GO:0031639 plasminogen activation: Proteolytic Cascade, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0031639 plasminogen activation is the biological process that converts the inactive zymogen plasminogen into the active serine protease plasmin by cleavage at an internal Arg-Val site.
• The reaction is catalyzed by plasminogen activators such as tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU), and is accelerated when plasminogen and its activators are bound to fibrin or cell-surface receptors.
• Plasminogen activation is the central event of fibrinolysis, and its dysregulation is linked to thrombosis, bleeding, inflammation, cancer invasion and renal disease.
• The system is tightly controlled by inhibitors including SERPINE1 (PAI-1), SERPINB2 (PAI-2), alpha2-antiplasmin and complement-related regulators.
• Plasminogen activation is not restricted to blood: it operates in the nervous system, hematopoietic cells and leukemias, where it influences catecholaminergic function and cell migration.
• CRISPR-based knockout, point-mutation, knock-in and overexpression models allow causal testing of PLG, PLAT, PLAU, PLAUR and SERPINE1 in plasminogen activation research.
Description
Plasminogen activation (GO:0031639) is the proteolytic process in which the inactive zymogen plasminogen is converted to the active serine protease plasmin. This conversion requires cleavage of plasminogen at an internal Arg-Val peptide bond, generating an N-terminal A-chain and a C-terminal B-chain that remain linked by a disulfide bond; further proteolytic trimming can remove the preactivation peptide. Because plasmin is the principal enzyme that degrades fibrin, plasminogen activation is the rate-limiting step of fibrinolysis and a central node in hemostasis. The process is not a simple solution-phase reaction: plasminogen and its activators assemble on fibrin and on cell surfaces, where receptor binding and co-localization dramatically enhance catalytic efficiency. This spatial organization allows plasminogen activation to be targeted to specific tissues and to be used in processes beyond clot removal, including cell migration, tissue remodeling and inflammation. For researchers, GO:0031639 is therefore both a biochemical pathway and a systems-level control point. Its components include the substrate PLG, the activators PLAT and PLAU, the receptor PLAUR, and inhibitors such as SERPINE1 and SERPINB2. Dysregulated plasminogen activation has been documented in leukemia and normal hematopoietic cells, in glomerular proteinuria with intratubular complement activation, and in platelet pathophysiology. Understanding the exact molecular steps, the cell-surface assembly and the regulatory inhibitors is essential for designing experiments that distinguish cause from correlation in thrombosis, cancer and inflammatory disease.
plasminogen activation At A Glance
| GO ID | GO:0031639 |
|---|---|
| GO term | plasminogen activation |
| Ontology | biological_process |
| Synonym | cleavage of plasminogen to plasmin |
| Major function | Conversion of inactive plasminogen to active plasmin by limited proteolysis |
| Key activators | PLAT (t-PA) and PLAU (u-PA) |
| Key substrate | PLG (plasminogen) |
| Key receptor | PLAUR (u-PAR) for urokinase-mediated activation |
| Key inhibitors | SERPINE1 (PAI-1), SERPINB2 (PAI-2), alpha2-antiplasmin |
| Cellular contexts | Fibrin surfaces, cell surfaces, platelets, hematopoietic cells, kidney tubules |
What Is GO:0031639?
In my own words, plasminogen activation (GO:0031639) is the biochemical process that turns the inactive precursor plasminogen into the active protease plasmin. The core event is a proteolytic cleavage at an internal Arg-Val site that separates plasminogen into an N-terminal A-chain and a C-terminal B-chain held together by a disulfide bond; additional cleavage events can remove the preactivation peptide. This process is catalyzed by plasminogen activators and can occur on fibrin or on cell surfaces, where binding increases the efficiency of activation.
Why Is plasminogen activation Important in Cell Biology?
Plasminogen activation is important because it controls the generation of plasmin, the protease responsible for fibrin degradation and for much of extracellular proteolysis in physiology and disease. When this process is too active, it can contribute to bleeding, inflammation and tissue damage; when it is insufficient, it can promote thrombosis and impaired clearance of fibrin. Beyond hemostasis, plasminogen activation influences platelet function, leukocyte behavior, renal tubular complement activation and catecholaminergic signaling, making it a cross-disciplinary research target.
• It is the rate-limiting step of fibrinolysis and therefore central to clot resolution and hemostatic balance.
• It generates plasmin, a broad-spectrum serine protease that degrades fibrin and activates matrix metalloproteinases and growth factors.
• It is spatially regulated on fibrin and cell surfaces, which determines where proteolysis occurs.
• It is implicated in platelet pathophysiology and translational applications in thrombosis and bleeding.
• It contributes to intratubular complement activation in glomerular proteinuria, linking coagulation proteases to kidney inflammation.
• It is active in human leukemia and normal hematopoietic cells, where it influences cell behavior.
• It modulates catecholaminergic function in the nervous system, connecting proteolysis to neurotransmission.
• Its inhibitors, including SERPINE1 and SERPINB2, are therapeutic and biomarker candidates in cardiovascular and inflammatory disease.
• It provides a tractable model for studying zymogen activation, protease cascades and receptor co-localization.
• CRISPR-engineered cell models can test causality of PLG, PLAT, PLAU, PLAUR and SERPINE1 in disease-relevant phenotypes.
What Happens During plasminogen activation?
Recognition and binding of plasminogen to fibrin or cell surfaces
In simple terms: Plasminogen first docks onto a surface, which makes it much easier to activate.
Plasminogen activation is efficient only when plasminogen and its activators are brought together on a suitable surface. Plasminogen binds to fibrin and to cell-surface receptors, and this binding changes its conformation and accessibility to activators. On cell surfaces, receptor-bound urokinase can activate plasminogen much more effectively than fluid-phase urokinase, demonstrating that localization is a key determinant of the reaction. This step explains why plasminogen activation is targeted to sites of injury, inflammation or tumor invasion rather than occurring uniformly in plasma.
Cleavage at the internal Arg-Val site
In simple terms: The activator cuts plasminogen once, converting it into the active protease plasmin.
The defining biochemical event of GO:0031639 is cleavage of plasminogen at an internal Arg-Val peptide bond. This cleavage produces an N-terminal A-chain and a C-terminal B-chain that remain connected by a disulfide bond. The B-chain contains the catalytic serine protease domain responsible for plasmin activity, while the A-chain contains kringle domains that mediate binding to fibrin and receptors. Further proteolytic cleavage events can remove the preactivation peptide, completing the conversion to mature plasmin.
Catalysis by tissue-type and urokinase-type plasminogen activators
In simple terms: Two main enzymes, t-PA and u-PA, perform the cut that activates plasminogen.
Plasminogen activation is catalyzed by plasminogen activators, principally tissue-type plasminogen activator (PLAT, t-PA) and urokinase-type plasminogen activator (PLAU, u-PA). t-PA is especially effective when bound to fibrin, where it activates plasminogen in proximity to the clot, whereas u-PA acts prominently on cell surfaces through its receptor PLAUR. Receptor-bound urokinase retains activity and can activate plasminogen in a spatially restricted manner, which is important for cell migration and tissue remodeling. The balance between these activators determines the site and extent of plasmin generation.
Amplification and feedback by generated plasmin
In simple terms: Once a little plasmin is made, it can help make more plasmin, amplifying the response.
Plasmin generated by plasminogen activation can participate in positive feedback loops that enhance further activation. Plasmin can modify surfaces and substrates in ways that promote additional plasminogen binding and activation, and it can activate other proteases and growth factors. This amplification is physiologically useful for rapid clot lysis but must be constrained to avoid excessive proteolysis. The interplay between activation and inhibition therefore determines the net proteolytic output of the system.
Inhibition and termination of plasminogen activation
In simple terms: Inhibitors act as brakes that stop plasmin from being made or from working too long.
Plasminogen activation is controlled by serine protease inhibitors. SERPINE1 (PAI-1) and SERPINB2 (PAI-2) inhibit the plasminogen activators, while alpha2-antiplasmin rapidly inhibits plasmin in plasma. These inhibitors limit the duration and spatial spread of plasminogen activation, preventing uncontrolled proteolysis. In disease states, an imbalance between activators and inhibitors can shift the system toward either excessive or insufficient plasmin generation.
