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. 2017 Dec 5;9(12):392. doi: 10.3390/toxins9120392

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© 2017 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Schematic representation of the plasminogen/fibrinolytic system. Local effects of plasminogen activators (PAs) (physiological and snake venom PAs) and direct-acting fibrinolytic agents. PAs convert plasminogen to active enzyme plasmin, which degrades fibrin. In parallel using fibrin as substrate, direct-acting P-I SVMPs or endogenous plasmin proteolytically degrade fibrin and dissolve the fibrin clot. Inhibition (indicated by dotted lines) occurs either (i) at the level of PAs by plasminogen activator inhibitor (mainly by PAI-1 and PAI-2) or (ii) by plasmin inhibitors (by α2-antiplasmin and α2-macroglobulin). Matrix metalloproteinases (MMPs) degrade fibrin into smaller fragments, termed fibrin degradation products (FDP), and are inhibited by tissue inhibitor of MMPs (TIMPs). Snake venom serine proteinases, PAs (TSV-PA, LV-PA and Haly-PA [62]) and the direct-acting fibrinolytic metalloproteinases (bar-I, leuc-a, alfimeprase and mut-II), are shown at their site of inhibition.