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Mice Lacking Thioredoxin-interacting Protein Provide Evidence Linking Cellular Redox State to Appropriate Response to
 

Summary: Mice Lacking Thioredoxin-interacting Protein Provide Evidence
Linking Cellular Redox State to Appropriate Response to
Nutritional Signals*
Received for publication, February 5, 2004, and in revised form, March 24, 2004
Published, JBC Papers in Press, March 26, 2004, DOI 10.1074/jbc. M401280200
To Yuen Hui, Sonal S. Sheth§, J. Matthew Diffley, Douglas W. Potter, Aldons J. Lusis§,
Alan D. Attie¶, and Roger A. Davis
From the Mammalian Cell and Molecular Biology Laboratory, Department of Biology, Molecular Biology Institute and
Heart Institute, San Diego State University, San Diego, California 92182, §Molecular Biology Institute and Department
of Medicine, Microbiology and Human Genetics, University of California, Los Angeles, California 90095, and
¶Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706
Thioredoxin-interacting protein (Txnip) is a ubiqui-
tous protein that binds with high affinity to thioredoxin
and inhibits its ability to reduce sulfhydryl groups via
NADPH oxidation. HcB-19 mice contain a nonsense mu-
tation in Txnip that eliminates its expression. Unlike
normal animals, HcB-19 mice have 3-fold increase in
insulin levels when fasted. The C-peptide/insulin ratio is
normal, suggesting that the hyperinsulinemia is due to
increased insulin secretion. Fasted HcB-19 mice are hy-

  

Source: Attie, Alan D. - Department of Biochemistry, University of Wisconsin at Madison

 

Collections: Biology and Medicine