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Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit
Author(s) -
Percario Valentina,
Boncompagni Simona,
Protasi Feliciano,
Pertici Irene,
Pinzauti Francesca,
Caremani Marco
Publication year - 2018
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jp275404
Subject(s) - sarcomere , myosin , gene isoform , skeletal muscle , chemistry , biophysics , isometric exercise , soleus muscle , molecular motor , anatomy , biochemistry , biology , microbiology and biotechnology , myocyte , physiology , gene
Key points The different performance of slow and fast muscles is mainly attributed to diversity of the myosin heavy chain (MHC) isoform expressed within them. In this study fast sarcomere‐level mechanics has been applied to Ca 2+ ‐activated single permeabilised fibres isolated from soleus (containing the slow myosin isoform) and psoas (containing the fast myosin isoform) muscles of rabbit for a comparative definition of the mechano‐kinetics of force generation by slow and fast myosin isoforms in situ . The stiffness and the force of the slow myosin isoform are three times smaller than those of the fast isoform, suggesting that the stiffness of the myosin motor is a determinant of the isoform‐dependent functional diversity between skeletal muscles. These results open the question of the mechanism that can reconcile the reduced performance of the slow MHC with the higher efficiency of the slow muscle.Abstract The skeletal muscle exhibits large functional differences depending on the myosin heavy chain (MHC) isoform expressed in its molecular motor, myosin II. The differences in the mechanical features of force generation by myosin isoforms were investigated in situ by using fast sarcomere‐level mechanical methods in permeabilised fibres (sarcomere length 2.4 μm, temperature 12°C, 4% dextran T‐500) from slow (soleus, containing the MHC‐1 isoform) and fast (psoas, containing the MHC‐2X isoform) skeletal muscle of the rabbit. The stiffness of the half‐sarcomere was determined at the plateau of Ca 2+ ‐activated isometric contractions and in rigor and analysed with a model that accounted for the filament compliance to estimate the stiffness of the myosin motor (ε). ε was 0.56 ± 0.04 and 1.70 ± 0.37 pN nm −1 for the slow and fast isoform, respectively, while the average strain per attached motor ( s 0 ) was similar (∼3.3 nm) in both isoforms. Consequently the force per motor ( F 0 = ε s 0 ) was three times smaller in the slow isoform than in the fast isoform (1.89 ± 0.43 versus 5.35 ± 1.51 pN). The fraction of actin‐attached motors responsible for maximum isometric force at saturating Ca 2+ ( T 0,4.5 ) was 0.47 ± 0.09 in soleus fibres, 70% larger than that in psoas fibres (0.29 ± 0.08), so that F 0 in slow fibres was decreased by only 53%. The lower stiffness and force of the slow myosin isoform open the question of the molecular basis of the higher efficiency of slow muscle with respect to fast muscle.