Summary of SERPINE1
The gene codes for a protein, serpin family E member 1. Defects cause plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency). High concentrations are linked to thrombophilia [R].
The Function of SERPINE1
Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.
Protein names
Recommended name:
Plasminogen activator inhibitor 1Short name:
PAIAlternative name(s):
PAI-1Endothelial plasminogen activator inhibitor
Serpin E1
- RS1799768 (SERPINE1) ??
- RS2227631 (SERPINE1) ??
- RS2227667 (SERPINE1) ??
- RS2227684 (SERPINE1) ??
- RS7242 (SERPINE1) ??
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Top Gene-Substance Interactions
SERPINE1 Interacts with These Diseases
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Substances That Increase SERPINE1
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Substances That Decrease SERPINE1
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Advanced Summary
From NCBI Gene: Plasminogen activator inhibitor type 1 deficiencyFrom UniProt: High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions. Plasminogen activator inhibitor-1 deficiency (PAI-1D): 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. [MIM:613329]
From NCBI Gene: This 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 this gene are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), and high concentrations of the gene product are associated with thrombophilia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009] From UniProt: Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.
Conditions with Increased Gene Activity
Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
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Conditions with Decreased Gene Activity
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Technical
The following transcription factors affect gene expression:
Tissue specificity:
Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.
Gene Pathways:
Molecular Function:
Biological Processes:
- Angiogenesis
- Cellular Response To Lipopolysaccharide
- Chronological Cell Aging
- Circadian Rhythm
- Defense Response To Gram-Negative Bacterium
- Extracellular Matrix Organization
- Fibrinolysis
- Negative Regulation Of Blood Coagulation
- Negative Regulation Of Cell Adhesion Mediated By Integrin
- Negative Regulation Of Cell Migration
- Negative Regulation Of Endopeptidase Activity
- Negative Regulation Of Endothelial Cell Apoptotic Process
- Negative Regulation Of Extrinsic Apoptotic Signaling Pathway Via Death Domain Receptors
- Negative Regulation Of Fibrinolysis
- Negative Regulation Of Plasminogen Activation
- Negative Regulation Of Smooth Muscle Cell-Matrix Adhesion
- Negative Regulation Of Smooth Muscle Cell Migration
- Negative Regulation Of Vascular Wound Healing
- Negative Regulation Of Wound Healing
- Platelet Degranulation
- Positive Regulation Of Angiogenesis
- Positive Regulation Of Blood Coagulation
- Positive Regulation Of Inflammatory Response
- Positive Regulation Of Interleukin-8 Production
- Positive Regulation Of Leukotriene Production Involved In Inflammatory Response
- Positive Regulation Of Monocyte Chemotaxis
- Positive Regulation Of Receptor-Mediated Endocytosis
- Positive Regulation Of Transcription From Rna Polymerase Ii Promoter
- Regulation Of Receptor Activity
Drug Bank:
- Alteplase
- Anistreplase
- Drotrecogin Alfa
- Urokinase
- Tenecteplase
- Reteplase