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Protein tyrosine nitration in the ventilatory muscles: role of nitric oxide synthases.
Am J Respir Cell Mol Biol. 2002 Apr; 26(4):438-46.AJ

Abstract

Modification of tyrosine residues and formation of 3-nitrotyrosine is one of the most commonly identified effects of reactive nitrogen species on proteins. In this study we evaluated the presence and localization of tyrosine nitration in various ventilatory and limb muscles. We also assessed the contribution of the neuronal (nNOS), the endothelial (eNOS), and the inducible (iNOS) isoforms of nitric oxide synthase (NOS) to tyrosine nitration in skeletal muscles both under normal conditions and in response to severe sepsis. In normal rats and mice, muscle tyrosine nitration was detected at 52, 48, 40, 30, 18, and 10 kD protein bands. Tyrosine nitration of the majority of these protein bands was significantly reduced within 1 h of in vivo NOS inhibition in rats. Diaphragmatic protein tyrosine nitration in mice deficient in the inducible NOS (iNOS-/-) averaged ~ 50% of that detected in wild-type (iNOS+/+) mice. Injection of bacterial lipopolysaccharides (LPS) in rats produced a significant rise in protein tyrosine nitration in the mitochondrial and membrane fractions but not in the cytosol of ventilatory muscles. Absence of iNOS expression (iNOS-/-), but not nNOS (nNOS-/-) or eNOS (eNOS-/-), in genetically altered mice resulted in a significant reduction in LPS-mediated rise in diaphragmatic nitrotyrosine. We conclude that tyrosine nitration of proteins occurs in normal muscle fibers and is dependent mainly on the activity of the iNOS isoform. Sepsis-mediated increase in protein tyrosine nitration is limited to the mitochondria and cell membrane and is highly dependent on the activity of the iNOS but not the nNOS or eNOS isoforms.

Authors+Show Affiliations

Critical Care Division, Royal Victoria Hospital and Meakins-Christie Laboratories, McGill University, Montreal, Quebec, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11919080

Citation

Barreiro, Esther, et al. "Protein Tyrosine Nitration in the Ventilatory Muscles: Role of Nitric Oxide Synthases." American Journal of Respiratory Cell and Molecular Biology, vol. 26, no. 4, 2002, pp. 438-46.
Barreiro E, Comtois AS, Gea J, et al. Protein tyrosine nitration in the ventilatory muscles: role of nitric oxide synthases. Am J Respir Cell Mol Biol. 2002;26(4):438-46.
Barreiro, E., Comtois, A. S., Gea, J., Laubach, V. E., & Hussain, S. N. (2002). Protein tyrosine nitration in the ventilatory muscles: role of nitric oxide synthases. American Journal of Respiratory Cell and Molecular Biology, 26(4), 438-46.
Barreiro E, et al. Protein Tyrosine Nitration in the Ventilatory Muscles: Role of Nitric Oxide Synthases. Am J Respir Cell Mol Biol. 2002;26(4):438-46. PubMed PMID: 11919080.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein tyrosine nitration in the ventilatory muscles: role of nitric oxide synthases. AU - Barreiro,Esther, AU - Comtois,Alain S, AU - Gea,Joaquin, AU - Laubach,Victor E, AU - Hussain,Sabah N A, PY - 2002/3/29/pubmed PY - 2002/5/1/medline PY - 2002/3/29/entrez SP - 438 EP - 46 JF - American journal of respiratory cell and molecular biology JO - Am J Respir Cell Mol Biol VL - 26 IS - 4 N2 - Modification of tyrosine residues and formation of 3-nitrotyrosine is one of the most commonly identified effects of reactive nitrogen species on proteins. In this study we evaluated the presence and localization of tyrosine nitration in various ventilatory and limb muscles. We also assessed the contribution of the neuronal (nNOS), the endothelial (eNOS), and the inducible (iNOS) isoforms of nitric oxide synthase (NOS) to tyrosine nitration in skeletal muscles both under normal conditions and in response to severe sepsis. In normal rats and mice, muscle tyrosine nitration was detected at 52, 48, 40, 30, 18, and 10 kD protein bands. Tyrosine nitration of the majority of these protein bands was significantly reduced within 1 h of in vivo NOS inhibition in rats. Diaphragmatic protein tyrosine nitration in mice deficient in the inducible NOS (iNOS-/-) averaged ~ 50% of that detected in wild-type (iNOS+/+) mice. Injection of bacterial lipopolysaccharides (LPS) in rats produced a significant rise in protein tyrosine nitration in the mitochondrial and membrane fractions but not in the cytosol of ventilatory muscles. Absence of iNOS expression (iNOS-/-), but not nNOS (nNOS-/-) or eNOS (eNOS-/-), in genetically altered mice resulted in a significant reduction in LPS-mediated rise in diaphragmatic nitrotyrosine. We conclude that tyrosine nitration of proteins occurs in normal muscle fibers and is dependent mainly on the activity of the iNOS isoform. Sepsis-mediated increase in protein tyrosine nitration is limited to the mitochondria and cell membrane and is highly dependent on the activity of the iNOS but not the nNOS or eNOS isoforms. SN - 1044-1549 UR - https://www.unboundmedicine.com/medline/citation/11919080/Protein_tyrosine_nitration_in_the_ventilatory_muscles:_role_of_nitric_oxide_synthases_ L2 - https://www.atsjournals.org/doi/10.1165/ajrcmb.26.4.4634?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -