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PAI-1/SerpinE1 Protein, Antibody, ELISA Kit, cDNA Clone

PAI-1/SerpinE1 Related Areas

PAI-1/SerpinE1 Related Pathways

PAI-1/SerpinE1 Related Product

    PAI-1/SerpinE1 Summary & Protein Information

    PAI-1/SerpinE1 Background

    Gene Summary: SERPINE1 gene encodes a member of the serine proteinase inhibitor (serpin) superfamily. This member is the principal inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), and hence is an inhibitor of fibrinolysis. Defects in SERPINE1 gene are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), and high concentrations of the SERPINE1 gene product are associated with thrombophilia. Alternatively spliced transcript variants encoding different isoforms have been found for SERPINE1 gene. [provided by RefSeq, Sep 2009]
    General information above from NCBI
    Subunit structure: Forms protease inhibiting heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation.
    Subcellular location: Secreted.
    Tissue specificity: Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.
    Post-translational: Inactivated by proteolytic attack of the urokinase-type (u- PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond.
    Involvement in disease: Plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]: A hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.
    Sequence similarity: Belongs to the serpin family.
    General information above from UniProt

    Plasminogen activator inhibitor 1, also known as PAI-1, Endothelial plasminogen activator inhibitor, SerpinE1 and PLANH1, is a secreted glycoprotein which belongs to the serpin family. SerpinE1 is the primary physiological inhibitor of the two plasminogen activators urokinase (uPA) and tissue plasminogen activator (tPA). Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. Defects in SerpinE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency) which is characterized by abnormal bleeding due to SerpinE1 defect in the plasma. High concentrations of SerpinE1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis. Studies of PAI-1 have contributed significantly to the elucidation of the protease inhibitory mechanism of serpins, which is based on a metastable native state becoming stabilised by insertion of the RCL into the central beta-sheet A and formation of covalent complexes with target proteases. Greater expression of PAI-1 has been associated with increased survival of cells and resistance to apoptosis. PAI-1 appears to influence apoptosis by decreasing cell adhesion (anoikis) as well as its effect on intracellular signaling. PAI-1, in its active state, also binds to the extracellular protein vitronectin. When in complex with its target proteases, it binds with high affinity to endocytosis receptors of the low density receptor family. The mechanisms of PAI-1 overexpression during obesity are complex, and it is conceivable that several inducers are involved at the same time at several sites of synthesis. PAI-1 is also implicated in adipose tissue development and in the control of insulin signaling in adipocytes. It suggests that PAI-1 inhibitors serve in the control of atherothrombosis and insulin resistance.

    PAI-1/SerpinE1 Alternative Name

    PAI,PAI1,PAI-1,PLANH1,serpin E1,SERPINE1, [human]
    Serpine1,PAI,PAI1,PAI-1,Planh1 serpin E1, [mouse]

    PAI-1/SerpinE1 Related Studies

  • Alessi MC, et al. (2006) PAI-1 and the metabolic syndrome: links, causes, and consequences. Arterioscler Thromb Vasc Biol. 26(10): 2200-7.
  • Schneider DJ, et al. (2008) The effect of plasminogen activator inhibitor type 1 on apoptosis. Thromb Haemost. 100(6): 1037-40.
  • Dupont DM, et al. (2009) Biochemical properties of plasminogen activator inhibitor-1. Front Biosci. 14: 1337-61.
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