{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPlasminogen (PLG) is a multifunctional circulating zymogen whose canonical role is in fibrinolysis. It circulates in a closed, activation‐resistant conformation maintained in part by its Pan–apple and serine protease domains, with its five kringle domains mediating critical ligand interactions with fibrin and various cell‐surface receptors. Binding to fibrin induces an open conformation that permits activation by tissue‐ or urokinase–type plasminogen activators, thereby generating plasmin to dissolve clots and remodel extracellular matrices. This finely tuned regulation is subject to modification—for example, glycation in diabetes alters lysine–binding interactions and impairs plasmin generation, and plasmin can even act as a backup protease (degrading substrates such as von Willebrand factor) when the primary regulators are deficient."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its role in hemostasis, numerous pathogens have evolved strategies to hijack the host PLG system in order to enhance tissue invasion and evade immune clearance. For instance, group A Streptococcus secretes streptokinase to convert PLG into plasmin, thereby dissolving local fibrin barriers and facilitating dissemination. Similarly, Streptococcus mutans and other oral streptococci bind PLG via surface‐associated glycolytic enzymes such as enolase. Fungal pathogens like Candida albicans, as well as bacteria including Borrelia recurrentis, non–typeable Haemophilus influenzae, Staphylococcus aureus, and even commensals such as bifidobacteria, express surface proteins that capture PLG; once activated, the resulting plasmin degrades matrix and complement proteins to promote invasion and immune evasion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its proteolytic functions, plasmin generated from PLG can modulate cellular signaling and influence disease susceptibility. In human monocytes, plasmin triggers proinflammatory signaling pathways—including the MAP kinase and JAK/STAT cascades—leading to expression of chemokines and co–stimulatory molecules. In parallel, plasmin has been shown to cleave extracellular protein aggregates such as α–synuclein, implicating the PLG system in neurodegenerative disease biology. Moreover, genetic analyses have uncovered pathogenic variants in PLG that are associated with atypical thrombotic microangiopathies, highlighting its role in the regulation of complement activity and vascular immunity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, the activation of PLG extends its impact to tissue remodeling, angiogenesis, and cancer progression. Plasmin–mediated cleavage of substrates such as the γ–subunit of epithelial sodium channels and collagen XVII not only contributes to extracellular matrix turnover and wound repair but can also give rise to potent antiangiogenic fragments (for example, the angiostatic kringle 5 domain). In the tumor microenvironment, overexpression of cell–surface PLG receptors facilitates localized plasmin generation, thereby promoting invasion and metastasis. Alterations in plasmin activity further influence vascular remodeling in pathologic states such as diabetic heart disease, giant cell arteritis, and chronic inflammatory conditions of the oral mucosa."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ruby H P Law, Tom Caradoc-Davies, Nathan Cowieson, et al. 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