Product description |
Glutamate-cysteine ligase catalytic subunit (GCLC) catalyzes the ligation of glutamate and cysteine, the first and rate-limiting step in glutathione biosynthesis. Studies show that deubiquitinases protect cancer cells when glutathione synthesis is suppressed. Upon inhibition of both GCLC and deubiquitinases, cancer cells undergo proteotoxic stress, leading to cell death. In addition, deletion of Gclc enhances reactive oxygen species in mouse regulatory T cells (Tregs). Glutathione synthesized in part by Gclc is required for the suppressive function of mouse Tregs. Furthermore, in non-small cell lung cancer (NSCLC) cell lines, the transcription factor NRF2 stimulates GCLC expression. When NSCLC cells are starved for cysteine, GCLC, through its non-canonical activity, catalyzes the synthesis of γ-glutamyl-peptide, therefore reducing glutamate levels to protect cells against ferroptosis. |
Background |
Glutamate-cysteine ligase catalytic subunit (GCLC) catalyzes the ligation of glutamate and cysteine, the first and rate-limiting step in glutathione biosynthesis. Studies show that deubiquitinases protect cancer cells when glutathione synthesis is suppressed. Upon inhibition of both GCLC and deubiquitinases, cancer cells undergo proteotoxic stress, leading to cell death. In addition, deletion of Gclc enhances reactive oxygen species in mouse regulatory T cells (Tregs). Glutathione synthesized in part by Gclc is required for the suppressive function of mouse Tregs. Furthermore, in non-small cell lung cancer (NSCLC) cell lines, the transcription factor NRF2 stimulates GCLC expression. When NSCLC cells are starved for cysteine, GCLC, through its non-canonical activity, catalyzes the synthesis of γ-glutamyl-peptide, therefore reducing glutamate levels to protect cells against ferroptosis. |