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Literature summary for 3.4.21.73 extracted from
- Regulation of arterial remodeling and angiogenesis by urokinase-type plasminogen activator (2009), Can. J. Physiol. Pharmacol., 87, 231-251.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | Thrombin hydrolysis provides the mechanism of proteolytic inactivation of uPA cleavage of the Arg156-Phe157 enzyme bond that does not exclude nonproteolytic functioning of such peptide forms | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | uPA is secreted by cells as a single-chain polypeptide | Mus musculus | - |
- |
| extracellular | uPA is secreted by cells as a single-chain polypeptide | Homo sapiens | - |
- |
| extracellular | uPA is secreted by cells as a single-chain polypeptide | Rattus norvegicus | - |
- |
| additional information | the uPA receptor is concentrated in caveolae, special intrusions of the plasma membrane maintained by the membrane protein caveolin. Urokinase stabilizes the vitronectin-binding conformation of the uPAR and thus stimulates a vitronectin-dependent adhesion of some cells | Mus musculus | - |
- |
| additional information | the uPA receptor is concentrated in caveolae, special intrusions of the plasma membrane maintained by the membrane protein caveolin. Urokinase stabilizes the vitronectin-binding conformation of the uPAR and thus stimulates a vitronectin-dependent adhesion of some cells | Homo sapiens | - |
- |
| additional information | the uPA receptor is concentrated in caveolae, special intrusions of the plasma membrane maintained by the membrane protein caveolin. Urokinase stabilizes the vitronectin-binding conformation of the uPAR and thus stimulates a vitronectin-dependent adhesion of some cells | Rattus norvegicus | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 54000 | - |
x * 54000, single-chain proenzyme, SDS-PAGE | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Mus musculus | uPA-uPAR complexes concentrate the plasmin production that provides extracellular matrix proteolysis, weakened cell-cell contact, and increased cell motility. The proteolytic mechanisms include uPA-induced plasmin generation at focal adhesion sites, which results in extracellular matrix degradation and thus facilitates the detachment of the cell's trailing edge. Plasmin inhibitors can suppress cell migration both in vitro, mechanisms by which uPA can regulate arterial remodeling, angiogenesis, and cell migration and proliferation after arterial injury, overview. Urokinase signaling, overview | ? | - |
? |  |
| additional information | Homo sapiens | uPA-uPAR complexes concentrate the plasmin production that provides extracellular matrix proteolysis, weakened cell-cell contact, and increased cell motility. The proteolytic mechanisms include uPA-induced plasmin generation at focal adhesion sites, which results in extracellular matrix degradation and thus facilitates the detachment of the cell's trailing edge. Plasmin inhibitors can suppress cell migration both in vitro, mechanisms by which uPA can regulate arterial remodeling, angiogenesis, and cell migration and proliferation after arterial injury, overview. Urokinase signaling, overview | ? | - |
? | |
| additional information | Rattus norvegicus | uPA-uPAR complexes concentrate the plasmin production that provides extracellular matrix proteolysis, weakened cell-cell contact, and increased cell motility. The proteolytic mechanisms include uPA-induced plasmin generation at focal adhesion sites, which results in extracellular matrix degradation and thus facilitates the detachment of the cell's trailing edge. Plasmin inhibitors can suppress cell migration both in vitro, mechanisms by which uPA can regulate arterial remodeling, angiogenesis, and cell migration and proliferation after arterial injury, overview. Urokinase signaling, overview | ? | - |
? | |
| plasminogen + H2O | Mus musculus | the uPA proteolytic domain specifically cleaves plasminogen and converts it into the serine protease plasmin with wide substrate specificity. Plasmin directly degrades fibrin, leading to thrombus dissolution and activating a number of matrix metalloproteinases | plasmin + ? | - |
? | |
| plasminogen + H2O | Homo sapiens | the uPA proteolytic domain specifically cleaves plasminogen and converts it into the serine protease plasmin with wide substrate specificity. Plasmin directly degrades fibrin, leading to thrombus dissolution and activating a number of matrix metalloproteinases | plasmin + ? | - |