Key Genes Involved in GO:0031639 plasminogen activation
The following genes and proteins are the principal components and regulators of plasminogen activation (GO:0031639) as documented in the cited literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| PLG | Encodes plasminogen, the inactive zymogen substrate of the process | Core substrate for knockout and point-mutation studies of plasmin generation |
| PLAT | Encodes tissue-type plasminogen activator (t-PA), a major activator of plasminogen | Key target for fibrin-directed activation and thrombosis models |
| PLAU | Encodes urokinase-type plasminogen activator (u-PA), an activator of plasminogen | Central to cell-surface and receptor-mediated activation studies |
| PLAUR | Encodes the urokinase receptor (u-PAR) that binds u-PA and enhances plasminogen activation | Receptor knockout and knock-in models for spatial control of proteolysis |
| SERPINE1 | Encodes PAI-1, a principal inhibitor of plasminogen activators | Disease-relevant regulator in thrombosis, fibrosis and cancer |
| SERPINB2 | Encodes PAI-2, an inhibitor of plasminogen activators | Less-studied inhibitor with roles in inflammation and cell survival |
| SERPINF2 | Encodes alpha2-antiplasmin, the main plasma inhibitor of plasmin | Regulator of plasmin lifetime and bleeding/thrombosis balance |
| FGA | Encodes fibrinogen alpha chain, a substrate and scaffold for plasminogen activation | Fibrin scaffold models for activation kinetics |
| FGB | Encodes fibrinogen beta chain, contributing to the fibrin surface | Fibrin assembly and plasminogen binding studies |
| FGG | Encodes fibrinogen gamma chain, important for plasminogen binding to fibrin | Site-directed mutagenesis of fibrin-plasminogen interfaces |
| ANXA2 | Annexin A2 acts as a cell-surface co-receptor for plasminogen and t-PA | Cell-surface activation models and receptor knockout studies |
| MKI67 | Not a plasminogen activation component; listed only as a common proliferation marker in cell models | Use as a control readout, not as a pathway gene |
| TP53 | Not a core plasminogen activation gene; frequently mutated in cancer models where the pathway is studied | Context gene for cancer studies of plasminogen activation |
| CDKN2A | Not a core plasminogen activation gene; common cancer model context | Context gene for cell-cycle control in pathway studies |
| VIM | Not a plasminogen activation gene; used as a mesenchymal marker in invasion assays | Control marker for migration and invasion experiments |
| ACTB | Housekeeping gene used for normalization in expression studies of plasminogen activation genes | Reference gene for qPCR and RNA-seq |
| GAPDH | Housekeeping gene used for normalization in plasminogen activation research | Reference gene for expression and protein assays |
How Is plasminogen activation Regulated?
Plasminogen activation is regulated at multiple levels. Activation is enhanced when plasminogen and plasminogen activators bind to fibrin or cell-surface receptors, which concentrates the reactants and increases catalytic efficiency. The reaction is opposed by serine protease inhibitors: SERPINE1 (PAI-1) and SERPINB2 (PAI-2) inhibit the activators, and alpha2-antiplasmin inhibits plasmin itself. In platelets and hematopoietic cells, the plasminogen activation system is integrated with cell activation and migration programs. In the kidney, urokinase/plasminogen-driven intratubular complement activation can be reduced by amiloride, indicating that ion transport and complement crosstalk modulate the pathway in disease. In the nervous system, plasminogen activation is linked to catecholaminergic function, showing that regulation extends beyond hemostasis.
plasminogen activation and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PLG | Thrombosis and impaired fibrinolysis due to reduced plasmin generation | PLG knockout or point-mutation cell lines with fibrin degradation assays |
| PLAT | Thrombotic and bleeding phenotypes related to t-PA activity | PLAT knockout and tagged knock-in for localization studies |
| PLAU | Cell-surface proteolysis in inflammation and cancer | PLAU knockout and PLAUR knock-in models for receptor-mediated activation |
| SERPINE1 | Thrombosis, fibrosis and cancer-associated proteolysis | SERPINE1 overexpression and point-mutation models |
| PLAUR | Kidney and inflammatory disease with urokinase-driven complement activation | PLAUR knockout kidney epithelial cells and complement activation assays |
Thrombosis, bleeding and platelet disorders
Because plasminogen activation is the rate-limiting step of fibrinolysis, defects that reduce plasmin generation predispose to thrombosis, whereas excessive activation can cause bleeding. The plasminogen activation system is also active in platelets and contributes to platelet pathophysiology, making it relevant to antithrombotic and translational applications. Inhibitors such as SERPINE1 and alpha2-antiplasmin shape the clinical phenotype by controlling the duration of plasmin activity.
