Fig. 7. FXII interacts with uPAR through its FN2 and kringle domains.

a Computational model of the FXII-uPAR complex with magnified areas depicting the interaction of FXII’s fibronectin type II (FN2) and Kringle domains with uPAR domain 2 at multiple sites. b Representative immunoblots for FXII and uPAR from uPAR coimmunoprecipitation (IP, top) and immunoblots for uPAR, and α-Tubulin from the input (input, bottom) of HKC-8 cells exposed to purified human FXII (62 nM) in the presence of Zn²⁺ (10 µM) for 24 h with and without pretreatment with FXII sequential peptides (HR13, TY10 and PW15; 300 µM) for 1 h compared to control non-treated cells (C). Input serves as a loading control. Immunoblots represent 3 independent experiments. c Representative immunoblots (loading control: α-Tubulin) for γ-H2AX, p21, and KIM-1 expression in experimental groups (as described in b). Immunoblots represent 3 independent experiments. d Representative immunoblots for FXII and uPAR from uPAR coimmunoprecipitation (IP, top) and immunoblots for uPAR, and α-Tubulin from the input (input, bottom) of HKC-8 cells exposed to purified human FXII (62 nM) in the presence of Zn²⁺ (10 µM) for 24 h with and without pretreatment with uPAR based peptides (RL20, DL19, and DV20; 300 µM) for 1 h compared to control non-treated cells. Input serves as a loading control. Immunoblots represent 3 independent experiments. e Representative immunoblots (loading control: α-Tubulin) for γ-H2AX, p21, and KIM-1 expression in experimental groups (as described in d). Immunoblots represent 3 independent experiments.