リケラボ論文検索は、全国の大学リポジトリにある学位論文・教授論文を一括検索できる論文検索サービスです。

リケラボ 全国の大学リポジトリにある学位論文・教授論文を一括検索するならリケラボ論文検索大学・研究所にある論文を検索できる

リケラボ 全国の大学リポジトリにある学位論文・教授論文を一括検索するならリケラボ論文検索大学・研究所にある論文を検索できる

大学・研究所にある論文を検索できる 「Use of a Baculovirus-Mammalian Cell Expression-System for Expression of Drug-Metabolizing Enzymes: Optimization of Infection With a Focus on Cytochrome P450 3A4」の論文概要。リケラボ論文検索は、全国の大学リポジトリにある学位論文・教授論文を一括検索できる論文検索サービスです。

コピーが完了しました

URLをコピーしました

論文の公開元へ論文の公開元へ
書き出し

Use of a Baculovirus-Mammalian Cell Expression-System for Expression of Drug-Metabolizing Enzymes: Optimization of Infection With a Focus on Cytochrome P450 3A4

Miyauchi, Yuu 宮内, 優 Kimura, Akane 木村, 茜 キムラ, アカネ Sawai, Madoka サワイ, マドカ Fujimoto, Keiko 藤本, 景子 フジモト, ケイコ Hirota, Yuko 廣田, 有子 ヒロタ, ユウコ Tanaka, Yoshitaka 田中, 嘉孝 タナカ, ヨシタカ Takechi, Shinji 武知, 進士 タケチ, シンジ Mackenzie, Peter I. Ishii, Yuji 石井, 祐次 九州大学

2022.02.22

概要

Heterologous expression systems are important for analyzing the effects of genetic factors including single nucleotide polymorphisms on the functions of drug-metabolizing enzymes. In this study, we fo

この論文で使われている画像

参考文献

UGT1A1/7 Variants. Drug Metab. Dispos. 42, 229–238. doi:10.1124/dmd.113.

054833

Ishii, Y., Takeda, S., and Yamada, H. (2010). Modulation of UDPGlucuronosyltransferase Activity by Protein-Protein Association. Drug

Metab. Rev. 42, 145–158. doi:10.3109/03602530903208579

Jarvis, D. L. (2003). Developing Baculovirus-Insect Cell Expression Systems for

Humanized Recombinant Glycoprotein Production. Virology 310, 1–7. doi:10.

1016/s0042-6822(03)00120-x

Khan, K. H. (2013). Gene Expression in Mammalian Cells and its Applications.

Adv. Pharm. Bull. 3, 257–263. doi:10.5681/apb.2013.042

Kruh, J. (1982). Effects of Sodium Butyrate, a New Pharmacological Agent, on Cells

in Culture. Mol. Cel. Biochem. 42, 65–82. doi:10.1007/BF00222695

Kumondai, M., Hishinuma, E., Gutiérrez Rico, E. M., Ito, A., Nakanishi, Y.,

Saigusa, D., et al. (2020). Heterologous Expression of High-Activity

Cytochrome P450 in Mammalian Cells. Sci. Rep. 10, 14193. doi:10.1038/

s41598-020-71035-5

Kusano, K., Waterman, M. R., Sakaguchi, M., Omura, T., and Kagawa, N. (1999).

Protein Synthesis Inhibitors and Ethanol Selectively Enhance Heterologous

Expression of P450s and Related Proteins in Escherichia C. Arch. Biochem.

Biophys. 367, 129–136. doi:10.1006/abbi.1999.1248

Luckow, V. A. (1993). Baculovirus Systems for the Expression of Human Gene

Products. Curr. Opin. Biotechnol. 4, 564–572. doi:10.1016/0958-1669(93)

90078-b

Mackenzie, P. I. (1986). Rat Liver UDP-Glucuronosyltransferase. cDNA Sequence

and Expression of a Form Glucuronidating 3-Hydroxyandrogens. J. Biol. Chem.

261, 14112–14117. doi:10.1016/s0021-9258(18)66989-3

Mackenzie, P. I. (1990). The Effect of N-Linked Glycosylation on the Substrate

Preferences of UDP Glucuronosyltransferases. Biochem. Biophys. Res.

Commun. 166, 1293–1299. doi:10.1016/0006-291x(90)91006-e

Makkonen, K. E., Airenne, K., and Ylä-Herttulala, S. (2015). Baculovirus-Mediated

Gene Delivery and RNAi Applications. Viruses 7, 2099–2125. doi:10.3390/

v7042099

Marchal, I., Jarvis, D. L., Cacan, R., and Verbert, A. (2001). Glycoproteins from

Insect Cells: Sialylated or Not? Biol. Chem. 382, 151–159. doi:10.1515/BC.