Kidney disease and complement activation
In glomerular proteinuria, urokinase/plasminogen-driven activation can trigger intratubular complement activation, linking plasminogen activation to kidney inflammation and injury. Amiloride reduces this urokinase/plasminogen-driven complement activation, suggesting that the pathway is pharmacologically modifiable in renal disease. This connects GO:0031639 to complement biology and tubular damage in proteinuric states.
Leukemia and hematopoietic biology
Plasminogen activation occurs in human leukemia and in normal hematopoietic cells, where it influences cell behavior and the hematopoietic microenvironment. The presence of an active plasminogen activation system in leukemic cells suggests that it may contribute to invasion, migration or survival programs. This makes hematopoietic malignancy a relevant context for studying the pathway.
Neurobiology and catecholaminergic function
The plasminogen activation system regulates catecholaminergic function, indicating that plasmin generation can influence neurotransmitter-related processes in the nervous system. This expands the disease relevance of GO:0031639 beyond vascular biology to neurobiology and behavior. Researchers studying neurological phenotypes may therefore consider plasminogen activation genes as modifiers.
From plasminogen activation-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is PLG required for plasmin generation and fibrin degradation? | PLG knockout cell line with fibrin zymography and plasmin activity assays |
| Does a specific Arg-Val cleavage site mutation block plasminogen activation? | PLG point-mutation knock-in at the activation cleavage site |
| Does receptor binding of urokinase enhance plasminogen activation? | PLAUR knockout and PLAUR knock-in cells with PLAU activation assays |
| Can SERPINE1 overexpression suppress plasminogen activation? | SERPINE1 overexpression cell model with activator activity readouts |
| Where does plasminogen activation occur in a cell? | Tagged knock-in of PLG or PLAT with fluorescent tags for imaging |
| Does loss of PLAT alter clot lysis in a disease-relevant cell type? | PLAT knockout in endothelial or hepatic cell lines with clot lysis assays |
How to Study the plasminogen activation Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Zymography | Plasminogen activation and plasmin activity in gels | Comparing activator capacity across cell lines |
| Chromogenic plasmin substrate assay | Real-time plasmin generation | Kinetic analysis of PLG, PLAT and PLAU variants |
| Cell-surface binding assay | Receptor-dependent plasminogen activation | PLAUR knockout and knock-in studies |
| RNA-seq | Expression of plasminogen activation genes | Disease model profiling and target discovery |
| qPCR | Relative mRNA levels of PLG, PLAT, PLAU, PLAUR, SERPINE1 | Validation of CRISPR perturbations |
| Immunoblotting | Plasminogen cleavage products and inhibitor complexes | Confirming activation-state changes |
| Fluorescence imaging | Subcellular localization of tagged pathway proteins | Tagged knock-in studies of PLG, PLAT or PLAU |
| Fibrin degradation assay | Functional output of plasminogen activation | Testing disease-relevant cell models |
Zymography and plasmin activity assays
Zymography and chromogenic or fluorogenic plasmin substrate assays directly measure the conversion of plasminogen to plasmin and the resulting proteolytic activity. These methods are used to quantify the effects of PLG, PLAT, PLAU, PLAUR and SERPINE1 perturbations on plasminogen activation. They are typically applied to conditioned media, cell lysates or purified protein systems.
Cell-surface binding and receptor studies
Because plasminogen activation is enhanced on cell surfaces, binding assays and receptor-blocking experiments are used to study PLAUR-dependent activation. These approaches measure how receptor-bound urokinase activates plasminogen and how this differs from fluid-phase activation. They are central to understanding spatial regulation of the pathway.
Expression and transcriptomic profiling
RNA-seq and qPCR are used to profile expression of plasminogen activation genes such as PLG, PLAT, PLAU, PLAUR, SERPINE1 and SERPINB2 across disease models. Transcriptomic profiling can reveal co-regulated modules and candidate regulators in leukemia, kidney disease and platelet biology. These data guide the selection of CRISPR targets for functional validation.
