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S360A-activated protein C (S360A-APC) is a **recombinant, catalytically inactive variant** of activated protein C (APC). The S360A mutation eliminates the protease activity of activated protein C but preserves its ability to bind important biological receptors, such as endothelial protein C receptor (EPCR). This variant acts as a non-proteolytic anticoagulant by **inhibiting the activation of factor Va (FVa) and factor VIIIa (FVIIIa) via competitive binding**, down-regulating the generation of factor Xa (FXa) and thrombin, but without directly cleaving them. Additionally, S360A-APC maintains the **cytoprotective and anti-inflammatory signaling** properties of wild-type APC, especially through shifting thrombin-PAR1 signaling from pro-inflammatory to anti-inflammatory outcomes when bound to EPCR. Preclinical studies have demonstrated its ability to reduce myocardial infarct size and modulate inflammation with a **lower risk of bleeding** due to its lack of proteolytic activity[1][3][4][13]. The molecule has been investigated as a pharmacological tool and as a potential therapeutic in models of ischemia/reperfusion injury and chronic inflammation.
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