Insulin-degrading enzyme is exported via an unconventional protein secretion pathway
2009
Insulin-degrading enzyme is exported via an unconventional protein secretion pathway
publication
Evidence: moderate
Author Information
Author(s): Zhao Ji, Li Lilin, Leissring Malcolm A
Primary Institution: The Scripps Research Institute
Hypothesis
Does insulin-degrading enzyme (IDE) secretion occur via the classical secretion pathway?
Conclusion
The study found that IDE secretion is not dependent on the classical secretion pathway, identifying it as an unconventionally secreted protein.
Supporting Evidence
- IDE secretion was unaffected by classical secretion inhibitors like brefeldin A, monensin, or nocodazole.
- IDE secretion was similarly unaffected by stimulators of protein secretion such as glyburide and Bz-ATP.
- The calcium ionophore A23187 increased extracellular IDE activity but was also cytotoxic.
Takeaway
The insulin-degrading enzyme, which helps break down insulin and other important proteins, is released from cells in a way that doesn't follow the usual rules for protein secretion.
Methodology
The study used cell-based assays to investigate the effects of various inhibitors and stimulators on IDE secretion from murine hepatocytes and HeLa cells.
Statistical Information
P-Value
p<0.01
Statistical Significance
p<0.01
Digital Object Identifier (DOI)
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