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Details on Person Western blotting and mass spectrometry analyses revealed tha...
| Class:Id | Summation:9655838 |
|---|---|
| _displayName | Western blotting and mass spectrometry analyses revealed tha... |
| _timestamp | 2025-01-13 18:10:07 |
| created | [InstanceEdit:9655846] Shamovsky, Veronica, 2019-07-26 |
| literatureReference | [LiteratureReference:9655861] Endothelial PAI-1 (Plasminogen Activator Inhibitor-1) Blocks the Intrinsic Pathway of Coagulation, Inducing the Clearance and Degradation of FXIa (Activated Factor XI) [LiteratureReference:9655859] Plasminogen activator inhibitor (PAI-1) in plasma and platelets [LiteratureReference:9655853] Platelets retain high levels of active plasminogen activator inhibitor 1 [LiteratureReference:9655856] Interaction of type 1 plasminogen activator inhibitor with the enzymes of the contact activation system [LiteratureReference:9655867] Platelets synthesize large amounts of active plasminogen activator inhibitor 1 |
| modified | [InstanceEdit:9674480] Shamovsky, Veronica, 2020-01-13 [InstanceEdit:9769725] Shamovsky, Veronica, 2022-03-22 [InstanceEdit:9935196] Shamovsky, Veronica, 2025-01-13 |
| text | Western blotting and mass spectrometry analyses revealed that FXIa forms a complex with endothelial plasminogen activator inhibitor-1 (PAI-1 or SERPINE1), which is either released from activated platelets or present in the extracellular environment of endothelial cells (ECs) and their surrounding matrix (Booth NA et al., 1988; Brogren H et al., 2004, 2011; Puy C et al., 2019). Immunoblotting confirmed that SERPINE1 interacts with FXIa and neutralizes its activity in a purified system (Berrettini M et al., 1989). Blocking endothelial SERPINE1 increased FXIa-mediated cleavage of a chromogenic substrate and enhanced the ability of FXIa to promote fibrin formation in plasma (Puy C et al., 2019). Western blot and immunofluorescence analyses further demonstrated that FXIa:SERPINE1 complexes are either released into the media or trafficked to early and late endosomes, as well as lysosomes, within human umbilical vein endothelial cells (HUVEC) (Puy C et al., 2019). Additionally, circulating FXIa:SERPINE1 complexes were detected using ELISA in a baboon model of Staphylococcus aureus sepsis (Puy C et al., 2019). These findings suggest that SERPINE1 forms a complex with FXIa on ECs, inhibiting its activity while promoting the clearance and degradation of FXIa. |
| (summation) | [Reaction:9655851] factor XIa binds SERPINE1 [Homo sapiens] |
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