ArticleNeurochemical research2004
In vitro proteolytic degradation of bovine brain calcineurin by m-calpain.
Article in Neurochemical research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 24 citations in OpenAlex.
- DYRK1A and Parkinson's disease, facts and hypotheses.Neurobiology of disease · 2026Review
- Calcineurin in cancer signaling networks.Nagoya journal of medical science · 2025Review
- Expression of calcineurin, calpastatin and heat shock proteins during ischemia and reperfusion.Biochemistry and biophysics reports · 2015Article
- Proteases in cardiometabolic diseases: Pathophysiology, molecular mechanisms and clinical applications.Biochimica et biophysica acta · 2015Review
- Tear me down: role of calpain in the development of cardiac ventricular hypertrophy.Circulation research · 2011Review
- Molecular cloning and biochemical characterization of bovine retina calcineurin.Molecular and cellular biochemistry · 2010Article
- Calpain-mediated signaling mechanisms in neuronal injury and neurodegeneration.Molecular neurobiology · 2008Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A major cause of neuronal dysfunction is due to altered Ca2+ regulation. An increase in Ca2+ influx can activate Ca2+-dependent enzymes including calpains, causing the proteolysis of its specific substrates. In the present study, calcineurin (CaN) was found to be proteolysed by a Ca2+-dependent cysteine protease, m-calpain. In the presence of Ca2+, the 60 kDa subunit (CaN A) was degraded to a 46 kDa immunoreactive fragment, whereas in the presence of Ca2+ /calmodulin (CaM) immunoreactive fragments of 48 and 54 kDa were observed. The beta-subunit (CaN B) was not proteolysed in either condition. The proteolysis of CaN A increased its phosphatase activity and rendered it totally CaM-independent after 10 min of proteolysis. The molecular weight of the proteolytic fragments suggested that the m-calpain cleaved CaN A in the CaN B binding domain. A CaM-overlay experiment revealed that the CaM-binding site was present only in the 54 kDa fragment produced by CaN A proteolysis in the presence of Ca2+ /CaM. Thus, the increase in CaN A phosphatase activity observed in many neuronal disorders, may be due to the action of calpain.
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Registered trials
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