Piemonte (&) Molecular Medicine Unit, Children’s Hospital and Research Institute ‘‘Bambino Gesu`’’, P.za S. 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.ĬhiaraPassarelli and Stefania Petrini contributed equally to the work reported here.Ībbreviations GSH Reduced glutathione GSSG Oxidized glutathione GSPro Glutathionylated proteins ROS Reactive oxygen speciesĬ.
Myosin function is also sensitive to glutathionylation, which modulates its ATPase activity depending on GSSG redox balance. Glutathionylation of myosin has an important impact on the protein structure, as documented by the lowerįluorescence quantum yield of glutathionylated myosin and its increased susceptibility to the proteolytic cleavage.
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. Protein glutathionylation has a key role in redox regulation of proteins and signal transduction.
VALENTINA POSTERINO FREE
2008Ībstract 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. Received: 25 June 2008 / Accepted: 28 August 2008 / Published online: 9 September 2008 Ó Springer Science+Business Media B.V. Gaeta Æ Giulia Tozzi Æ Enrico Bertini Æ Monica Canepari Æ Rosetta Rossi Æ Fiorella Piemonte Myosin as a potential redox-sensor: an in vitro study Chiara Passarelli Æ Stefania Petrini Æ Anna Pastore Æ Valentina Bonetto Æ Patrizio Sale Æ Laura M.
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