2001.023

Miyauchi, Y., Kurita, A., Yamashita, R., Takamatsu, T., Ikushiro, S., Mackenzie, P.

I., et al. (2020a). Hetero-oligomer Formation of Mouse UDPGlucuronosyltransferase (UGT) 2b1 and 1a1 Results in the Gain of

Glucuronidation Activity towards Morphine, an Activity Which Is Absent

in Homo-Oligomers of Either UGT. Biochem. Biophys. Res. Commun. 525,

348–353. doi:10.1016/j.bbrc.2020.02.075

Miyauchi, Y., Kurohara, K., Kimura, A., Esaki, M., Fujimoto, K., Hirota, Y., et al.

(2020b). The Carboxyl-Terminal Di-lysine Motif Is Essential for Catalytic

Activity of UDP-Glucuronosyltransferase 1A9. Drug Metab. Pharmacokinet.

35, 466–474. doi:10.1016/j.dmpk.2020.07.006

Miyauchi, Y., Nagata, K., Yamazoe, Y., Mackenzie, P. I., Yamada, H., and Ishii, Y.

(2015). Suppression of Cytochrome P450 3A4 Function by UDPGlucuronosyltransferase 2B7 through a Protein-Protein Interaction:

Cooperative Roles of the Cytosolic Carboxyl-Terminal Domain and the

Luminal Anchoring Region. Mol. Pharmacol. 88, 800–812. doi:10.1124/mol.

115.098582

Miyauchi, Y., Takechi, S., and Ishii, Y. (2021). Functional Interaction between

Cytochrome P450 and UDP-Glucuronosyltransferase on the Endoplasmic

Reticulum Membrane: One of post-translational Factors Which Possibly

Contributes to Their Inter-Individual Differences. Biol. Pharm. Bull. 44,

1635–1644. doi:10.1248/bpb.b21-00286

Miyauchi, Y., Yamada, H., and Ishii, Y. (2019). Advantage of a Co-Expression

System for Estimating Physiological Effects of Functional Interaction between

Cytochrome P450 3A4 and Uridine 5’-Diphospho-Glucuronosyltransferase

2B7. BPB Rep. 2, 61–66. doi:10.1248/bpbreports.2.5_61

Morales-Perez, C. L., Noviello, C. M., and Hibbs, R. E. (2016). Manipulation of

Subunit Stoichiometry in Heteromeric Membrane Proteins. Structure 24,

797–805. doi:10.1016/j.str.2016.03.004

Nagaoka, K., Hanioka, N., Ikushiro, S., Yamano, S., and Narimatsu, S. (2012). The

Effects of N-Glycosylation on the Glucuronidation of Zidovudine and

Morphine by UGT2B7 Expressed in HEK293 Cells. Drug Metab.

Pharmacokinet. 27, 388–397. doi:10.2133/dmpk.dmpk-11-rg-135

Aoyama, K., Yoshinari, K., Kim, H. J., Nagata, K., and Yamazoe, Y. (2009).

Simultaneous Expression of Plural Forms of Human Cytochrome P450 at

Desired Ratios in HepG2 Cells: Adenovirus-Mediated Tool for Cytochrome

P450 Reconstitution. Drug Metab. Pharmacokinet. 24, 209–217. doi:10.2133/

dmpk.24.209

Asseffa, A., Smith, S. J., Nagata, K., Gillette, J., Gelboin, H. V., and Gonzalez, F. J.

(1989). Novel Exogenous Heme-Dependent Expression of Mammalian

Cytochrome P450 Using Baculovirus. Arch. Biochem. Biophys. 274, 481–490.

doi:10.1016/0003-9861(89)90461-x

Backes, W. L., and Kelley, R. W. (2003). Organization of Multiple Cytochrome

P450s with NADPH-Cytochrome P450 Reductase in Membranes. Pharmacol.

Ther. 98, 221–233. doi:10.1016/s0163-7258(03)00031-7

Barbier, O., Girard, C., Breton, R., Bélanger, A., and Hum, D. W. (2000).

