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Tissue factor (TF) is the primary physiological initiator of the injury-induced blood coagulation cascade (Grover and Mackman, 2018). It is an integral transmembrane glycoprotein, with no intrinsic protease activity, that binds and allosterically activates clotting factor VII, which in turn cleaves and activates factor X or factor IX. TF is expressed by many cell types, including in the brain, lungs, heart, kidney, and subendothelial cells of the vasculature. Under normal circumstances, cells in contact with blood do not express physiologically active TF. However, when mechanical or chemical damage of the vascular wall occurs, subendothelial TF is exposed to blood flow and binds factor VII, leading to activation of the extrinsic coagulation cascade. Low levels of TF are found in the circulation, associated predominantly with extracellular vesicles (EV) (Grover and Mackman, 2018). Further, TF positive EV are elevated in a range of conditions, including diabetes, dyslipidaemia and various malignancies (Owens and Mackman, 2011). In terms of CKD, local dysregulated TF expression in the kidneys can also increase the risk of thrombosis and lead to chronic fibrin deposition (Grover and Mackman, 2018). TF is localized to both the glomerulus and kidney tubules during various inflammatory CKDs, such as glomerular and tubulointerstitial nephritis (Lwaleed and Bass, 2006; Moussa et al., 2007). In these conditions, elevated levels of TF can also be found in the urine and are associated with phospholipid vesicles that appear to originate from cells within the kidney itself, rather than the glomerular blood filtrate (Lwaleed et al., 1999). Some studies have suggested measuring urinary TF as a clinical biomarker for glomerulonephritis (Lwaleed et al., 1997, 1998).
To investigate whether other PAR members (1, 3, and 4) are capable of inducing synthesis of TF, we compared the effect on TF synthesis of an appropriate activating peptide specific for each receptor, PAR1, PAR2, PAR3, and PAR4. The PAR1-activating peptide TFLLRN-NH2 is reported not to cross-react with PAR2, like some other PAR-1 peptides, and unlike thrombin cannot elicit a PAR1-mediated transactivation of PAR2 (Blackhart et al., 1996). The PAR3 (TFRGAP-NH2) and PAR4 (GYPGKF-NH2) activating peptides (at 200 μM) failed to induce TF synthesis (n = 4, Figures 3A,B). Thus, only the peptide (2F) that activates PAR2 was capable of directly inducing TF synthesis.
Activation of PAR2 is intimately related to the coagulation cascade, and mice lacking the Par2/F2rl1 gene show reduced fibrin deposition in bleomycin-induced lung injury and glomerular nephritis (Moussa et al., 2007; Borensztajn et al., 2010; Bardou et al., 2016). Matriptase, a potent and highly specific PAR2-activating cell membrane-bound protease, has also been identified recently as a central coordinator of epithelial PAR2 activation, downstream of coagulation-related proteases TF-FVIIa and FXa (Le Gall et al., 2016). The specific roles for matriptase-PAR2 signaling in cellular mechanisms of physiology and disease, especially in the regulation of kidney hemostasis, remain unknown. As both trypsinogen and matriptase are expressed by kidney tubule cells, PAR2 may provide a molecular link between coagulation, epithelial proteases and kidney function (Koshikawa et al., 1998; Oberst et al., 2003).
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