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Inhibition of glutathione S-transferase omega 1-catalyzed protein deglutathionylation suppresses adipocyte differentiation.


ABSTRACT: Glutathione S-transferase omega 1 (GstO1) is closely associated with various human diseases, including obesity and diabetes, but its functional mechanism is not fully understood. In the present study, we found that the GstO1-specific inhibitor C1-27 effectively suppressed the adipocyte differentiation of 3T3-L1 preadipocytes. GstO1 expression was immediately upregulated upon the induction of adipocyte differentiation, and barely altered by C1-27. However, C1-27 significantly decreased the stability of GstO1. Moreover, GstO1 catalyzed the deglutathionylation of cellular proteins during the early phase of adipocyte differentiation, and C1-27 inhibited this activity. These results demonstrate that GstO1 is involved in adipocyte differentiation by catalyzing the deglutathionylation of proteins critical for the early phase of adipocyte differentiation. [BMB Reports 2023; 56(8): 457-462].

SUBMITTER: Iram S 

PROVIDER: S-EPMC10471458 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature

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Inhibition of glutathione S-transferase omega 1-catalyzed protein deglutathionylation suppresses adipocyte differentiation.

Iram Sana S   Mashaal Areeba A   Go Seulgi S   Kim Jihoe J  

BMB reports 20230801 8


Glutathione S-transferase omega 1 (GstO1) is closely associated with various human diseases, including obesity and diabetes, but its functional mechanism is not fully understood. In the present study, we found that the GstO1-specific inhibitor C1-27 effectively suppressed the adipocyte differentiation of 3T3-L1 preadipocytes. GstO1 expression was immediately upregulated upon the induction of adipocyte differentiation, and barely altered by C1-27. However, C1-27 significantly decreased the stabil  ...[more]

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