The Mammalian Cysteine Protease Legumain in Health and Disease
Abstract
:1. Introduction
1.1. Legumain Expression and Synthesis
1.2. Legumain Structure and Activity
1.3. Regulation of Legumain Transcription
Legumain Substrate | Result of Substrate Cleavage by Legumain | Reference |
---|---|---|
Acetoacetyl-CoA synthetase | Degradation | [27] |
A disintegrin and metalloproteinase (ADAM) 10 and 17 | Degradation | [28] |
Alpha-1-macroglobulin | Activation | [29] |
Alpha (α)-synuclein | Processing | [30,31] |
Amphiphysin I | Processing | [32] |
Amyloid precursor protein (APP) | Processing | [33] |
Annexin A2 | Degradation | [34,35] |
Beta-amyloid protein 1–40 | n/a | [29] |
Betaine-homocysteine S-methyltransferase 1 | Degradation | [36] |
Cathepsin B, H, L | Processing | [37] |
Cofilin-1 | Processing | [38] |
Cystatin C and E/M | Processing | [39] |
Fibronectin | Degradation | [40,41] |
Forkhead box P3 (FOXP3) | Degradation | [42] |
Inhibitor 2 of protein phosphatase 2 (I2PP2A)/SET | Degradation | [43,44] |
Invariant chain chaperone (li) | Processing | [45] |
Myelin basic protein (MBP) | Processing/degradation | [46,47] |
p53 | Degradation | [48] |
Promatrix metalloproteinase 2 (proMMP-2) | Activation | [49] |
Prolegumain | Autoactivation | [9,14,15] |
Prothymosin α | Processing | [50] |
Serotransferrin | n/a | [29] |
Serum albumin | n/a | [29] |
Serin/treonin protein kinase 2 (SRPK2) | Activation | [51] |
Synaptojanin 1 (SYNJ1) | Processing | [52] |
TAR DNA-binding protein 43 (TDP-43) | Processing | [53] |
Tau | Processing | [51,54,55,56,57] |
Toll-like receptor 7 (TLR7) | Processing | [58] |
Toll-like receptor 9 (TLR9) | Processing | [59,60,61] |
Tropomodulin-3 (Tmod-3) | Processing | [62] |
Vitamin-D-binding protein (VDBP) | Degradation | [35] |
1.4. Legumain Cellular Localization and Substrates
1.5. Endogenous Legumain Inhibitors
2. Role of Legumain in Kidney Homeostasis
3. Role of Legumain in Regulation of Hematopoietic Homeostasis
4. Role of Legumain in Bone Remodeling
5. Role of Legumain in Vascular Homeostasis, Cardiovascular, and Cerebrovascular Diseases
6. Role of Legumain in Fibrosis
7. Role of Legumain in Age-Related Tissue Senescence
8. Role of Legumain in Neurodegenerative Diseases
9. Role of Legumain in Cancer
10. Pharmacological Inhibition of Legumain
11. Conclusions
Funding
Conflicts of Interest
References
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Solberg, R.; Lunde, N.N.; Forbord, K.M.; Okla, M.; Kassem, M.; Jafari, A. The Mammalian Cysteine Protease Legumain in Health and Disease. Int. J. Mol. Sci. 2022, 23, 15983. https://doi.org/10.3390/ijms232415983
Solberg R, Lunde NN, Forbord KM, Okla M, Kassem M, Jafari A. The Mammalian Cysteine Protease Legumain in Health and Disease. International Journal of Molecular Sciences. 2022; 23(24):15983. https://doi.org/10.3390/ijms232415983
Chicago/Turabian StyleSolberg, Rigmor, Ngoc Nguyen Lunde, Karl Martin Forbord, Meshail Okla, Moustapha Kassem, and Abbas Jafari. 2022. "The Mammalian Cysteine Protease Legumain in Health and Disease" International Journal of Molecular Sciences 23, no. 24: 15983. https://doi.org/10.3390/ijms232415983