Controls the Attachment of
Myosin Heads by Its Interaction With Myosin S2
by Gudrun Kunst, Kai R. Kress, Mathias Gruen, Dietmar Uttenweiler, Mathias Gautel,
and Rainer H. A. Fink
Circulation Research
Volume 86(1):51-58
January 7, 2000
Copyright © American Heart Association, Inc. All rights reserved.
A, Domain structure of cardiac MyBP-C.
Gudrun Kunst et al. Circ Res. 2000;86:51-58
Copyright © American Heart Association, Inc. All rights reserved.
A, Maximal Ca2+-activated isometric force (in the presence of 32 μmol/L Ca2+).
Gudrun Kunst et al. Circ Res. 2000;86:51-58
Copyright © American Heart Association, Inc. All rights reserved.
Maximal Ca2+-activated dynamic stiffness (per half-sarcomere; in the presence of 32 μmol/L
Ca2+) and rigor stiffness normalized to T0; comparison between unphosphorylated C1C2
fragment (C1C2, n=7) and the control (n=7).
Gudrun Kunst et al. Circ Res. 2000;86:51-58
Copyright © American Heart Association, Inc. All rights reserved.
Rigor kinetics.
Gudrun Kunst et al. Circ Res. 2000;86:51-58
Copyright © American Heart Association, Inc. All rights reserved.
pCa/force relations of unphosphorylated MyBP-C C1C2 fragment (A; C1C2, n=5) and
phosphorylated MyBP-C C1C2 fragment (B; C1C2-P, n=4) compared with the pCa/force relation
of the control (n=7). *P≤0.05 compared with control.
Gudrun Kunst et al. Circ Res. 2000;86:51-58
Copyright © American Heart Association, Inc. All rights reserved.