My watch list
my.chemeurope.com  

my.chemeurope.com

With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.

  • My watch list
  • My saved searches
  • My saved topics
  • My newsletter
Register free of charge
Login  
eng  
DeutschEnglishFrançaisEspañol

Plasmin



Plasminogen
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
Identifiers
Symbol(s) PLG; DKFZp779M0222
External IDs OMIM: 173350 MGI: 97620 Homologene: 55452
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5340 18815
Ensembl ENSG00000122194 ENSMUSG00000059481
Uniprot P00747 Q3V1T9
Refseq NM_000301 (mRNA)
NP_000292 (protein) 		NM_008877 (mRNA)
NP_032903 (protein)
Location Chr 6: 161.04 - 161.09 Mb Chr 17: 12.22 - 12.26 Mb
Pubmed search [1] [2]
Plasmin is an important enzyme (EC 3.4.21.7) present in blood that degrades many blood plasma proteins, most notably fibrin clots. The degradation of fibrin is termed fibrinolysis.

Functions

It is a serine protease that is released as plasminogen into the circulation and activated by tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), thrombin, fibrin and factor XII (Hageman factor). It is inactived 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.



Pathology

Deficiency in plasmin may lead to thrombosis, as clots are not degraded adequately.

Further reading

  • Anglés-Cano E, Rojas G (2003). "Apolipoprotein(a): structure-function relationship at the lysine-binding site and plasminogen activator cleavage site.". Biol. Chem. 383 (1): 93-9. PMID 11928826.
  • Ranson M, Andronicos NM (2004). "Plasminogen binding and cancer: promises and pitfalls.". Front. Biosci. 8: s294-304. PMID 12700073.
v • d • e
Proteins: coagulation
Coagulation factorsintrinsic pathway (FXII, FXI, FIX, FVIII) - extrinsic pathway (Tissue factor, FVII) - common pathway (FX, FV, (Pro)thrombin / FII, Fibrin / FI, FXIII) - HMWK - vWF - Kallikrein
InhibitorsAntithrombin - Protein C - Protein S - Protein Z - ZPI - TFPI
FibrinolysisPlasmin - tPA/urokinase - PAI-1/2 - α2-AP - α2-macroglobulin - TAFI
v • d • e
Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive systemEnteropeptidase - Trypsin - Chymotrypsin - Elastase (Neutrophil, Pancreatic)
Complement systemFactor B - Factor D - Factor I - MASP (MASP1, MASP2) - C3-convertase
Coagulationfactors: Thrombin - Factor VIIa - Factor IXa - Factor Xa - Factor XIa - Factor XIIa - Kallikrein (PSA)
fibrinolysis: Plasmin - Tissue plasminogen activator - Urinary plasminogen activator
Immune systemChymase - Granzyme - Tryptase - Proteinase 3/Myeloblastin
VenombinAncrod - Batroxobin
OtherAcrosin - Prolyl endopeptidase - Pronase - Proprotein convertases (1, 2) - Subtilisin/Furin - Streptokinase - S1P
v • d • e
Globulins: beta globulins
Angiostatin - Haemopexin - Beta-2 microglobulin - Factor H - Plasminogen - Properdin - Sex hormone binding globulin - Transferrin
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Plasmin". A list of authors is available in Wikipedia.
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE