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Research ArticleArticle

Induction of Two UDP-Glucuronosyltransferase Isoforms Sensitive to Phenobarbital that are Involved in Morphine Glucuronidation

Production of Isoform-Selective Antipeptide Antibodies toward UGT1.1r and UGT2B1

Yuji Ishii, Atsuko Takami, Kazuoki Tsuruda, Akiko Kurogi, Hideyuki Yamada and Kazuta Oguri
Drug Metabolism and Disposition February 1997, 25 (2) 163-167;
Yuji Ishii
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Atsuko Takami
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Kazuoki Tsuruda
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Akiko Kurogi
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Hideyuki Yamada
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Kazuta Oguri
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Production of Isoform-Selective Antipeptide Antibodies toward UGT1.1r and UGT2B1

Abstract

We document here in that two UDP-glucuronosyltransferase (UGT) isoforms sensitive to phenobarbital are involved in morphine glucuronidation in Wistar and Sprague-Dawley rats. The hepatic microsomal morphine UGT activity in untreated Gunn rats was significantly less than that of untreated Wistar rats. Although the morphine UGT activity in the liver of Gunn rats was increased by phenobarbital (PB) treatment, this was significantly less than that in the liver of PB-treated Wistar rats. UGT1.1r is an isoform of morphine UGT in rat, and UGT2B1 is also considered an isoform of morphine UGT, because UGT2B1 (stably expressed in V79 cells) exhibited morphine UGT activity. We prepared specific antipeptide antibodies against UGT1.1r and UGT2B1. Using isoform-specific antipeptide antibodies, both UGT1.1r and UGT2B1 in Wistar and Sprague-Dawley rats were inducible by PB treatment. However, UGT1.1r is not present in the liver from Gunn rats. This study is the first demonstration that protein levels of two morphine UGT isoforms, UGT1.1r and UGT2B1, in the liver of Wistar and Sprague-Dawley rats are inducible by PB treatment.

Footnotes

  • Send reprint requests to: Dr. Kazuta Oguri, Faculty of Pharmaceutical Sciences, Kyushu University-62, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-82, Japan.

  • This work was supported in part by the Sasakawa Scientific Research Grant from the Japan Science Society. Presented at the 10th annual meeting of the Japanese Society for Xenobiotics, Ohmiya, Japan, November 1995 [Y. Ishii, A. Takami, K. Tsuruda, A. Kurogi, H. Yamada, and K. Oguri: Xenobiot. Metab. Dispos.10(Suppl.), 341 (abstr.) (1995)].

  • ↵2 A new nomenclature for the designation of UDP-glucuronosyltransferase (9) was used.

  • Abbreviations used are::
    M-3-G
    morphine-3-glucuronide
    M-6-G
    morphine-6-glucuronide
    UGT
    UDP-glucuronosyltransferase
    PB
    phenobarbital
    UGT1.1r and UGT2B1
    gene products of UGT1.1r and UGT2B1
    KLH
    Keyhole Limpet Hemocyanin
    BSA
    bovine serum albumin
    CH-Sepharose 4B
    ω-carboxypentylamino Sepharose 4B
    CNBr
    cyanide bromide
    IgG
    immunoglobulin G
    PBS
    phosphate-buffered saline
    SDS-PAGE
    sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    PVDF
    polyvinylidene difluoride
    SDS
    sodium dodecyl sulfate
    TBS-Triton
    Tris-buffered saline:Triton X-100
    ECL
    enhanced chemiluminescence
    RT-PCR
    reverse transcriptase-polymerase chain reaction
    MC
    3-methylcholanthrene
    • Received July 10, 1996.
    • Accepted November 13, 1996.
  • The American Society for Pharmacology and Experimental Therapeutics
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Drug Metabolism and Disposition
Vol. 25, Issue 2
1 Feb 1997
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Research ArticleArticle

Induction of Two UDP-Glucuronosyltransferase Isoforms Sensitive to Phenobarbital that are Involved in Morphine Glucuronidation

Yuji Ishii, Atsuko Takami, Kazuoki Tsuruda, Akiko Kurogi, Hideyuki Yamada and Kazuta Oguri
Drug Metabolism and Disposition February 1, 1997, 25 (2) 163-167;

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Research ArticleArticle

Induction of Two UDP-Glucuronosyltransferase Isoforms Sensitive to Phenobarbital that are Involved in Morphine Glucuronidation

Yuji Ishii, Atsuko Takami, Kazuoki Tsuruda, Akiko Kurogi, Hideyuki Yamada and Kazuta Oguri
Drug Metabolism and Disposition February 1, 1997, 25 (2) 163-167;
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