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. Author manuscript; available in PMC: 2012 Apr 3.
Published in final edited form as: Circulation. 2011 Mar 14;123(12):1326–1334. doi: 10.1161/CIRCULATIONAHA.110.000885

Figure 1. Inhibition of fibrin-bound tPA activity by PN-1.

Figure 1

(A–B) tPA (2.5 nM) was bound to fibrin surfaces, and plasmin formation was recorded in absence or presence of recombinant PN-1 (10 nM), with the chromogenic substrate CBS0065. The curves represent the average of the raw data corresponding to the change in absorbance as a function of time in the absence and the presence of rPN-1. To simplify the plots, error standards are represented only every 20 or 40 min. (B) Rates of substrate hydrolysis were calculated from the initial velocity and compared to a plasmin standard curve. Data are representative of 3 different experiments, each performed in triplicate. *P < 0.05 significantly different from tPA alone. (C–D) Plasminogen activation by tPA was measured by fibrin-plasminogen-agar zymography after incubation of tPA with the supernatant from resting platelets or activated platelets by PAR1-AP or PAR4-AP as described in Methods. tPA was incubated (C) with human platelet secretion products in the presence or absence of an anti-PN-1 IgG, or (D) with platelet secretion products from WT and PN-1−/− mice. Data are representative of 5 separate experiments from different donors or mice.