ArticleBlood2010
Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its de-encryption.
Article in Blood, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Protein disulfide isomerase inhibition blocks thrombin generation in humans by interfering with platelet factor V activation.JCI insight · 2017Trial
- ERO1-PDI Redox Signaling in Health and Disease.Antioxidants & redox signaling · 2021Review
- Murine tissue factor disulfide mutation causes a bleeding phenotype with sex specific organ pathology and lethality.Haematologica · 2020Article
- Protein disulfide isomerase in cardiovascular disease.Experimental & molecular medicine · 2020Review
- Direct Amplification of Tissue Factor:Factor VIIa Procoagulant Activity by Bile Acids Drives Intrahepatic Coagulation.Arteriosclerosis, thrombosis, and vascular biology · 2019Article
- Increasing the sensitivity of the human microvesicle tissue factor activity assay.Thrombosis research · 2019Article
- Role of Cell Surface Lipids and Thiol-Disulphide Exchange Pathways in Regulating the Encryption and Decryption of Tissue Factor.Thrombosis and haemostasis · 2019Review
- Protein disulfide isomerase enhances tissue factor-dependent thrombin generation.Biochemical and biophysical research communications · 2018Article
- The intersection of protein disulfide isomerase and cancer associated thrombosis.Thrombosis research · 2018Review
- Tissue Factor Prothrombotic Activity Is Regulated by Integrin-arf6 Trafficking.Arteriosclerosis, thrombosis, and vascular biology · 2017Article
- The Role of Putative Phosphatidylserine-Interactive Residues of Tissue Factor on Its Coagulant Activity at the Cell Surface.PloS one · 2016Article
- Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.Arteriosclerosis, thrombosis, and vascular biology · 2015Review
- Synergies of phosphatidylserine and protein disulfide isomerase in tissue factor activation.Thrombosis and haemostasis · 2014Review
- Role of tissue factor in Mycobacterium tuberculosis-induced inflammation and disease pathogenesis.PloS one · 2014Article
- Article
- Protein disulfide isomerase in thrombosis and vascular inflammation.Journal of thrombosis and haemostasis : JTH · 2013Review
- Analysis of tissue factor expression in various cell model systems: cryptic vs. active.Journal of thrombosis and haemostasis : JTH · 2013Article
- Disulfide reduction abolishes tissue factor cofactor function.Biochimica et biophysica acta · 2013Article
- Article
- Thioredoxin and thioredoxin reductase control tissue factor activity by thiol redox-dependent mechanism.The Journal of biological chemistry · 2013Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Tissue factor (TF) on cell surfaces resides mostly in a cryptic state. It is not entirely clear how cryptic TF differs from procoagulantly active TF and how deencryption occurs. Here, we critically evaluated the importance of cystine 186-cystine 209 (Cys186-Cys209) bond formation for TF procoagulant activity and its de-encryption. Chinese hamster ovary cells transfected with TF(C186S), TF(C209S), or TF(C186S/C209S) expressed little procoagulant activity at the cell surface. TF monoclonal antibody and activated factor VII (FVIIa) binding studies showed that little TF protein was present at the cell surface in cells expressing mutant TF. Similar data were obtained in human umbilical vein endothelial cells (HUVECs) transduced to express TF(C186S), TF(C209S), or TF(C186S/C209S). Analysis of TF activity in HUVECs expressing similar levels of wild-type TF and TF(C186S/C209S) showed that TF mutant in the presence of saturating concentrations of FVIIa exhibited similar coagulant activity as that of wild-type TF. More importantly, treatment of HUVECs expressing TF(C186S/C209S) with HgCl(2) or ionomycin increased the cell-surface TF activity to the same extent as that of the wild-type TF. Our data provide clear evidence that TF lacking the Cys186-Cys209 bond is coagulantly active once it is complexed with FVIIa, and TF de-encryption does not require Cys186-Cys209 disulfide bond formation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.