Published: 23 June, 2017 | Volume 2 - Issue 1 | Pages: 029-034
Figure 1:
Fibrinolysis is initiated when tPA released from the vessel wall binds to its binding site on the D-domain of intact fibrin and activates plasminogen bound to an adjacent site. This ternary complex with fibrin promotes tPA plasminogen activation by about 1,000-fold. Fibrin degradation creates two new plasminogen binding sites on the fibrin E-domain. The fi rst of these is a triple carboxyl lysine binding site which induces a unique conformational
change in plasminogen that enables the intrinsic activity of proUK to activate it. This is accompanied by reciprocal activation of proUK to UK which activates the remaining plasminogen completing fibrinolysis.
Read Full Article HTML DOI: 10.29328/journal.jccm.1001010 Cite this Article Read Full Article PDF
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