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Plasmin: Wikis


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PDB rendering based on 1b2i.
Available structures
1b2i, 1bml, 1bui, 1cea, 1ceb, 1ddj, 1hpj, 1hpk, 1i5k, 1ki0, 1krn, 1l4d, 1l4z, 1pk4, 1pkr, 1pmk, 1qrz, 1rjx, 2doh, 2doi, 2pk4, 5hpg
Symbols PLG; DKFZp779M0222
External IDs OMIM173350 MGI97620 HomoloGene55452 GeneCards: PLG Gene
EC number
RNA expression pattern
PBB GE PLG 209978 s at tn.png
PBB GE PLG 209977 at tn.png
PBB GE PLG 205871 at tn.png
More reference expression data
Species Human Mouse
Entrez 5340 18815
Ensembl ENSG00000122194 ENSMUSG00000059481
UniProt P00747 Q3V1T9
RefSeq (mRNA) NM_000301 NM_008877
RefSeq (protein) NP_000292 NP_032903
Location (UCSC) Chr 6:
161.04 - 161.09 Mb
Chr 17:
12.22 - 12.26 Mb
PubMed search [1] [2]

Plasmin is an important enzyme (EC present in blood that degrades many blood plasma proteins, most notably, fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein is encoded by the PLG gene.[1]



Plasminogen (PLG) is a circulating zymogen that is converted to the active enzyme plasmin by cleavage of the peptide bond between Arg-560 and Val-561, which is mediated by urokinase and tissue plasminogen activator. The main function of plasmin is to dissolve fibrin blood clots. Plasmin, like trypsin, belongs to the family of serine proteases.[1][2][3]

Plasmin is a serine protease that is released as plasminogen from the liver into the circulation and activated by tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), and factor XII (Hageman factor). Fibrin is a cofactor for plasminogen activation by tissue plasminogen activator. Urokinase plasminogen activator receptor (uPAR) is a cofactor for plasminogen activation by urokinase plasminogen activator. Plasmin is inactivated by alpha 2-antiplasmin, a serine protease inhibitor (serpin).

Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: It activates collagenases, some mediators of the complement system and weakens the wall of the Graafian follicle (leading to ovulation). It cleaves fibrin, fibronectin, thrombospondin, laminin, and von Willebrand factor.

Apart from fibrinolysis, plasminogen is shown to play important role in wound healing, liver repair as well as the maintenance of liver homeostasis.

Plasmin cleavage produces angiostatin.

Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.


Deficiency in plasmin may lead to thrombosis, as clots are not degraded adequately. Plasminogen deficiency in mice leads to defective wound healing, defective liver repair, reproductive abnormalities.

In human, a rare disorder called plasminogen deficiency type I (OMIM 217090) is caused by mutations of the PLG gene and is often manifested by ligneous conjunctivitis.


Plasmin has been shown to interact with Thrombospondin 1,[4][5] Alpha 2-antiplasmin[6][7] and IGFBP3.[8]


  1. ^ a b "Entrez Gene: plasminogen".  
  2. ^ Miyata T, Iwanaga S, Sakata Y, Aoki N (October 1982). "Plasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site". Proc. Natl. Acad. Sci. U.S.A. 79 (20): 6132–6. doi:10.1073/pnas.79.20.6132. PMID 6216475. PMC 347073.  
  3. ^ Forsgren M, Råden B, Israelsson M, Larsson K, Hedén LO (March 1987). "Molecular cloning and characterization of a full-length cDNA clone for human plasminogen". FEBS Lett. 213 (2): 254–60. doi:10.1016/0014-5793(87)81501-6.  
  4. ^ Silverstein, R L; Leung L L, Harpel P C, Nachman R L (Nov. 1984). "Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator". J. Clin. Invest. (UNITED STATES) 74 (5): 1625–33. doi:10.1172/JCI111578. ISSN 0021-9738. PMID 6438154.  
  5. ^ DePoli, P; Bacon-Baguley T, Kendra-Franczak S, Cederholm M T, Walz D A (Mar. 1989). "Thrombospondin interaction with plasminogen. Evidence for binding to a specific region of the kringle structure of plasminogen". Blood (UNITED STATES) 73 (4): 976–82. ISSN 0006-4971. PMID 2522013.  
  6. ^ Wiman, B; Collen D (Sep. 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". J. Biol. Chem. (UNITED STATES) 254 (18): 9291–7. ISSN 0021-9258. PMID 158022.  
  7. ^ Shieh, B H; Travis J (May. 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. (UNITED STATES) 262 (13): 6055–9. ISSN 0021-9258. PMID 2437112.  
  8. ^ Campbell, P G; Durham S K, Suwanichkul A, Hayes J D, Powell D R (Aug. 1998). "Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3". Am. J. Physiol. (UNITED STATES) 275 (2 Pt 1): E321-31. ISSN 0002-9513. PMID 9688635.  

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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