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2. Novel advances in biotransformation and bioactivation research – 2020 year in review

Author

Khojasteh, S Cyrus, Argikar, Upendra A, Driscoll, James P, Heck, Carley JS, King, Lloyd, Jackson, Klarissa D, Jian, Wenying, Kalgutkar, Amit S, Miller, Grover P, Kramlinger, Valerie, Rietjens, Ivonne MCM, Teitelbaum, Aaron M, Wang, Kai, Wei, Cong, Johnson, Benjamin M, Shu, Yue-Zhong, Zhuo, Xiaoliang, Meanwell, Nicholas A, Cerny, Matthew A, Obach, R Scott, Sharma, Raman, Spracklin, Douglas K, Walker, Gregory S, Goracci, Laura, Desantis, Jenny, Valeri, Aurora, Castellani, Beatrice, Eleuteri, Michela, Cruciani, Gabriele, Lall, Manjinder S, Bassyouni, Asser, Bradow, James, Brown, Maria, Bundesmann, Mark, Chen, Jinshan, Ciszewski, Gregory, Hagen, Anne E, Hyek, Dennis, Jenkinson, Stephen, Liu, Bo, Pan, Senliang, Reilly, Usa, Sach, Neal, Smaltz, Daniel J, Starr, Jeremy, Wagenaar, Melissa, de Bruyn Kops, Christina, Sicho, Martin, Mazzolari, Angelica, Kirchmair, Johannes, Korprasertthaworn, Porntipa, Chau, Nuy, Nair, Pramod C, Rowland, Andrew, Miners, John O, Wrobleski, Stephen T, Moslin, Ryan, Lin, Shuqun, Zhang, Yanlei, Spergel, Steven, Kempson, James, Tokarski, John S, Strnad, Joann, Zupa-Fernandez, Adriana, Cheng, Lihong, Shuster, David, Gillooly, Kathleen, Yang, Xiaoxia, Heimrich, Elizabeth, McIntyre, Kim W, Chaudhry, Charu, Khan, Javed, Ruzanov, Max, Tredup, Jeffrey, Mulligan, Dawn, Xie, Dianlin, Sun, Huadong, Huang, Christine, D'Arienzo, Celia, Aranibar, Nelly, Chiney, Manoj, Chimalakonda, Anjaneya, Pitts, William J, Lombardo, Louis, Carter, Percy H, Burke, James R, Weinstein, David S, Li, Jing, Liu, Ju, Enders, Jennifer, Arciprete, Michael, Tran, Chris, Aluri, Krishna, Guan, Li-Hua, O'Shea, Jonathan, Bisbe, Anna, Charisse, Klaus, Zlatev, Ivan, Najarian, Diana, Xu, Yuanxin, Kim, Jaeah, El Zahar, Noha M, Bartlett, Michael G, Katyayan, Kishore, Yi, Ping, Monk, Scott, Cassidy, Kenneth, Takahashi, Ryan H, Grandner, Jessica M, Bobba, Sudheer, Liu, Yanzhou, Beroza, Paul, Zhang, Donglu, Ma, Shuguang, Post, Noah, Yu, Rosie, Greenlee, Sarah, Gaus, Hans, Hurh, Eunju, Matson, John, Wang, Yanfeng, Tajima, Yuya, Toyoda, Takeshi, Hirayama, Yuichiro, Matsushita, Kohei, Yamada, Takanori, Ogawa, Kumiko, Watanabe, Kenji, Takamura-Enya, Takeji, Totsuka, Yukari, Wakabayashi, Keiji, Miyoshi, Noriyuki, Zhang, Jiayin, Chan, Chi-Kong, Ham, Yat-Hing, Chan, Wan, Schleiff, Mary Alexandra, Flynn, Noah R, Payakachat, Sasin, Schleiff, Benjamin Mark, Pinson, Anna O, Province, Dennis W, Swamidass, S Joshua, Boysen, Gunnar, Nardone-White, Dasean T, Bissada, Jennifer E, Abouda, Arsany A, Zhang, Zhuming, Connolly, Peter J, Lim, Heng Keang, Pande, Vineet, Meerpoel, Lieven, Teleha, Christopher, Branch, Jonathan R, Ondrus, Janine, Hickson, Ian, Bush, Tammy, Luistro, Leopoldo, Packman, Kathryn, Bischoff, James R, Ibrahim, Salam, Parrett, Christopher, Chong, Yolanda, Gottardis, Marco M, Bignan, Gilles, Mulder, Teresa, Bobba, Sudder, Johnson, Kevin M, Wang, Wei, Zhang, Chenghong, Cai, Jingwei, Choo, Edna F, Crawford, James J, Landry, Matthew L, Chen, Huifen, Kenny, Jane R, Lee, Wendy, Young, Wendy B, Geib, Timon, Thulasingam, Madhuranayaki, Haeggstrom, Jesper Z, Sleno, Lekha, Monroe, James J, Tanis, Keith Q, Podtelezhnikov, Alexei A, Nguyen, Truyen, Machotka, Sam V, Lynch, Donna, Evers, Raymond, Palamanda, Jairam, Miller, Randy R, Pippert, Todd, Cabalu, Tamara D, Johnson, Timothy E, Aslamkhan, Amy G, Kang, Wen, Tamburino, Alex M, Mitra, Kaushik, Agrawal, Nancy GB, and Sistare, Frank D

Subjects
METABOLISM, Toxicology, 030226 pharmacology & pharmacy, 03 medical and health sciences, nonp450 enzymes, 0302 clinical medicine, p450 enzymes, Biotransformation, INTRINSIC CLEARANCE, Political science, MASS-BALANCE, Humans, Pharmacology (medical), Pharmacology & Pharmacy, P450 Enzymes, General Pharmacology, Toxicology and Pharmaceutics, ANTISENSE OLIGONUCLEOTIDE, Toxicologie, VLAG, ARISTOLOCHIC ACID, Drug metabolism, Science & Technology, WIMEK, bioactivation, IDENTIFICATION, Year in review, IN-VITRO, NONHEPATOTOXIC DRUGS, Drug metabolizing enzymes, Drug development, 030220 oncology & carcinogenesis, COVALENT BINDING DATA, Engineering ethics, biotransformation, LIVER-MICROSOMES, Life Sciences & Biomedicine
Abstract

This annual review is the sixth of its kind since 2016 (see references). Our objective is to explore and share articles which we deem influential and significant in the field of biotransformation and bioactivation. These fields are constantly evolving with new molecular structures and discoveries of corresponding pathways for metabolism that impact relevant drug development with respect to efficacy and safety. Based on the selected articles, we created three sections: (1) drug design, (2) metabolites and drug metabolizing enzymes, and (3) bioactivation and safety (Table 1). Unlike in years past, more biotransformation experts have joined and contributed to this effort while striving to maintain a balance of authors from academic and industry settings.[Table: see text]. ispartof: DRUG METABOLISM REVIEWS vol:53 issue:3 pages:384-433 ispartof: location:England status: published

Published
2021

7. Scaling factors for the in vitro-in vivo extrapolation (IV-IVE) of renal drug and xenobiotic glucuronidation clearance

Author

Fallon, John K., Knights, Kathleen M., Smith, Philip C., Spencer, Shane M., Chau, Nuy, and Miners, John O.

Abstract

AIM: To determine the scaling factors required for inclusion of renal drug glucuronidation clearance in the prediction of total clearance via glucuronidation (CLUGT ). METHODS: Microsomal protein per gram of kidney (MPPGK) was determined for human 'mixed' kidney (n = 5) microsomes (MKM). The glucuronidation activities of deferiprone (DEF), propofol (PRO) and zidovudine (AZT) by MKM and paired cortical (KCM) and medullary (KMM) microsomes were measured, along with the UGT 1A6, 1A9 and 2B7 protein contents of each enzyme source. Unbound intrinsic clearances (CLint,u,UGT ) for PRO and morphine (MOR; 3- and 6-) glucuronidation by MKM, human liver microsomes (HLM) and recombinant UGT1A9 and 2B7 were additionally determined. Data were scaled using in vitro-in vivo extrapolation (IV-IVE) approaches to assess the influence of renal CLint,u,UGT on the prediction accuracy of the calculated CLUGT values of PRO and MOR. RESULTS: MPPGK was 9.3 ± 2.0 mg g(-1) (mean ± SD). The respective rates of DEF (UGT1A6), PRO (UGT1A9) and AZT (UGT2B7) glucuronidation by KCM were 1.4-, 5.2- and 10.5-fold higher than those for KMM. UGT 1A6, 1A9 and 2B7 were the only enzymes expressed in kidney. Consistent with the activity data, the abundance of each of these enzymes was greater in KCM than in KMM. The abundance of UGT1A9 in MKM (61.3 pmol mg(-1) ) was 2.7 fold higher than that reported for HLM. CONCLUSIONS: Scaled renal PRO glucuronidation CLint,u,UGT was double that of liver. Renal CLint,u,UGT should be accounted for in the IV-IVE of UGT1A9 and considered for UGT1A6 and 2B7 substrates.

