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Plasminogen (PLG) is a 92-kDa protein consisting of 791 amino acids, including a serine protease region, five kringle domains, and an aminoterminal sequence [1]. Rich in the plasma component of blood, Plasminogen plays an essential role in degrading fibrin, collagen, and other structural components of tissues [3]. It is transformed into the enzyme plasmin, which degrades fibrin, on clot surfaces by tissue plasminogen activator (t-PA) and exhibits enhanced affinity for t-PA when bound to fibrin [2]. Plasminogen can interact with various ligands via lysine binding sites located in the five kringle domains at its N-terminus [4]. Apart from fibrin proteolysis, Plasmin also participates in cell migration, tissue remodeling, and inflammation [5]. Similar to Apo(a), plasminogen structural domains are also known as kringles, and both proteins have a serine‐proteinase region [6]. Plasminogen is activated upon its binding proteins exposing C-terminal basic residues on cell surfaces [7]. Pathogens bind plasminogen to their surface and activate plasmin to degrade the host extracellular matrix [8]. Additionally, pathogens including plasmodium, that express enolases, bind to plasminogen, facilitating pathogen adhesion and extracellular matrix degradation [9].
References:
[1] T. Dejouvencel, L. Doeuvre, R. Lacroix, P. Laurent, F. Dignat-George, H. Lijnenet al., "Fibrinolytic cross-talk: a new mechanism for plasmin formation", Blood, vol. 115, no. 10, p. 2048-2056, 2010. https://doi.org/10.1182/blood-2009-06-228817
[2] E. Nilebäck, F. Westberg, J. Deinum, & S. Svedhem, "Viscoelastic sensing of conformational changes in plasminogen induced upon binding of low molecular weight compounds", Analytical Chemistry, vol. 82, no. 20, p. 8374-8376, 2010. https://doi.org/10.1021/ac1016419
[3] J. Stie, G. Bruni, & D. Fox, "Surface-associated plasminogen binding of cryptococcus neoformans promotes extracellular matrix invasion", Plos One, vol. 4, no. 6, p. e5780, 2009. https://doi.org/10.1371/journal.pone.0005780
[4] M. Sanderson-Smith, M. Dowton, M. Ranson, & M. Walker, "The plasminogen-binding group a streptococcal m protein-related protein prp binds plasminogen via arginine and histidine residues", Journal of Bacteriology, vol. 189, no. 4, p. 1435-1440, 2007. https://doi.org/10.1128/jb.01218-06
[5] E. Plow, D. Freaney, J. Plescia, & L. Miles, "The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type.", The Journal of Cell Biology, vol. 103, no. 6, p. 2411-2420, 1986. https://doi.org/10.1083/jcb.103.6.2411
[6] E. Anglés-Cano, A. Díaz, & S. Loyau, "Inhibition of fibrinolysis by lipoprotein(a)", Annals of the New York Academy of Sciences, vol. 936, no. 1, p. 261-275, 2001. https://doi.org/10.1111/j.1749-6632.2001.tb03514.x
[7] N. Andronicos, E. Chen, N. Baik, H. Bai, C. Parmer, W. Kiosseset al., "Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, plg-rkt, a major regulator of cell surface plasminogen activation", Blood, vol. 115, no. 7, p. 1319-1330, 2010. https://doi.org/10.1182/blood-2008-11-188938
[8] S. Poltermann, A. Kunert, M. Heide, R. Eck, A. Hartmann, & P. Zipfel, "Gpm1p is a factor h-, fhl-1-, and plasminogen-binding surface protein of candida albicans", Journal of Biological Chemistry, vol. 282, no. 52, p. 37537-37544, 2007. https://doi.org/10.1074/jbc.m707280200
[9] A. Ghosh and M. Jacobs-Lorena, "Surface-expressed enolases of plasmodium and other pathogens", Memórias Do Instituto Oswaldo Cruz, vol. 106, no. suppl 1, p. 85-90, 2011. https://doi.org/10.1590/s0074-02762011000900011
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