139446-70-1
Chemical Structure
PAI-1
- CAS No.: 139446-70-1
- Formula:C27H47N9O9S
- Molecular Weight:673.78
InChIKey: TYNGDHHMGWFOOJ-DYKIIFRCSA-N
SMILES: [H]N[C@H](C(N[C@@H](CCCNC(N)=N)C(N[C@H](C(N[C@H](C(N1CCC[C@H]1C(N[C@@H](CCC(O)=O)C(O)=O)=O)=O)C)=O)CCSC)=O)=O)C
Biological Activity: PAI-1 is a serine protease inhibitor (SERPIN). PAI-1 binds to and irreversibly inhibits uPA, tPA and furin; it also interacts with vitronectin, α1-acid glycoprotein, CRT, TLR4, proteasome α-3 subunit, uPAR, LRP1, Integrin αvβ3 and thrombin. PAI-1 regulates fibrinolysis, extracellular matrix turnover, cell migration, angiogenesis, inflammatory response and tissue remodeling; it mediates epithelial-mesenchymal transition (EMT)/endothelial-mesenchymal transition (EndMT), apoptosis and thrombus stabilization. PAI-1 can be used in research related to sepsis, acute lung injury, cardiovascular diseases, tissue fibrosis, diabetic nephropathy, obstructive nephropathy and non-insulin-dependent diabetes mellitus[1][2][3][4][5][6][7][8][9][10].
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PAI-1 | PAI-1 is a serine protease inhibitor (SERPIN). PAI-1 binds to and irreversibly inhibits uPA, tPA and furin; it also interacts with vitronectin, α1-acid glycoprotein, CRT, TLR4, proteasome α-3 subunit, uPAR, LRP1, Integrin αvβ3 and thrombin. PAI-1 regulates fibrinolysis, extracellular matrix turnover, cell migration, angiogenesis, inflammatory response and tissue remodeling; it mediates epithelial-mesenchymal transition (EMT)/endothelial-mesenchymal transition (EndMT), apoptosis and thrombus stabilization. PAI-1 can be used in research related to sepsis, acute lung injury, cardiovascular diseases, tissue fibrosis, diabetic nephropathy, obstructive nephropathy and non-insulin-dependent diabetes mellitus. | |||||||||||||||||||||
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References
- [1]. Park YJ, et al. PAI-1 inhibits neutrophil efferocytosis. Proceedings of the National Academy of Sciences of the United States of America. 2008 Aug 19;105(33):11784-9. [Content Brief]
- [2]. Sillen M, et al. Targeting PAI-1 in Cardiovascular Disease: Structural Insights Into PAI-1 Functionality and Inhibition. Frontiers in cardiovascular medicine. 2020;7:622473. [Content Brief]
- [3]. Ghosh AK, et al. PAI-1 in tissue fibrosis. Journal of cellular physiology. 2012 Feb;227(2):493-507. [Content Brief]
- [4]. Huang Y, Border WA, Yu L, Zhang J, Lawrence DA, Noble NA. A PAI-1 mutant, PAI-1R, slows progression of diabetic nephropathy. J Am Soc Nephrol. 2008 Feb;19(2):329-38. [Content Brief]
- [5]. Ehrlich HJ, et al. Functional interaction of plasminogen activator inhibitor type 1 (PAI-1) and heparin. Biochemistry. 1991 Jan 29;30(4):1021-8. [Content Brief]
- [6]. Oda T, et al. PAI-1 deficiency attenuates the fibrogenic response to ureteral obstruction. Kidney international. 2001 Aug;60(2):587-96. [Content Brief]
- [7]. Matsuo S, et al. Multifunctionality of PAI-1 in fibrogenesis: evidence from obstructive nephropathy in PAI-1-overexpressing mice. Kidney Int. 2005 Jun;67(6):2221-38. [Content Brief]
- [8]. Vaughan DE. PAI-1 and atherothrombosis. J Thromb Haemost. 2005 Aug;3(8):1879-83. [Content Brief]
- [9]. Tang Z, et al. Surface immobilization of a protease through an inhibitor-derived affinity ligand: a bioactive surface with defensive properties against an inhibitor. Chemical communications (Cambridge, England). 2015 Sep 28;51(75):14263-6. [Content Brief]
- [10]. Nordt TK, et al. Induction of plasminogen activator inhibitor type-1 (PAI-1) by proinsulin and insulin in vivo. Circulation. 1995 Feb 01;91(3):764-70. [Content Brief]