Published
2016
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11. Drug and Chemical Glucosidation by Control Supersomes and Membranes from Spodoptera frugiperda(Sf) 9 Cells: Implications for the Apparent Glucuronidation of Xenobiotics by UDP-glucuronosyltransferase 1A5

Author

Chau, Nuy, Kaya, Leyla, Lewis, Benjamin C., Mackenzie, Peter I., and Miners, John O.

Abstract

Accumulating evidence indicates that several human UDP-glucuronosyltransferase (UGT) enzymes catalyze both glucuronidation and glucosidation reactions. Baculovirus-infected insect cells [Trichoplusia niand Spodoptera frugiperda(Sf9)] are used widely for the expression of recombinant human UGT enzymes. Following the observation that control Supersomes (c-SUP) express a native enzyme capable of glucosidating morphine, we characterized the glucosidation of a series of aglycones with a hydroxyl (aliphatic or phenolic), carboxylic acid, or amine functional group by c-SUP and membranes from uninfected Sf9 cells. Although both enzyme sources glucosidated the phenolic substrates investigated, albeit with differing activities, differences were observed in the selectivities of the native UDP-glucosyltransferases toward aliphatic alcohols, carboxylic acids, and amines. For example, zidovudine was solely glucosidated by c-SUP. By contrast, c-SUP lacked activity toward the amines lamotrigine and trifluoperazine and did not form the acyl glucoside of mycophenolic acid, reactions all catalyzed by uninfected Sf9 membranes. Glucosidation intrinsic clearances were high for several substrates, notably 1-hydroxypyrene (∼1400–1900 µl/min⋅mg). The results underscore the importance of including control cell membranes in the investigation of drug and chemical glucosidation by UGT enzymes expressed in T. ni(High-Five) and Sf9 cells. In a coincident study, we observed that UGT1A5 expressed in Sf9, human embryonic kidney 293T, and COS7 cells lacked glucuronidation activity toward prototypic phenolic substrates. However, Sf9 cells expressing UGT1A5 glucosidated 1-hydroxypyrene with UDP-glucuronic acid as the cofactor, presumably due to the presence of UDP-glucose as an impurity. Artifactual glucosidation may explain, at least in part, a previous report of phenolic glucuronidation by UGT1A5.

Published
2019
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17. The Novel UDP Glycosyltransferase 3A2: Cloning, Catalytic Properties, and Tissue Distribution

Author

MacKenzie, Peter I., Rogers, Anne, Elliot, David J., Chau, Nuy, Hulin, Julie-Ann, Miners, John O., and Meech, Robyn

Abstract

The human UDP glycosyltransferase (UGT) 3A family is one of three families involved in the metabolism of small lipophilic compounds. Members of these families catalyze the addition of sugar residues to chemicals, which enhances their excretion from the body. The UGT1 and UGT2 family members primarily use UDP glucuronic acid to glucuronidate numerous compounds, such as steroids, bile acids, and therapeutic drugs. We showed recently that UGT3A1, the first member of the UGT3 family to be characterized, is unusual in using UDP N-acetylglucosamine as sugar donor, rather than UDP glucuronic acid or other UDP sugar nucleotides (J Biol Chem 283:36205–36210, 2008). Here, we report the cloning, expression, and characterization of UGT3A2, the second member of the UGT3 family. Like UGT3A1, UGT3A2 is inactive with UDP glucuronic acid as sugar donor. However, in contrast to UGT3A1, UGT3A2 uses both UDP glucose and UDP xylose but not UDP N-acetylglucosamine to glycosidate a broad range of substrates including 4-methylumbelliferone, 1-hydroxypyrene, bioflavones, and estrogens. It has low activity toward bile acids and androgens. UGT3A2 transcripts are found in the thymus, testis, and kidney but are barely detectable in the liver and gastrointestinal tract. The low expression of UGT3A2 in the latter, which are the main organs of drug metabolism, suggests that UGT3A2 has a more selective role in protecting the organs in which it is expressed against toxic insult rather than a more generalized role in drug metabolism. The broad substrate and novel UDP sugar specificity of UGT3A2 would be advantageous for such a function.

