Krüppel‐like factor 10 regulates the contractile properties of skeletal muscle fibers in mice

2021 ◽  
Author(s):  
Malek Kammoun ◽  
Philippe Pouletaut ◽  
Sandrine Morandat ◽  
Malayannan Subramaniam ◽  
John R. Hawse ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Contractile Properties ◽  
Skeletal Muscle Fibers

Assessment of the Contractile Properties of Permeabilized Skeletal Muscle Fibers

2016 ◽  
pp. 321-336 ◽  
Author(s):  
Dennis R. Claflin ◽  
Stuart M. Roche ◽  
Jonathan P. Gumucio ◽  
Christopher L. Mendias ◽  
Susan V. Brooks
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Contractile Properties ◽  
Skeletal Muscle Fibers

scholarly journals Coupled expression of troponin T and troponin I isoforms in single skeletal muscle fibers correlates with contractility

2006 ◽  
Vol 290 (2) ◽  
pp. C567-C576 ◽  
Author(s):  
Marco A. Brotto ◽  
Brandon J. Biesiadecki ◽  
Leticia S. Brotto ◽  
Thomas M. Nosek ◽  
Jian-Ping Jin
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin T ◽  
Muscle Fibers ◽  
Contractile Properties ◽  
Type I ◽  
Myosin Isoforms ◽  
Mammalian Skeletal Muscle ◽  
Single Fibers ◽  
Skeletal Muscle Fibers

Striated muscle contraction is powered by actin-activated myosin ATPase. This process is regulated by Ca2+ via the troponin complex. Slow- and fast-twitch fibers of vertebrate skeletal muscle express type I and type II myosin, respectively, and these myosin isoenzymes confer different ATPase activities, contractile velocities, and force. Skeletal muscle troponin has also diverged into fast and slow isoforms, but their functional significance is not fully understood. To investigate the expression of troponin isoforms in mammalian skeletal muscle and their functional relationship to that of the myosin isoforms, we concomitantly studied myosin, troponin T (TnT), and troponin I (TnI) isoform contents and isometric contractile properties in single fibers of rat skeletal muscle. We characterized a large number of Triton X-100-skinned single fibers from soleus, diaphragm, gastrocnemius, and extensor digitorum longus muscles and selected fibers with combinations of a single myosin isoform and a single class (slow or fast) of the TnT and TnI isoforms to investigate their role in determining contractility. Types IIa, IIx, and IIb myosin fibers produced higher isometric force than that of type I fibers. Despite the polyploidy of adult skeletal muscle fibers, the expression of fast or slow isoforms of TnT and TnI is tightly coupled. Fibers containing slow troponin had higher Ca2+ sensitivity than that of the fast troponin fibers, whereas fibers containing fast troponin showed a higher cooperativity of Ca2+ activation than that of the slow troponin fibers. These results demonstrate distinct but coordinated regulation of troponin and myosin isoform expression in skeletal muscle and their contribution to the contractile properties of muscle.

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