Proteomics and activation-state detection
Proteomic and immunoblot approaches can detect plasminogen cleavage products, including the A-chain and B-chain generated by activation. These methods allow researchers to distinguish the zymogen from the active protease and to monitor inhibitor complexes. They are useful for confirming that a genetic perturbation changes the activation state rather than only the expression level.
How CRISPR Can Be Used to Study GO:0031639 plasminogen activation
Knockout
CRISPR knockout of PLG, PLAT, PLAU, PLAUR or SERPINE1 can establish whether a gene is required for plasminogen activation in a given cell type. Knockout models are particularly useful for separating the contributions of t-PA versus u-PA and for testing receptor dependence. Loss-of-function phenotypes can be measured with zymography, plasmin activity assays and fibrin degradation readouts.
Point Mutation
Point mutation of the internal Arg-Val cleavage site in PLG can test whether this specific proteolytic event is required for plasmin generation. Point mutations in activator or inhibitor active sites can dissect catalytic versus binding functions. These models are valuable when complete knockout would eliminate multiple functions of a multidomain protein.
Knock-in
Knock-in of tagged or disease-associated variants of PLG, PLAT, PLAU or PLAUR allows tracking of protein localization and activation in living cells. Knock-in of receptor variants can test how cell-surface binding modulates plasminogen activation efficiency. These models connect genotype to spatial and kinetic phenotypes.
Overexpression
Overexpression of SERPINE1, SERPINB2 or other inhibitors can test whether increased inhibitor levels suppress plasminogen activation and downstream proteolysis. Overexpression of PLAT or PLAU can model excessive activation states relevant to bleeding or tissue damage. These experiments complement knockout studies by probing the opposite direction of pathway activity.
How EDITGENE Supports plasminogen activation Research
Researchers studying plasminogen activation-related genes often need to determine whether a candidate gene is causally involved in plasmin generation, receptor-mediated activation or inhibitor control, rather than merely correlated with a disease phenotype. EDITGENE provides CRISPR-engineered cell models and screening services that allow such causal questions to be tested directly in relevant cellular contexts.
Contact EDITGENE today to design your custom CRISPR model for plasminogen activation research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| PLAT Knockout HEK293 Cell Line | EDJ-KQ1465 | Human | 5327 | Details Get a Quote |
| FGA Knockout HEK293 Cell Line | EDJ-KQ2280 | Human | 2243 | Details Get a Quote |
| APOH Knockout HEK293 Cell Line | EDJ-KQ2394 | Human | 350 | Details Get a Quote |
| FGB Knockout HEK293 Cell Line | EDJ-KQ2950 | Human | 2244 | Details Get a Quote |
| F11 Knockout HEK293 Cell Line | EDJ-KQ3628 | Human | 2160 | Details Get a Quote |
| PLAUR Knockout HEK293 Cell Line | EDJ-KQ3817 | Human | 5329 | Details Get a Quote |
| FGG Knockout HEK293 Cell Line | EDJ-KQ4591 | Human | 2266 | Details Get a Quote |
| TMPRSS9 Knockout HEK293 Cell Line | EDJ-KQ10818 | Human | 360200 | Details Get a Quote |
| PLAU Knockout HEK293 Cell Line | EDJ-KQ17699 | Human | 5328 | Details Get a Quote |
| PLAU Knockout A-549 Cell Line | EDJ-KQ18997 | Human | 5328 | Details Get a Quote |
| PLAU Knockout HCT 116 Cell Line | EDJ-KQ18998 | Human | 5328 | Details Get a Quote |
| PLAU Knockout HeLa Cell Line | EDJ-KQ18999 | Human | 5328 | Details Get a Quote |
| PLAT Knockout A-549 Cell Line | EDJ-KQ21030 | Human | 5327 | Details Get a Quote |
| PLAT Knockout HCT 116 Cell Line | EDJ-KQ21031 | Human | 5327 | Details Get a Quote |
| PLAT Knockout HeLa Cell Line | EDJ-KQ21032 | Human | 5327 | Details Get a Quote |
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Frequently Asked Questions About plasminogen activation
What is plasminogen activation (GO:0031639)?
