Please use this identifier to cite or link to this item: https://doi.org/10.1021/cb100007s
Title: Isozyme-specific fluorescent inhibitor of glutathione S -Transferase omega 1
Authors: Son, J.
Lee, J.-J.
Lee, J.-S.
Schller, A.
Chang, Y.-T. 
Issue Date: 21-May-2010
Citation: Son, J., Lee, J.-J., Lee, J.-S., Schller, A., Chang, Y.-T. (2010-05-21). Isozyme-specific fluorescent inhibitor of glutathione S -Transferase omega 1. ACS Chemical Biology 5 (5) : 449-453. ScholarBank@NUS Repository. https://doi.org/10.1021/cb100007s
Abstract: 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. © 2010 American Chemical Society.
Source Title: ACS Chemical Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/76420
ISSN: 15548929
DOI: 10.1021/cb100007s
Appears in Collections:Staff Publications

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