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redox regulation of insulin degradation by insulin-degrading enzyme氧化还原调控胰岛素降解酶降解
Redox Regulation of Insulin Degradation by
Insulin-Degrading Enzyme
Crystal M. Cordes1,3, Robert G. Bennett1,2,4, Gerri L. Siford1,2, Frederick G. Hamel1,2,3*
1 Research Service, Omaha Veterans Affairs Medical Center, Omaha, Nebraska, United States of America, 2 Department of Internal Medicine, University of Nebraska
Medical Center, Omaha, Nebraska, United States of America, 3 Department of Pharmacology and Experimental Neuroscience, University of Nebraska Medical Center,
Omaha, Nebraska, United States of America, 4 Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, United States
of America
Abstract
Insulin-degrading enzyme (IDE) is a thiol sensitive peptidase that degrades insulin and amyloid b, and has been linked to
type 2 diabetes mellitus and Alzheimer’s disease. We examined the thiol sensitivity of IDE using S-nitrosoglutathione,
reduced glutathione, and oxidized glutathione to distinguish the effects of nitric oxide from that of the redox state. The in
vitro activity of IDE was studied using either partially purified cytosolic enzyme from male Sprague-Dawley rats, or purified
rat recombinant enzyme. We confirm that nitric oxide inhibits the degrading activity of IDE, and that it affects proteasome
activity through this interaction with IDE, but does not affect the proteasome directly. Oxidized glutathione inhibits IDE
through glutathionylation, which was reversible by dithiothreitol but not by ascorbic acid. Reduced glutathione had no
effect on IDE, but reacted with partially degraded insulin to disrupt its disulfide bonds and accelerate its breakdown to
trichloroacetic acid soluble fragments. Our results demonstrate the sensitivity of insulin degradation by IDE to the redox
environment and suggest another mechanism by which the cell’s oxidation state may c
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