ArticleNitric oxide : biology and chemistry2011
Cell surface thiol isomerases may explain the platelet-selective action of S-nitrosoglutathione.
Article in Nitric oxide : biology and chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Succination of Protein Disulfide Isomerase Links Mitochondrial Stress and Endoplasmic Reticulum Stress in the Adipocyte During Diabetes.Antioxidants & redox signaling · 2017Article
- Protein disulfide isomerase in thrombosis and vascular inflammation.Journal of thrombosis and haemostasis : JTH · 2013Review
- Inhibitory role of S-nitrosoglutathione in the aggregation of frozen platelets, and its effect on the expression of membrane glycoproteins.Experimental and therapeutic medicine · 2013Article
- S-nitrosothiols and the S-nitrosoproteome of the cardiovascular system.Antioxidants & redox signaling · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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 (csPDI) (EC 5.3.4.1). We have now compared csPDI expression and activity on platelets, endothelial cells and vascular smooth muscle cells, and the dependence on thiol reductase activity of these cell types for NO uptake from GSNO. csPDI expression was measured by flow cytometry and its reductase activity using the pseudosubstrate dieosin glutathione disulphide. This activity assay was adapted and validated for 96-well plate format. Flow cytometry revealed csPDI on all three cell types, but percentage positivity of expression was higher on platelets than on vascular cells. Consistent with this, thiol isomerase-related reductase activity was higher on platelets (P<0.01), and cellular activation (with either phorbol myristate acetate or ionomycin) increased csPDI activity on both platelets and smooth muscle cells, but not on endothelium. Intracellular NO delivery from GSNO was greater in platelets than in vascular cells (P<0.002), and was more sensitive to thiol isomerase inhibition using phenylarsine oxide (P<0.05). Increased surface thiol isomerase activity on platelets, compared with cells of the vascular wall, may explain the platelet-selective actions of GSNO and help define its antithrombotic potential.
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