Nitric oxide (NO•) is synthesized in skeletal muscle and its production increases during contractile activity. Although myosin is the most abundant protein in muscle, it is not known whether myosin is a target of NO• or NO• derivatives. In the present study, we have shown that exercise increases protein S-nitrosylation in muscle, and, among contractile proteins, myosin is the principal target of exogenous SNOs (S-nitrosothiols) in both skinned skeletal muscle fibres and differentiated myotubes. The reaction of isolated myosin with S-nitrosoglutathione results in S-nitrosylation at multiple cysteine thiols and produces two populations of protein-bound SNOs with different stabilities. The less-stable population inhibits the physiological ATPase activity, without affecting the affinity of myosin for actin. However, myosin is neither inhibited nor S-nitrosylated by the NO• donor diethylamine NONOate, indicating a requirement for transnitrosylation between low-mass SNO and myosin cysteine thiols rather than a direct reaction of myosin with NO• or its auto-oxidation products. Interestingly, alkylation of the most reactive thiols of myosin by N-ethylmaleimide does not inhibit formation of a stable population of protein-SNOs, suggesting that these sites are located in less accessible regions of the protein than those that affect activity. The present study reveals a new link between exercise and S-nitrosylation of skeletal muscle contractile proteins that may be important under (patho)physiological conditions.
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Research Article|
November 11 2009
Myosin is reversibly inhibited by S-nitrosylation Available to Purchase
Leonardo Nogueira;
*Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, RJ 21941-590, Brazil
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Cicero Figueiredo-Freitas;
Cicero Figueiredo-Freitas
2
*Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, RJ 21941-590, Brazil
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Gustavo Casimiro-Lopes;
Gustavo Casimiro-Lopes
*Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, RJ 21941-590, Brazil
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Margaret H. Magdesian;
Margaret H. Magdesian
*Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, RJ 21941-590, Brazil
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Jamil Assreuy;
Jamil Assreuy
†Departamento de Farmacologia, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, SC 88015-420, Brazil
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Martha M. Sorenson
Martha M. Sorenson
3
*Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, RJ 21941-590, Brazil
3To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
July 30 2009
Revision Received:
September 03 2009
Accepted:
September 11 2009
Accepted Manuscript online:
September 11 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 424 (2): 221–231.
Article history
Received:
July 30 2009
Revision Received:
September 03 2009
Accepted:
September 11 2009
Accepted Manuscript online:
September 11 2009
Citation
Leonardo Nogueira, Cicero Figueiredo-Freitas, Gustavo Casimiro-Lopes, Margaret H. Magdesian, Jamil Assreuy, Martha M. Sorenson; Myosin is reversibly inhibited by S-nitrosylation. Biochem J 1 December 2009; 424 (2): 221–231. doi: https://doi.org/10.1042/BJ20091144
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