N-Glycosylation and Residue 96 Are Involved in the Functional Properties

of UDP-Glucuronosyltransferase Enzymes. Biochemistry 39, 11540–11552.

doi:10.1021/bi000779p

Boyce, F. M., and Bucher, N. L. (1996). Baculovirus-Mediated Gene Transfer into

Mammalian Cells. Proc. Natl. Acad. Sci. U. S. A. 93, 2348–2352. doi:10.1073/

pnas.93.6.2348

Clark, B. J., and Waterman, M. R. (1991). Heterologous Expression of Mammalian

P450 in COS Cells. Methods Enzymol. 206, 100–108. doi:10.1016/00766879(91)06081-d

Condreay, J. P., Witherspoon, S. M., Clay, W. C., and Kost, T. A. (1999). Transient

and Stable Gene Expression in Mammalian Cells Transduced with a

Recombinant Baculovirus Vector. Proc. Natl. Acad. Sci. U. S. A. 96,

127–132. doi:10.1073/pnas.96.1.127

Court, M. H. (2010). Interindividual Variability in Hepatic Drug Glucuronidation:

Studies into the Role of Age, Sex, Enzyme Inducers, and Genetic Polymorphism

Using the Human Liver Bank as a Model System. Drug Metab. Rev. 42, 209–224.

doi:10.3109/03602530903209288

Crespi, C. L., and Miller, V. P. (1999). The Use of Heterologously Expressed Drug

Metabolizing Enzymes-State of the Art and Prospects for the Future.

Pharmacol. Ther. 84, 121–131. doi:10.1016/s0163-7258(99)00028-5

Duisit, G., Saleun, S., Douthe, S., Barsoum, J., Chadeuf, G., and Moullier, P. (1999).

Baculovirus Vector Requires Electrostatic Interactions Including Heparan

Sulfate for Efficient Gene Transfer in Mammalian Cells. J. Gene Med. 1,

93–102.

doi:10.1002/(SICI)1521-2254(199903/04)1:2<93:AID-JGM19>3.0.

CO;2-1

Evans, W. E., and Relling, M. V. (1999). Pharmacogenomics: Translating

Functional Genomics into Rational Therapeutics. Science 286, 487–491.

doi:10.1126/science.286.5439.487

Finel, M., and Kurkela, M. (2008). The UDP-Glucuronosyltransferases as

Oligomeric Enzymes. Curr. Drug Metab. 9, 70–76. doi:10.2174/

138920008783331158

Gluzman, Y. (1981). SV40-Transformed Simian Cells Support the Replication of

Early SV40 Mutants. Cell 23, 175–182. doi:10.1016/0092-8674(81)90282-8

Gorman, C. M., Howard, B. H., and Reeves, R. (1983). Expression of Recombinant

Plasmids in Mammalian Cells Is Enhanced by Sodium Butyrate. Nucleic Acids

Res. 11, 7631–7648. doi:10.1093/nar/11.21.7631

Guengerich, F. P. (2006). Cytochrome P450s and Other Enzymes in Drug

Metabolism and Toxicity. AAPS J. 8, E101–E111. doi:10.1208/aapsj080112

Guengerich, F. P., Parikh, A., Johnson, E. F., Richardson, T. H., Von Wachenfeldt,

C., Cosme, J., et al. (1997). Heterologous Expression of Human DrugMetabolizing Enzymes. Drug Metab. Dispos. 25, 1234–1241.

Hofmann, C., Sandig, V., Jennings, G., Rudolph, M., Schlag, P., and Strauss, M.

(1995). Efficient Gene Transfer into Human Hepatocytes by Baculovirus

Vectors. Proc. Natl. Acad. Sci. U. S. A. 92, 10099–10103. doi:10.1073/pnas.

92.22.10099

Hu, Y. C. (2005). Baculovirus as a Highly Efficient Expression Vector in Insect and

Mammalian Cells. Acta Pharmacol. Sin. 26, 405–416. doi:10.1111/j.1745-7254.

2005.00078.x

Ishii, Y., Koba, H., Kinoshita, K., Oizaki, T., Iwamoto, Y., Takeda, S., et al. (2014).

Alteration of the Function of the UDP-Glucuronosyltransferase 1A Subfamily

by Cytochrome P450 3A4: Different Susceptibility for UGT Isoforms and

Frontiers in Pharmacology | www.frontiersin.org

February 2022 | Volume 13 | Article 832931

Miyauchi et al.

Bac-Mam System for Drug-Metabolizing Enzymes

To-Phenotype Studies. Pharmacogenomics J. 2, 48–56. doi:10.1038/sj.tpj.

6500089

Volkman, L. E., and Goldsmith, P. A. (1983). In Vitro Survey of Autographa Californica

Nuclear Polyhedrosis Virus Interaction with Nontarget Vertebrate Host Cells. Appl.