Published
2011

18. Effects of ketamine on human UDP-glucuronosyltransferases in vitro predict potential drug-drug interactions arising from ketamine inhibition of codeine and morphine glucuronidation

Author

John O. Miners, Benjamas Janchawee, Allan M. Evans, Pritsana Raungrut, Verawan Uchaipichat, Nuy Chau, Uchaipichat, Verawan, Raungrut, Pritsana, Chau, Nuy, Janchawee, Benjamas, Evans, Allan M, and Miners, John O

Subjects
UGT1A4, Insecta, Glucuronidation, Cell Culture Techniques, Pharmaceutical Science, reaction, Pharmacology, Transfection, Pharmacokinetics, In vivo, Predictive Value of Tests, medicine, Animals, Humans, Ketamine, Drug Interactions, Glucuronosyltransferase, Dose-Response Relationship, Drug, Morphine, Chemistry, Codeine, Culture Media, Analgesics, Opioid, enzyme, HEK293 Cells, anesthetic, Anesthetic, Inactivation, Metabolic, Microsomes, Liver, human liver, medicine.drug, Protein Binding
Abstract

In this study, the selectivity of UDP-glucuronosyltransferase (UGT) enzyme inhibition by ketamine (KTM) and the kinetics of KTM inhibition of human liver microsomal morphine (MOR) and codeine (COD) glucuronidation were characterized to explore a pharmacokinetic basis for the KTM-opioid interaction. With the exception of UGT1A4, KTM inhibited the activities of recombinant human UGT enzymes in a concentration-dependent manner. However, IC50 values were 50% increases in the in vivo area under the curve ratios) with MOR and COD were predicted for anesthetic doses of KTM and for a subanesthetic dose of KTM on COD glucuronidation. Refereed/Peer-reviewed

Published
2011

19. Drug and Chemical Glucosidation by Control Supersomes and Membranes from Spodoptera frugiperda (Sf) 9 Cells: Implications for the Apparent Glucuronidation of Xenobiotics by UDP-glucuronosyltransferase 1A5.

Author

Chau N, Kaya L, Lewis BC, Mackenzie PI, and Miners JO

Subjects
Animals, COS Cells, Cell Membrane metabolism, Chlorocebus aethiops, Coenzymes metabolism, Glucuronides metabolism, HEK293 Cells, Humans, Sf9 Cells, Uridine Diphosphate Glucose metabolism, Uridine Diphosphate Glucuronic Acid metabolism, Glucuronosyltransferase metabolism, Recombinant Proteins metabolism, Spodoptera metabolism, Subcellular Fractions metabolism, Xenobiotics metabolism
Abstract

Accumulating evidence indicates that several human UDP-glucuronosyltransferase (UGT) enzymes catalyze both glucuronidation and glucosidation reactions. Baculovirus-infected insect cells [ Trichoplusia ni and Spodoptera frugiperda (Sf9)] are used widely for the expression of recombinant human UGT enzymes. Following the observation that control Supersomes (c-SUP) express a native enzyme capable of glucosidating morphine, we characterized the glucosidation of a series of aglycones with a hydroxyl (aliphatic or phenolic), carboxylic acid, or amine functional group by c-SUP and membranes from uninfected Sf9 cells. Although both enzyme sources glucosidated the phenolic substrates investigated, albeit with differing activities, differences were observed in the selectivities of the native UDP-glucosyltransferases toward aliphatic alcohols, carboxylic acids, and amines. For example, zidovudine was solely glucosidated by c-SUP. By contrast, c-SUP lacked activity toward the amines lamotrigine and trifluoperazine and did not form the acyl glucoside of mycophenolic acid, reactions all catalyzed by uninfected Sf9 membranes. Glucosidation intrinsic clearances were high for several substrates, notably 1-hydroxypyrene (∼1400-1900 µ l/min⋅mg). The results underscore the importance of including control cell membranes in the investigation of drug and chemical glucosidation by UGT enzymes expressed in T. ni (High-Five) and Sf9 cells. In a coincident study, we observed that UGT1A5 expressed in Sf9, human embryonic kidney 293T, and COS7 cells lacked glucuronidation activity toward prototypic phenolic substrates. However, Sf9 cells expressing UGT1A5 glucosidated 1-hydroxypyrene with UDP-glucuronic acid as the cofactor, presumably due to the presence of UDP-glucose as an impurity. Artifactual glucosidation may explain, at least in part, a previous report of phenolic glucuronidation by UGT1A5., (Copyright © 2019 by The American Society for Pharmacology and Experimental Therapeutics.)

Published
2019
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