The DOI matches its Crossref record; 111 of the 111 references it cites were found in a registry or an index.
Calpains — An elaborate proteolytic system
Open accessAbstract
Calpain is an intracellular Ca(2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02). Recent expansion of sequence data across the species definitively shows that calpain has been present throughout evolution; calpains are found in almost all eukaryotes and some bacteria, but not in archaebacteria. Fifteen genes within the human genome encode a calpain-like protease domain. Interestingly, some human calpains, particularly those with non-classical domain structures, are very similar to calpain homologs identified in evolutionarily distant organisms. Three-dimensional structural analyses have helped to identify calpain's unique mechanism of activation; the calpain protease domain comprises two core domains that fuse to form a functional protease only when bound to Ca(2+)via well-conserved amino acids. This finding highlights the mechanistic characteristics shared by the numerous calpain homologs, despite the fact that they have divergent domain structures. In other words, calpains function through the same mechanism but are regulated independently. This article reviews the recent progress in calpain research, focusing on those studies that have helped to elucidate its mechanism of action. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome.
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Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus
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Cited by
Mahaman, Y. A. R., Huang, F., Wu, M., Wang, Y., Wei, Z., Bao, J., Salissou, M. T. M., Ke, D., Wang, Q., Liu, R., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180091 · Cited by 93
Chelko, S. P., Keceli, G., Carpi, A., Doti, N., Agrimi, J., Asimaki, A., Beti, C. B., Miyamoto, M., Amat-Codina, N., Bedja, D., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf0891 · Cited by 92
S-acylation regulates the membrane association and activity of Calpain-5
Gal, J., Bondada, V., Mashburn, C. B., Rodgers, D. W., Croall, D. E., & Geddes, J. W. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119298 · Cited by 8
Ye, Q., Henrickson, A., Demeler, B., Balasco Serrão, V. H., & Davies, P. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108133 · Cited by 4
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Metadata
- Authors
- Ono, Y., & Sorimachi, H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2012-01
- Volume
- 1824
- Issue
- 1
- Pages
- 224-236
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W1997151018
- Cited by
- 349
- References
- 111
- FWCI
- 7.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
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