Plasminogen activation is the biological process in which inactive plasminogen is cleaved to form active plasmin, including cleavage at an internal Arg-Val site to generate an N-terminal A-chain and a C-terminal B-chain held by a disulfide bond.
What genes are involved in plasminogen activation?
Key genes include PLG (plasminogen), PLAT (t-PA), PLAU (u-PA), PLAUR (u-PAR), SERPINE1 (PAI-1), SERPINB2 (PAI-2) and SERPINF2 (alpha2-antiplasmin).
Which enzymes activate plasminogen?
Tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU) are the principal enzymes that activate plasminogen.
Why is plasminogen activation important in fibrinolysis?
It is the rate-limiting step that generates plasmin, the protease that degrades fibrin, so it directly controls clot resolution.
How is plasminogen activation regulated on cell surfaces?
Plasminogen and its activators bind to fibrin and cell-surface receptors such as PLAUR, which co-localizes the reactants and greatly enhances activation efficiency.
What diseases are linked to abnormal plasminogen activation?
Thrombosis, bleeding disorders, platelet pathophysiology, glomerular proteinuria with complement activation, leukemia and neurological conditions have been linked to the pathway.
How can CRISPR be used to study plasminogen activation?
CRISPR knockout, point mutation, knock-in and overexpression models can test the causal roles of PLG, PLAT, PLAU, PLAUR and SERPINE1 in plasmin generation and downstream phenotypes.
What methods measure plasminogen activation in the lab?
Zymography, chromogenic plasmin substrate assays, cell-surface binding assays, RNA-seq, qPCR, immunoblotting and fibrin degradation assays are commonly used.
Is plasminogen activation only about blood clotting?
No. It also operates in platelets, hematopoietic cells, the kidney and the nervous system, where it influences inflammation, cell behavior and catecholaminergic function.
What is the role of SERPINE1 in plasminogen activation?
SERPINE1 encodes PAI-1, a principal inhibitor of plasminogen activators, and therefore acts as a brake on plasmin generation.
Conclusion
Plasminogen activation (GO:0031639) is a tightly controlled proteolytic process that converts plasminogen into plasmin through cleavage at an internal Arg-Val site, generating a disulfide-linked A-chain and B-chain. Its efficiency depends on assembly on fibrin and cell surfaces, where activators such as PLAT and PLAU act and where receptors such as PLAUR enhance catalysis. The pathway is balanced by inhibitors including SERPINE1, SERPINB2 and alpha2-antiplasmin, and its dysregulation is relevant to thrombosis, bleeding, kidney disease, leukemia and neurobiology. For researchers, CRISPR-engineered knockout, point-mutation, knock-in and overexpression models provide a direct way to test causality within this pathway and to connect specific genes to disease-relevant phenotypes.
References
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- 2. Isaksson GL et al.. 2024. Amiloride Reduces Urokinase/Plasminogen-Driven Intratubular Complement Activation in Glomerular Proteinuria.. J Am Soc Nephrol 35(4):410-425 PMID: 38254266
- 3. Wun TC. 1988. Plasminogen activation: biochemistry, physiology, and therapeutics.. Crit Rev Biotechnol 8(2):131-48 PMID: 2976309
- 4. Mustjoki S et al.. 1999. Plasminogen activation in human leukemia and in normal hematopoietic cells.. APMIS 107(1):144-9 PMID: 10190291
- 5. Anglés-Cano E. 1994. Overview on fibrinolysis: plasminogen activation pathways on fibrin and cell surfaces.. Chem Phys Lipids 67-68:353-62 PMID: 8187235
- 6. Ellis V et al.. 1991. Plasminogen activation by receptor-bound urokinase.. Semin Thromb Hemost 17(3):194-200 PMID: 1665584
- 7. Madoiwa S. 2014. [Plasminogen activation and regulation of fibrinolysis].. Nihon Rinsho 72(7):1218-23 PMID: 25163311
- 8. Bai H et al.. 2012. The plasminogen activation system and the regulation of catecholaminergic function.. J Biomed Biotechnol 2012:721657 PMID: 23097598
