H₂S- and Redox-State-Mediated PTP1B S-Sulfhydration in Insulin Signaling.

ABSTRACT: Because hydrogen sulfide (H₂S) is classified as a gaseous signaling molecule, protein S-sulfhydration is known to be one of the mechanisms by which H₂S signals are conducted. PTP1B, a negative regulator in insulin signaling, has been found to be S-sulfhydrated at Cys215-SH to form Cys215-SSH in response to endoplasmic reticulum (ER) stress. Therefore, we aimed to understand the change in PTP1B S-sulfhydration and cellular redox homeostasis in response to insulin stimulation. We demonstrated a feasible PEG-switch method to determine the levels of PTP1B S-sulfhydration. According to the results obtained from HEK293T and MDA-MB-231 cells, insulin induced a change in PTP1B S-sulfhydration that was similar to the change in Insulin receptor substrate 1 (IRS1) phosphorylatio

SUBMITTER: Lin YC 

PROVIDER: S-EPMC9917502 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature