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. Author manuscript; available in PMC: 2015 Nov 1.
Published in final edited form as: J Thromb Haemost. 2014 Oct 11;12(11):1918–1920. doi: 10.1111/jth.12729

Fig. 1.

Fig. 1

A hypothetical model of sPLA2-V impairment of protein C activation. Functional EPCR contains a phosphatidylcholine (PC) in its hydrophobic groove. In this conformation, EPCR can bind protein C. Thrombin (T):thrombomodulin (TM) complex activates the protein C bound to EPCR to generate activated protein C (APC). Secreted phospholipase A2, group V (sPLA2-V) hydrolyses the PC in the EPCR to lyso PC. The lipid modification in the hydrophobic groove of EPCR leads to a structural rearrangement in the helical region of EPCR, which probably results in narrowing of the pocket of the ligand-binding groove. The structurally rearranged EPCR is unable to bind protein C. The loss of protein C binding to EPCR translates into impaired protein C activation by thrombin:thrombomodulin complex.