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Last update 08 May 2025

GSTO1

Last update 08 May 2025

Basic Info

Synonyms

glutathione S-transferase omega 1, Glutathione S-transferase omega 1-1, Glutathione S-transferase omega-1

+ [10]

Introduction

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.

Drugs associated with GSTO1

ML175

Target

GSTO1

Mechanism

GSTO1 inhibitors

Active Org.-

Originator Org.

The Scripps Research Institute

Active Indication-

Inactive Indication-

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with GSTO1

100 Translational Medicine associated with GSTO1

0 Patents (Medical) associated with GSTO1

361

Literatures (Medical) associated with GSTO1

01 Dec 2025·Functional & Integrative Genomics

N-glycosylation of GSTO1 promotes cervical cancer migration and invasion through JAK/STAT3 pathway activation

Article

Author: Qiao, Hui ; Sun, Chongfeng ; Zhao, Zouyu ; Diao, Bowen ; Yang, Ping ; Wang, Yan ; Sun, Qianyu ; Li, Hong ; Yu, Panpan

Protein glycosylation is strongly associated with tumor progression. Glutathione S-transferase omega 1 (GSTO1) is a member of the glutathione S-transferase family. The significance of GSTO1 N-glycosylation in the progression of cervical cancer (CC) has remained elusive. In this study, we investigated the functional significance of GSTO1 N-glycosylation in CC progression. We employed immunohistochemistry to detect the relative expression of evaluating the link between GSTO1 in CC and benign tissues and the overall survival (OS) and progression-free survival (PFS) in CC patients.In vitro and in vivo experiments to detect CC cell proliferation or metastatic ability after GSTO1 downregulation. NetNGly1.0 Server database predicts potential N-glycosylation modification sites of GSTO1 (Asn55, Asn135, Asn190). Investigating GSTO1 N-glycosylation's function in cellular migration, invasion and epithelial-mesenchymal transition (EMT), we mutated the N-glycosylation sites of GSTO1 through lentivirus-based insertional mutagenesis. Detection of signalling pathways associated with N-glycosylation-modified GSTO1 by enrichment analysis and Western blot. Compared to normal cervical tissue, CC tissue showed significantly higher GSTO1 expression. Further, high GSTO1 levels were a poor predictor of OS and PFS. Both cell and animal experiments suggested that down-regulation of GSTO1 inhibited cell proliferation and metastasis. Glycosylation modification of targeted mutant GSTO1 at positions 55, 135 and 190 significantly inhibits migration and invasion of CC cells. GSTO1 N-glycosylation fixed point mutation inhibits EMT process in CC cells. Mechanistically, N-glycosylated GSTO1 promoted the expression of JAK/STAT3 pathway related markers. GSTO1 N-glycosylation is associated with CC progression and may promote EMT via JAK/STAT3 signaling.

01 May 2025·Pathology - Research and Practice

Proteomic insights into lymph node metastasis in breast cancer subtypes: Key biomarkers and pathways

Article

Author: Canturk, Nuh Zafer ; Simsek, Turgay ; Bal Albayrak, Merve Gulsen ; Kasap, Murat ; Akpinar, Gurler

BACKGROUNDBreast cancer (BC) is a significant global cause of death in women, primarily due to its diversity and metastatic potential.METHODSBC, healthy lymph node (HL), and metastatic lymph node (ML) tissues were collected from 19 patients diagnosed with infiltrating ductal carcinoma. Protein isolation was performed, followed by two-dimensional gel electrophoresis (2DE) and mass spectrometry (MALDI-TOF/TOF) to identify differentially expressed proteins. Bioinformatic analyses, including protein-protein interaction networks and molecular pathways, were conducted using STRING. Kaplan-Meier analysis was performed with KM plotter to evaluate the prognostic significance of identified proteins. Receiver operating characteristic (ROC) curves were generated using TCGA and GTEx data from UCSC Xena and easyROC to assess diagnostic relevance.RESULTSDistinct pathways related to cytoskeletal regulation, immune modulation, and oxidative stress response were enriched in each subtype. Key proteins such as TUBA1C, CCT6A, and Vimentin (LNA), CAPZB and ENO1 (LNB), GSTO1 (HER2 OE), and CORO1A and LAP3 (TNBC) were identified as significant in driving metastatic behavior. KM survival analysis showed that CAPZB (LNB) and CORO1A (TNBC) were associated with patient outcomes, while GSTO1 was linked to improved distant metastasis-free survival in HER2 OE. ROC analysis highlighted CAPZB as a strong diagnostic marker.CONCLUSIONSThese findings form a basis for comprehending the molecular mechanisms underlying metastasis in different subtypes of breast cancer. They may lead to the identification of new therapeutic targets for customized interventions against invasion and metastasis. Further validation is required to confirm their clinical utility in larger cohorts.

01 Apr 2025·Neurochemical Research

FTO Suppresses Proliferation and Induces Apoptosis of T98G Glioblastoma Cells via N6-methyladenosine Modification of GSTO1

Article

Author: Yu, Zhenfei ; Qian, Xiaoling ; Mao, Jianhao ; Dong, Jinjiang ; Wu, Weihua

Glioblastoma (GBM) is the most malignant type of glioma with a very poor prognosis. N6-methyladenosine (m6A) is well-documented to be involved in GBM progression, and FTO is a demethylase. GSTO1 is also associated with tumor progression. This study aimed to investigate the impact of FTO and GSTO1 on GBM progression and the regulation of FTO on m6A modification of GSTO1. T98G cell phenotypes including proliferation and apoptosis were analyzed by cell counting kit 8, colony formation assay, and flow cytometry. The regulation of m6A methylation mediated by FTO was evaluated by methylated RNA immunoprecipitation, RNA immunoprecipitation, and dual-luciferase reporter assay. The results showed that FTO expression was downregulated in GBM. Overexpression of FTO inhibited cell proliferation and facilitated apoptosis in vitro. Additionally, GSTO1 expression was elevated in GBM, and knockdown of GSTO1 suppressed cell proliferation and promoted apoptosis and oxidative stress. Moreover, FTO inhibited m6A methylation of GSTO1 and reduced the stability of GSTO1. Overexpression of GSTO1 abrogated T98G cellular processes mediated by FTO. The in vivo experiments showed that FTO inhibited tumor growth by downregulating GSTO1 expression. In conclusion, FTO decelerates GBM progression by inducing apoptosis through suppressing m6A methylation of GSTO1.

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GSTO1

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