? | |
| plasminogen + H2O | Rattus norvegicus | the uPA proteolytic domain specifically cleaves plasminogen and converts it into the serine protease plasmin with wide substrate specificity. Plasmin directly degrades fibrin, leading to thrombus dissolution and activating a number of matrix metalloproteinases | plasmin + ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | in the 2-chain urokinase, after cleavage of the single-chain proform, the polypeptide chains A and B, light and heavy chains, respectively, are connected by the Cys148-Cys279 disulfide bond. Thrombin hydrolysis provides the mechanism of proteolytic inactivation of uPA cleavage of the Arg156-Phe157 enzyme bond that does not exclude nonproteolytic functioning of such peptide forms | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| carcinoma cell | - |
Mus musculus | - |
| carcinoma cell | - |
Homo sapiens | - |
| carcinoma cell | - |
Rattus norvegicus | - |
| epithelial cell | - |
Mus musculus | - |
| epithelial cell | - |
Homo sapiens | - |
| epithelial cell | - |
Rattus norvegicus | - |
| fibroblast | - |
Mus musculus | - |
| fibroblast | - |
Homo sapiens | - |
| fibroblast | - |
Rattus norvegicus | - |
| macrophage | - |
Mus musculus | - |
| macrophage | - |
Homo sapiens | - |
| macrophage | - |
Rattus norvegicus | - |
| monocyte | - |
Mus musculus | - |
| monocyte | - |
Homo sapiens | - |
| monocyte | - |
Rattus norvegicus | - |
| myofibroblast | - |
Mus musculus | - |
| myofibroblast | - |
Homo sapiens | - |
| myofibroblast | - |
Rattus norvegicus | - |
| smooth muscle cell | - |
Mus musculus | - |
| smooth muscle cell | - |
Homo sapiens | - |
| smooth muscle cell | - |
Rattus norvegicus | - |
| vascular endothelial cell | - |
Mus musculus | - |
| vascular endothelial cell | - |
Homo sapiens | - |
| vascular endothelial cell | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | uPA-uPAR complexes concentrate the plasmin production that provides extracellular matrix proteolysis, weakened cell-cell contact, and increased cell motility. The proteolytic mechanisms include uPA-induced plasmin generation at focal adhesion sites, which results in extracellular matrix degradation and thus facilitates the detachment of the cell's trailing edge. Plasmin inhibitors can suppress cell migration both in vitro, mechanisms by which uPA can regulate arterial remodeling, angiogenesis, and cell migration and proliferation after arterial injury, overview. Urokinase signaling, overview | Mus musculus | ? | - |
? | |
| additional information | uPA-uPAR complexes concentrate the plasmin production that provides extracellular matrix proteolysis, weakened cell-cell contact, and increased cell motility. The proteolytic mechanisms include uPA-induced plasmin generation at focal adhesion sites, which results in extracellular matrix degradation and thus facilitates the detachment of the cell's trailing edge. Plasmin inhibitors can suppress cell migration both in vitro, mechanisms by which uPA can regulate arterial remodeling, angiogenesis, and cell migration and proliferation after arterial injury, overview. Urokinase signaling, overview | Homo sapiens | ? | - |
? | |
| additional information | uPA-uPAR complexes concentrate the plasmin production that provides extracellular matrix proteolysis, weakened cell-cell contact, and increased cell motility. The proteolytic mechanisms include uPA-induced plasmin generation at focal adhesion sites, which results in extracellular matrix degradation and thus facilitates the detachment of the cell's trailing edge. Plasmin inhibitors can suppress cell migration both in vitro, mechanisms by which uPA can regulate arterial remodeling, angiogenesis, and cell migration and proliferation after arterial injury, overview. Urokinase signaling, overview | Rattus norvegicus | ? | - |
? | |
| plasminogen + H2O | - |
Mus musculus | plasmin + ? | - |
? | |
| plasminogen + H2O | - |
Homo sapiens | plasmin + ? | - |
? | |
| plasminogen + H2O | - |
Rattus norvegicus | plasmin + ? | - |
? | |
| plasminogen + H2O | the uPA proteolytic domain specifically cleaves plasminogen and converts it into the serine protease plasmin with wide substrate specificity. Plasmin directly degrades fibrin, leading to thrombus dissolution and activating a number of matrix metalloproteinases | Mus musculus | plasmin + ? | - |
? | |
