title: [Tyrosine nitration as regulatory post-translational modification of proteins].
abstract: Review highlights new pathways of signal transduction from nitric oxide (NO) that is a recognized secondary messenger in regulatory cascades of phylogenetically distant species. Indirect (via Ca2+ and cGMP) and direct (protein S-nitrosylation and tyrosine nitration) pathways of NO signal transduction are presented. S-nitrosyation as new paradigm in signal transduction and protein functions regulations is discussed. The importance of animal and plant protein tyrosine nitration in vivo and the potential regulatory significance of this posttranslational modification are emphasized. Also review describes tree mechanisms of protein tyrosine nitration: via peroxynitrite, peroxydase and haem-peroxidase. Particular attention is paid to cytoskeleton proteins tyrosine nitration, particularly tubulines, because microtubules are involved into modulation of signal transduction from various messengers.
authors.forename: Ia B
authors.initials: IaB
authors.lastname: Blium
authors.forename: Iu A
authors.initials: IuA
authors.lastname: Krasylenko
authors.forename: A I
authors.initials: AI
authors.lastname: Iemets'
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D006152:Cyclic GMP / Q000378:metabolism; D006801:Humans; D009569:Nitric Oxide / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D009569:Nitric Oxide; D014443:Tyrosine; D006152:Cyclic GMP; D002118:Calcium