Cargando…
Cell surface thiol isomerases may explain the platelet-selective action of S-nitrosoglutathione
S-nitrosoglutathione (GSNO) at low concentration inhibits platelet aggregation without causing vasodilation, suggesting platelet-selective nitric oxide delivery. The mechanism of this selectivity is unknown, but may involve cell surface thiol isomerases, in particular protein disulphide isomerase (c...
Autores principales: | Xiao, Fang, Gordge, Michael P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Academic Press
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3200429/ https://www.ncbi.nlm.nih.gov/pubmed/21642008 http://dx.doi.org/10.1016/j.niox.2011.05.008 |
Ejemplares similares
-
The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function
por: Holbrook, L-M, et al.
Publicado: (2012) -
The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione
por: Truzzi, Daniela R., et al.
Publicado: (2020) -
Evidence for an Allosteric S-Nitrosoglutathione Binding Site in S-Nitrosoglutathione Reductase (GSNOR)
por: Fontana, Kathleen, et al.
Publicado: (2019) -
Plasmin-Induced Activation of Human Platelets Is Modulated by Thrombospondin-1, Bona Fide Misfolded Proteins and Thiol Isomerases
por: Pielsticker, Claudia, et al.
Publicado: (2020) -
Pathophysiological Role of S-Nitrosylation and Transnitrosylation Depending on S-Nitrosoglutathione Levels Regulated by S-Nitrosoglutathione Reductase
por: Choi, Min Sik
Publicado: (2018)