| plasminogen + H2O | the uPA proteolytic domain specifically cleaves plasminogen and converts it into the serine protease plasmin with wide substrate specificity. Plasmin directly degrades fibrin, leading to thrombus dissolution and activating a number of matrix metalloproteinases | Homo sapiens | plasmin + ? | - |
? | |
| plasminogen + H2O | the uPA proteolytic domain specifically cleaves plasminogen and converts it into the serine protease plasmin with wide substrate specificity. Plasmin directly degrades fibrin, leading to thrombus dissolution and activating a number of matrix metalloproteinases | Rattus norvegicus | plasmin + ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 54000, single-chain proenzyme, SDS-PAGE | Homo sapiens |
| More | the urokinase molecule consists of 3 structural domains: the N-terminal domain homologous to the epidermal growth factor-like domain, the kringle domain, and the C-terminal proteolytic domain, domain structure of proform and mature form of uPA, overview | Mus musculus |
| More | the urokinase molecule consists of 3 structural domains: the N-terminal domain homologous to the epidermal growth factor-like domain, the kringle domain, and the C-terminal proteolytic domain, domain structure of proform and mature form of uPA, overview | Homo sapiens |
| More | the urokinase molecule consists of 3 structural domains: the N-terminal domain homologous to the epidermal growth factor-like domain, the kringle domain, and the C-terminal proteolytic domain, domain structure of proform and mature form of uPA, overview | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| uPA | - |
Mus musculus |
| uPA | - |
Homo sapiens |
| uPA | - |
Rattus norvegicus |
| Urokinase-type plasminogen activator | - |
Mus musculus |
| Urokinase-type plasminogen activator | - |
Homo sapiens |
| Urokinase-type plasminogen activator | - |
Rattus norvegicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a wide variety of disorders are associated with an imbalance in the plasminogen activator system, including inflammatory diseases, atherosclerosis, intimal hyperplasia, the response mechanism to vascular injury, and restenosis. uPA is implicated in the stimulation of angiogenesis, detailed overview | Mus musculus |
| malfunction | a wide variety of disorders are associated with an imbalance in the plasminogen activator system, including inflammatory diseases, atherosclerosis, intimal hyperplasia, the response mechanism to vascular injury, and restenosis. uPA is implicated in the stimulation of angiogenesis, detailed overview | Homo sapiens |
| malfunction | a wide variety of disorders are associated with an imbalance in the plasminogen activator system, including inflammatory diseases, atherosclerosis, intimal hyperplasia, the response mechanism to vascular injury, and restenosis. uPA is implicated in the stimulation of angiogenesis, detailed overview | Rattus norvegicus |
| physiological function | uPA is a multifunctional protein that in addition to its fibrinolytic and matrix degradation capabilities also affects growth factor bioavailability, cytokine modulation, receptor shedding, cell migration and proliferation, phenotypic modulation, protein expression, and cascade activation of proteases, inhibitors, receptors, and modulators. uPA is the crucial protein for neointimal growth and vascular remodeling. Mechanism of fibroblast-to-myofibroblast transformation induced by uPA. Detailed overview | Mus musculus |
| physiological function | uPA is a multifunctional protein that in addition to its fibrinolytic and matrix degradation capabilities also affects growth factor bioavailability, cytokine modulation, receptor shedding, cell migration and proliferation, phenotypic modulation, protein expression, and cascade activation of proteases, inhibitors, receptors, and modulators. uPA is the crucial protein for neointimal growth and vascular remodeling. Mechanism of fibroblast-to-myofibroblast transformation induced by uPA. Detailed overview | Homo sapiens |
| physiological function | uPA is a multifunctional protein that in addition to its fibrinolytic and matrix degradation capabilities also affects growth factor bioavailability, cytokine modulation, receptor shedding, cell migration and proliferation, phenotypic modulation, protein expression, and cascade activation of proteases, inhibitors, receptors, and modulators. uPA is the crucial protein for neointimal growth and vascular remodeling. Mechanism of fibroblast-to-myofibroblast transformation induced by uPA. Detailed overview | Rattus norvegicus |
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