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plasminogen activator inhibitor 1; PAI; PAI-1; endothelial plasminogen activator inhibitor; Serpin E1 (SERPINE1 PAI1 PLANH1)
Function:
- serine protease inhibitor
- acts as 'bait' for tissue plasminogen activator, urokinase, protein C & matriptase-3/TMPRSS7
- its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis
- inactivated by proteolytic attack of the urokinase & tissue-type plasminogen activator (TPA), cleaving the 369-Arg-|-Met-370 bond
- forms protease inhibiting heterodimer with TMPRSS7
- interacts with VTN
- binds LRP1B
- binding is followed by internalization & degradation
Structure: belongs to the serpin family
Compartment: secreted
Expression:
- found in plasma & platelets, endothelial cells
- found in hepatoma & fibrosarcoma cells
- induced by hypoxia
Pathology:
- defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency*
- high concentrations of SERPINE1
- seem to contribute to development of venous thrombosis
- does not seem to contribute to development of arterial thrombosis
* heterozygousity of null SERPINE1 allele associated with longevity [6]
Related
PAI1 RNA-binding protein 1; PAI-RBP1; SERPINE1 mRNA-binding protein 1 (SERBP1, PAIRBP1, CGI-55)
plasminogen activator
plasminogen activator inhibitor 2; PAI-2; monocyte Arg-serpin; placental plasminogen activator inhibitor; Serpin B2; urokinase inhibitor (SERPINB2, PAI2, PLANH2)
SERPINE1 gene mutation
General
tissue plasminogen activator inhibitor; tPA inhibitor (TPA-I)
Properties
COMPARTMENT: plasma
INHIBITS: serine protease
SIZE: entity length = 402 aa
MW = 45 kD
MOTIF: signal sequence {1-23}
N-glycosylation site {N232}
N-glycosylation site {N288}
N-glycosylation site {N352}
peptide motif {369-370}
Database Correlations
OMIM correlations
MORBIDMAP 173360
UniProt P05121
Pfam PF00079
Entrez Gene 5054
Kegg hsa:5054
References
- UniProt :accession P05121
- GeneReviews
http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/SERPINE1
- Wikipedia; Note: plasminogen activator inhibitor-1 entry
http://en.wikipedia.org/wiki/plasminogen_activator_inhibitor-1
- SeattleSNPs
http://pga.gs.washington.edu/data/serpine1/
- Fibrinolysis, Thrombosis, & Hemostasis: Concepts,
Perspectives, and Clinical Applications. S Sherry,
Lea & Febiger, Philadelphia, 1992, pg 84
- Khan SS, Shah SJ, Klyachko E et al
A null mutation in SERPINE1 protects against biological aging
in humans.
Science Advances. 15 Nov 2017:Vol. 3, no. 11, eaao1617
PMID: 29152572 Free PMC Article
http://advances.sciencemag.org/content/3/11/eaao1617.full
Component-of
tPA/tPA inhibitor 1