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H2S- and Redox-State-Mediated PTP1B S-Sulfhydration in Insulin Signaling
Yu-Chin Lin1, Wan-Ting Zeng2, Der-Yen Lee2
1Ph.D. Program for Health Science and Industry, China Medical University, No. 91, Hsueh-Shih Road, Taichung 40402, Taiwan.
International Journal of Molecular Sciences
|February 11, 2023
Summary
Hydrogen sulfide (H2S) modulates protein PTP1B activity via S-sulfhydration, impacting insulin signaling. This study reveals how H2S and redox balance influence PTP1B during insulin stimulation.
Area of Science:
- Biochemistry
- Cell Biology
- Endocrinology
Background:
- Hydrogen sulfide (H2S) acts as a gaseous signaling molecule.
- Protein S-sulfhydration is a key H2S signaling mechanism.
- PTP1B, an insulin signaling inhibitor, undergoes S-sulfhydration at Cys215 in response to ER stress.
Purpose of the Study:
- To investigate alterations in PTP1B S-sulfhydration during insulin stimulation.
- To examine changes in cellular redox homeostasis in response to insulin.
- To understand the role of H2S in modulating PTP1B activity and insulin signaling.
Main Methods:
- Development of a PEG-switch assay to quantify PTP1B S-sulfhydration.
- Analysis of PTP1B S-sulfhydration and IRS1 phosphorylation in HEK293T and MDA-MB-231 cells.
- Assessment of cellular reactive oxygen species (ROS), H2S, glutathione (GSH), and glutathione disulfide (GSSG) levels.
Main Results:
- Insulin stimulation altered PTP1B S-sulfhydration similarly to IRS1 phosphorylation in both cell lines.
- Metformin significantly affected insulin-induced PTP1B S-sulfhydration and IRS1 phosphorylation only in HEK293T cells.
- Insulin increased ROS; H2S, GSH, and GSSG levels were modulated by insulin and metformin primarily in HEK293T cells.
Conclusions:
- PTP1B activity is regulated by H2S-mediated S-sulfhydration.
- Cellular redox state and H2S levels play a role in insulin signaling modulation.
- HEK293T cells exhibit distinct redox and H2S profiles compared to MDA-MB-231 cells.
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