Environ. Microbiol. 45, 1085–1093. doi:10.1128/AEM.45.3.1085-1093.1983

Zanger, U. M., and Schwab, M. (2013). Cytochrome P450 Enzymes in Drug Metabolism:

Regulation of Gene Expression, Enzyme Activities, and Impact of Genetic Variation.

Pharmacol. Ther. 138, 103–141. doi:10.1016/j.pharmthera.2012.12.007

Zhang, H., Patana, A. S., Mackenzie, P. I., Ikushiro, S., Goldman, A., and Finel, M.

(2012). Human UDP-Glucuronosyltransferase Expression in Insect Cells: Ratio

of Active to Inactive Recombinant Proteins and the Effects of a C-Terminal HisTag on Glucuronidation Kinetics. Drug Metab. Dispos. 40, 1935–1944. doi:10.

1124/dmd.112.046086

Nakajima, M., Koga, T., Sakai, H., Yamanaka, H., Fujiwara, R., and Yokoi, T.

(2010). N-Glycosylation Plays a Role in Protein Folding of Human UGT1A9.

Biochem. Pharmacol. 79, 1165–1172. doi:10.1016/j.bcp.2009.11.020

Nakamura, T., Yamaguchi, N., Miyauchi, Y., Takeda, T., Yamazoe, Y., Nagata, K.,

et al. (2016). Introduction of an N-Glycosylation Site into UDPGlucuronosyltransferase 2B3 Alters its Sensitivity to Cytochrome P450 3A1Dependent Modulation. Front. Pharmacol. 7, 427. doi:10.3389/fphar.2016.

00427

Oda, S., Nakajima, M., Hatakeyama, M., Fukami, T., and Yokoi, T. (2012).

Preparation of a Specific Monoclonal Antibody against Human UDPGlucuronosyltransferase (UGT) 1A9 and Evaluation of UGT1A9 Protein

Levels in Human Tissues. Drug Metab. Dispos. 40, 1620–1627. doi:10.1124/

dmd.112.045625

Omura, T., and Sato, R. (1964). The carbon monoxide-binding pigment of liver

microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239,

2370–2378.

Ramos, L., Kopec, L. A., Sweitzer, S. M., Fornwald, J. A., Zhao, H., Mcallister, P.,

et al. (2002). Rapid Expression of Recombinant Proteins in Modified CHO Cells

Using the Baculovirus System. Cytotechnology 38, 37–41. doi:10.1023/A:

1021189628274

Shin, H., Lee, Y. S., and Lee, Y. C. (2012). Sodium Butyrate-Induced DAPKMediated Apoptosis in Human Gastric Cancer Cells. Oncol. Rep. 27,

1111–1115. doi:10.3892/or.2011.1585

Sugatani, J. (2013). Function, Genetic Polymorphism, and Transcriptional

Regulation of Human UDP-Glucuronosyltransferase (UGT) 1A1. Drug

Metab. Pharmacokinet. 28, 83–92. doi:10.2133/dmpk.dmpk-12-rv-096

Tani, H., Nishijima, M., Ushijima, H., Miyamura, T., and Matsuura, Y. (2001).

Characterization of Cell-Surface Determinants Important for Baculovirus

Infection. Virology 279, 343–353. doi:10.1006/viro.2000.0699

Thomae, B. A., Eckloff, B. W., Freimuth, R. R., Wieben, E. D., and Weinshilboum,

R. M. (2002). Human Sulfotransferase SULT2A1 Pharmacogenetics: Genotype-

Frontiers in Pharmacology | www.frontiersin.org

Conflict of Interest: The authors declare that the research was conducted in the

absence of any commercial or financial relationships that could be construed as a

potential conflict of interest.

Publisher’s Note: All claims expressed in this article are solely those of the authors

and do not necessarily represent those of their affiliated organizations, or those of

the publisher, the editors and the reviewers. Any product that may be evaluated in

this article, or claim that may be made by its manufacturer, is not guaranteed or

endorsed by the publisher.

Copyright © 2022 Miyauchi, Kimura, Sawai, Fujimoto, Hirota, Tanaka, Takechi,

Mackenzie and Ishii. This is an open-access article distributed under the terms of the

Creative Commons Attribution License (CC BY). The use, distribution or

reproduction in other forums is permitted, provided the original author(s) and

the copyright owner(s) are credited and that the original publication in this journal is

cited, in accordance with accepted academic practice. No use, distribution or

reproduction is permitted which does not comply with these terms.

10

February 2022 | Volume 13 | Article 832931

...

参考文献をもっと見る

全国の大学の
卒論・修論・学位論文

一発検索!

この論文の関連論文を見る