Isozyme-specific fluorescent inhibitor of glutathione S -Transferase omega 1

Junghyun Son, Jae Jung Lee, Jun Seok Lee, Andreas Schller, Young Tae Chang

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)


Recently, the glutathione S-transferase omega 1 (GSTO1) is suspected to be involved in certain cancers and neurodegenerative diseases. However, profound investigation on the pathological roles of GSTO1 has been hampered by the lack of specific methods to determine or modulate its activity in biological systems containing other isoforms with similar catalytic function. Here, we report a fluorescent compound that is able to inhibit and monitor the activity of GSTO1. We screened 43 fluorescent chemicals and found a compound (6) that binds specifically to the active site of GSTO1. We observed that compound 6 inhibits GSTO1 by covalent modification but spares other isoforms in HEK293 cells and demonstrated that compound 6 could report the activity of GSTO1 in NIH/3T3 or HEK293 cells by measuring the fluorescence intensity of the labeled amount of GSTO1 in SDS?PAGE. Compound 6 is a useful tool to study GSTO1, applicable as a specific inhibitor and an activity reporter.

Original languageEnglish
Pages (from-to)449-453
Number of pages5
JournalACS Chemical Biology
Issue number5
Publication statusPublished - 2010 May 21
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine


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