Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 294, Issue 39, Pages 14267-14278Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.RA119.009825
Keywords
ATPase; myosin; cardiac muscle; skeletal muscle; computer modeling; ATP economy; developmental muscle; fast muscle; slow muscle; developmental myosin; adult skeletal myosin; cardiac myosin; ATPase
Categories
Funding
- National Institutes of Health [GM29090, HL117138]
- European Union Horizon 2020 Research and Innovation Programme [777204]
- MyoKardia, Inc
Ask authors/readers for more resources
Striated muscle myosins are encoded by a large gene family in all mammals, including humans. These isoforms define several of the key characteristics of the different striated muscle fiber types, including maximum shortening velocity. We have previously used recombinant isoforms of the motor domains of seven different human myosin isoforms to define the actin?myosin cross-bridge cycle in solution. Here, we present data on an eighth isoform, the perinatal, which has not previously been characterized. The perinatal is distinct from the embryonic isoform, appearing to have features in common with the adult fast-muscle isoforms, including weak affinity of ADP for actin?myosin and fast ADP release. We go on to use a recently developed modeling approach, MUSICO, to explore how well the experimentally defined cross-bridge cycles for each isoform in solution can predict the characteristics of muscle fiber contraction, including duty ratio, shortening velocity, ATP economy, and load dependence of these parameters. The work shows that the parameters of the cross-bridge cycle predict many of the major characteristics of each muscle fiber type and raises the question of what sequence changes are responsible for these characteristics.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available