Myosin as a potential redox-sensor: an in vitro study.

Abstract:

:A balanced redox status is necessary to optimize force production in contractile apparatus, where free radicals generated by skeletal muscle are involved in some basic physiological processes like excitation-contraction coupling. Protein glutathionylation has a key role in redox regulation of proteins and signal transduction. Here we show that myosin is sensitive to in vitro glutathionylation and MALDI-TOF analysis identified three potential sites of glutathione binding, two of them locating on the myosin head. Glutathionylation of myosin has an important impact on the protein structure, as documented by the lower fluorescence quantum yield of glutathionylated myosin and its increased susceptibility to the proteolytic cleavage. Myosin function is also sensitive to glutathionylation, which modulates its ATPase activity depending on GSSG redox balance. Thus, like the phosphorylation/dephosphorylation cycle, glutathionylation may represent a mechanism by which glutathione modulates sarcomere functions depending on the tissue redox state, and myosin may constitute a muscle redox-sensor.

authors

Passarelli C,Petrini S,Pastore A,Bonetto V,Sale P,Gaeta LM,Tozzi G,Bertini E,Canepari M,Rossi R,Piemonte F

doi

10.1007/s10974-008-9145-x

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

119-26

issue

2-5

eissn

0142-4319

issn

1573-2657

journal_volume

29

pub_type

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