Human glutathione S-transferases

doi:10.1016/0020-711X(94)90050-7

International Journal of Biochemistry

Volume 26, Issue 3, March 1994, Pages 295-308

https://doi.org/10.1016/0020-711X(94)90050-7 Get rights and content

Abstract

1.
1. Multiple forms of glutathione S-transferase (GST) isoenzymes present in human tissues are dimers of subunits belonging to three distinct gene families namely α, μ and π. Only the subunits within each class hybridize to give active dimers.
2.
2. These subunits are differentially expressed in a tissue-specific manner and the composition of glutathione S-transferases in various tissues differs significantly.
3.
3. Minor GST subunits not belonging to these three classes are also present in some tissues.
4.
4. An ortholog of rat GST 8-8 and mouse mGSTA4-4 is selectively expressed in some human tissues including bladder, brain, heart, liver, and pancreas. This isoenzyme designated as GST 5.8 expresses several fold higher activity towards 4-hydroxy-2,3-trans-nonenal as compared to the routinely used substrate 1-chloro-2,4-dinitrobenzene.

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