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Rapid CommunicationShort Communication

Characterization of Microsomal Glutathione S-Transferases MGST1, MGST2, and MGST3 in Cynomolgus Macaque

Yasuhiro Uno, Norie Murayama, Mutsuki Kunori and Hiroshi Yamazaki
Drug Metabolism and Disposition September 2013, 41 (9) 1621-1625; DOI: https://doi.org/10.1124/dmd.113.052977
Yasuhiro Uno
Pharmacokinetics and Bioanalysis Center, Shin Nippon Biomedical Laboratories, Ltd., Kainan, Japan (Y.U.); and Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Tokyo, Japan (N.M., M.K., H.Y.)
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Norie Murayama
Pharmacokinetics and Bioanalysis Center, Shin Nippon Biomedical Laboratories, Ltd., Kainan, Japan (Y.U.); and Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Tokyo, Japan (N.M., M.K., H.Y.)
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Mutsuki Kunori
Pharmacokinetics and Bioanalysis Center, Shin Nippon Biomedical Laboratories, Ltd., Kainan, Japan (Y.U.); and Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Tokyo, Japan (N.M., M.K., H.Y.)
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Hiroshi Yamazaki
Pharmacokinetics and Bioanalysis Center, Shin Nippon Biomedical Laboratories, Ltd., Kainan, Japan (Y.U.); and Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Tokyo, Japan (N.M., M.K., H.Y.)
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Abstract

The glutathione S-transferase (GST) family comprises cytosolic, mitochondrial, and microsomal GSTs, all essential enzymes that metabolize a wide range of endogenous and exogenous substrates. Among the microsomal GSTs (MGSTs) in humans, MGST1, MGST2, and MGST3 are involved in detoxification; however, MGSTs have not been fully investigated in cynomolgus macaque, an important primate species widely used in drug metabolism and toxicity studies. In the present study, cynomolgus MGST2 and MGST3 cDNAs were isolated from liver tissue and characterized along with previously isolated cynomolgus MGST1. For comparison with the cynomolgus cDNAs, MGST2 and MGST3 cDNAs were also isolated from rhesus macaque (closely related to cynomolgus macaque) liver. Cynomolgus MGST2 and MGST3, respectively, were highly identical (99 and 98%) to human MGST2 and MGST3 and nearly identical to the amino acid sequences of the rhesus orthologs, and they were closely clustered with human MGST2 and MGST3 by phylogenetic analysis. The analysis of genome data indicated that MGST1, MGST2, and MGST3, respectively, had similar gene structures and genomic organization in macaque and human. Therefore, cynomolgus MGSTs have molecular similarities to the corresponding human MGSTs. Cynomolgus MGST2 and MGST3 were expressed in liver, jejunum, and kidney, but at lower levels than MGST1. GST activities were measured with 1-chloro-2,4-dinitrobenzene and 1,2-epoxy-3-(p-nitrophenoxy)propane as substrates, using proteins heterologously expressed in Escherichia coli. Cynomolgus MGST1, MGST2, and MGST3 conjugated 1-chloro-2,4-dinitrobenzene and 1,2-epoxy-3-(p-nitrophenoxy)propane, indicating that cynomolgus MGST1, MGST2, and MGST3 are functional enzymes. These results suggest that these functional cynomolgus MGST enzymes and the corresponding human MGSTs are molecularly similar.

Footnotes

    • Received May 15, 2013.
    • Accepted June 19, 2013.
  • dx.doi.org/10.1124/dmd.113.052977.

  • ↵Embedded ImageThis article has supplemental material available at dmd.aspetjournals.org.

  • Copyright © 2013 by The American Society for Pharmacology and Experimental Therapeutics
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Drug Metabolism and Disposition: 41 (9)
Drug Metabolism and Disposition
Vol. 41, Issue 9
1 Sep 2013
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Rapid CommunicationShort Communication

Characterization of Cynomolgus MGSTs

Yasuhiro Uno, Norie Murayama, Mutsuki Kunori and Hiroshi Yamazaki
Drug Metabolism and Disposition September 1, 2013, 41 (9) 1621-1625; DOI: https://doi.org/10.1124/dmd.113.052977

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Rapid CommunicationShort Communication

Characterization of Cynomolgus MGSTs

Yasuhiro Uno, Norie Murayama, Mutsuki Kunori and Hiroshi Yamazaki
Drug Metabolism and Disposition September 1, 2013, 41 (9) 1621-1625; DOI: https://doi.org/10.1124/dmd.113.052977
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