Metrics
41 Record Views
Journal article
Oxidative stress inhibits calpain activity in situ
Journal of Biological Chemistry, Vol.273, pp.13331-13338
273
1998
PMID: 9582380
Web of Science ID: WOS:000073768500091
Abstract
In this study, the effects of oxidative stress on calpain-mediated proteolysis and calpain I autolysis in situ were examined. Calpain activity was stimulated in SH-SY5Y human neuroblastoma cells with the calcium ionophore, ionomycin. Calpain-mediated proteolysis of the membrane-permeable fluorescent substrate N-succinyl-L-leucyl-L-leucyl-L-valyl-L-tyrosine-7-amido-4-methylcoumarin, as well as the endogenous protein substrates microtubule-associated protein 2, tau and spectrin, was measured. Oxidative stress, induced by addition of either doxorubicin or 2-mercaptopyridine N-oxide, resulted in a significant decrease in the extent of ionophore-stimulated calpain activity of both the fluorescent compound and the endogenous substrates compared with control, normoxic conditions. Addition of glutathione ethyl ester, as well as other antioxidants, resulted in the retention/recovery of calpain activity, indicating that oxidation-induced calpain inactivation was preventable/reversible. The rate of autolytic conversion of the large subunit of calpain I from 80 to 78 to 76 kDa was decreased during oxidative stress; however, the extent of calpain autolysis was not altered. These data indicate that oxidative stress may reversibly inactivate calpain I in vivo.
Files and links (1)
Related links
Details
- Title
- Oxidative stress inhibits calpain activity in situ
- Publication Details
- Journal of Biological Chemistry, Vol.273, pp.13331-13338
- Resource Type
- Journal article
- Publisher
- The American Society for Biochemistry and Molecular Biology, Inc.; United States
- Series
- 273
- Format
- pdf
- Copyright
- This is an Open Access article under the CC BY license.
- Identifiers
- WOS:000073768500091; 99380090773806600
- Academic Unit
- Biology; Hal Marcus College of Science and Engineering
- Language
- English