The Function of PLAU
Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
Protein names
Recommended name:
Urokinase-type plasminogen activatorAlternative name(s):
U-plasminogen activatoruPA
- RS2227551 (PLAU) ??
- RS2227564 (PLAU) ??
- RS2688608 (PLAU) ??
To see your genotype, you should be logged in and have a file with your genotype uploaded.
Top Gene-Substance Interactions
PLAU Interacts with These Diseases
Disease | Score |
Substances That Increase PLAU
Substances | Interaction | Organism | Category |
Substances That Decrease PLAU
Substances | Interaction | Organism | Category |
Advanced Summary
Plasminogen activator, urokinase (PLAU), or urokinase-plasminogen activator (UPA).
PLAU gene encodes for a protein the converts an inactive protein plasminogen to the active form, plasmin [R]. Plasmin is a blood enzyme that degrades many blood plasma proteins and fibrin clots [R].
PLAU plays a role in the breakdown of fibrin, inflammation, tumor growth, and angiogenesis (the growth of new blood vessels from existing ones) [R].
The PLAU protein is processed through multiple forms before reaching its active state [R]. Certain mutations in the PLAU gene can keep the PLAU protein from transitioning to the active form [R].
An inactive form of the PLAU protein can bind to the PLAU receptor and trigger cell migration [R], degradation of the extracellular matrix, and tissue inflammation [R].These functions have been associated with wound healing and tumor cell metastasis [R].
Mutations in the PLAU gene have been associated with a number of diseases, including Quebec platelet disorder, late-onset Alzheimer’s disease, and many cancers [R].
In Quebec Platelet Disorder, PLAU is overproduced, causing increased and/or delayed bleeding [R1, R2].
In late-onset Alzheimer’s disease, a variation in PLAU keeps plasmin from breaking down certain proteins that cause the disease [R].
Evidence suggests an association with PLAU gene variations and asthma [R].
PLAU has been implicated in susceptibility to many cancers and in resistance to many cancer treatments [R].
Increased PLAU production has been implicated in atherosclerosis [R], myocardial infarction, [R], and mitral valve prolapse [R].
Potential Fixes:
PLAU provides a potential target for future gene therapy research and cancer drug research [R].
Treatment for PLAU induced Quebec syndrome involves fibrinolytic inhibitor therapy [R]
Conditions with Increased Gene Activity
Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
---|
Conditions with Decreased Gene Activity
Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
---|
Technical
The following transcription factors affect gene expression:
Tissue specificity:
Expressed in the prostate gland and prostate cancers.
Gene Pathways:
Enzyme Regulation:
Inhibited by SERPINA5.
Molecular Function:
Biological Processes:
- Blood Coagulation
- Chemotaxis
- Fibrinolysis
- Positive Regulation Of Cell Migration
- Proteolysis
- Regulation Of Cell Adhesion Mediated By Integrin
- Regulation Of Cell Proliferation
- Regulation Of Receptor Activity
- Regulation Of Smooth Muscle Cell-Matrix Adhesion
- Regulation Of Smooth Muscle Cell Migration
- Regulation Of Wound Healing
- Response To Hypoxia
- Signal Transduction
- Smooth Muscle Cell Migration
- Angiogenesis
- Cellular Response To Fluid Shear Stress
- Cellular Response To Glucose Stimulus
- Cellular Response To Hepatocyte Growth Factor Stimulus
- Cellular Response To Hypoxia
- Cellular Response To Lipopolysaccharide
- Cellular Response To Staurosporine
- Embryo Implantation
- Neuron Death
- Positive Regulation Of Cell Proliferation
- Positive Regulation Of Ovulation
- Positive Regulation Of Reactive Oxygen Species Metabolic Process
- Positive Regulation Of Smooth Muscle Cell Migration
- Regulation Of Hepatocyte Proliferation
- Response To Hyperoxia
- Skeletal Muscle Tissue Regeneration
- Spermatogenesis
Drug Bank:
- Urokinase
- Amiloride