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Diabetes 50:2013-2020, 2001
© 2001 by the American Diabetes Association, Inc.

Calpains Play a Role in Insulin Secretion and Action

Seamus K. Sreenan1, Yun-Ping Zhou1, Kenichi Otani1,8, Polly A. Hansen6, Kevin P.M. Currie2, Chien-Yuan Pan2, Jean-Pyo Lee1, Diane M. Ostrega1, William Pugh1, Yukio Horikawa3,5, Nancy J. Cox1,4, Craig L. Hanis7, Charles F. Burant6, Aaron P. Fox2, Graeme I. Bell1,3,4,5, and Kenneth S. Polonsky8

1 Medicine
2 Neurobiology, Pharmacology and Physiology
3 Biochemistry and Molecular Biology, and
4 Human Genetics, and the
5 Howard Hughes Medical Institute, the University of Chicago, Chicago, Illinois
6 Department of Cell Biology, Parke-Davis Pharmaceutical Research Division/Warner-Lambert Company, Ann Arbor, Michigan
7 Human Genetics Center, the University of Texas Health Science Center at Houston, Houston, Texas
8 Department of Medicine, Washington University, St. Louis, Missouri

Studies of the genetic basis of type 2 diabetes suggest that variation in the calpain-10 gene affects susceptibility to this common disorder, raising the possibility that calpain-sensitive pathways may play a role in regulating insulin secretion and/or action. Calpains are ubiquitously expressed cysteine proteases that are thought to regulate a variety of normal cellular functions. Here, we report that short-term (4-h) exposure to the cell-permeable calpain inhibitors calpain inhibitor II and E-64-d increases the insulin secretory response to glucose in mouse pancreatic islets. This dose-dependent effect is observed at glucose concentrations above 8 mmol/l. This effect was also seen with other calpain inhibitors with different mechanisms of action but not with cathepsin inhibitors or other protease inhibitors. Enhancement of insulin secretion with short-term exposure to calpain inhibitors is not mediated by increased responses in intracellular Ca2+ or increased glucose metabolism in islets but by accelerated exocytosis of insulin granules. In muscle strips and adipocytes, exposure to both calpain inhibitor II and E-64-d reduced insulin-mediated glucose transport. Incorporation of glucose into glycogen in muscle also was reduced. These results are consistent with a role for calpains in the regulation of insulin secretion and insulin action.


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Copyright © 2001 by the American Diabetes Association.