Author
Listed:
- Alicia M Evangelista
- Vijay S Rao
- Ashley R Filo
- Nadzeya V Marozkina
- Allan Doctor
- David R Jones
- Benjamin Gaston
- William H Guilford
Abstract
Background: Nitric oxide (NO) has long been recognized to affect muscle contraction [1], both through activation of guanylyl cyclase and through modification of cysteines in proteins to yield S-nitrosothiols. While NO affects the contractile apparatus directly, the identities of the target myofibrillar proteins remain unknown. Here we report that nitrogen oxides directly regulate striated muscle myosins. Principal Findings: Exposure of skeletal and cardiac myosins to physiological concentrations of nitrogen oxides, including the endogenous nitrosothiol S-nitroso-L-cysteine, reduced the velocity of actin filaments over myosin in a dose-dependent and oxygen-dependent manner, caused a doubling of force as measured in a laser trap transducer, and caused S-nitrosylation of cysteines in the myosin heavy chain. These biomechanical effects were not observed in response to S-nitroso-D-cysteine, demonstrating specificity for the naturally occurring isomer. Both myosin heavy chain isoforms in rats and cardiac myosin heavy chain from human were S-nitrosylated in vivo. Significance: These data show that nitrosylation signaling acts as a molecular “gear shift” for myosin—an altogether novel mechanism by which striated muscle and cellular biomechanics may be regulated.
Suggested Citation
Alicia M Evangelista & Vijay S Rao & Ashley R Filo & Nadzeya V Marozkina & Allan Doctor & David R Jones & Benjamin Gaston & William H Guilford, 2010.
"Direct Regulation of Striated Muscle Myosins by Nitric Oxide and Endogenous Nitrosothiols,"
PLOS ONE, Public Library of Science, vol. 5(6), pages 1-7, June.
Handle:
RePEc:plo:pone00:0011209
DOI: 10.1371/journal.pone.0011209
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