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Journal articles on the topic 'UDP-glucuronosyltransferase'

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Published: 4 June 2021

Last updated: 18 February 2022

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1

Matsui, M., and F. Nagai. "Genetic deficiency of androsterone UDP-glucuronosyltransferase activity in Wistar rats is due to the loss of enzyme protein." Biochemical Journal 234, no. 1 (February 15, 1986): 139–44. http://dx.doi.org/10.1042/bj2340139.

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Hepatic microsomal UDP-glucuronosyltransferases towards androsterone and testosterone were purified by chromatofocusing and UDP-hexanolamine affinity chromatography in Wistar rats which had genetic deficiency of androsterone UDP-glucuronosyltransferase activity. In rats with the high-activity phenotype, androsterone (the 3-hydroxy androgen) UDP-glucuronosyltransferase was eluted at about pH 7.4 and had a subunit Mr of 52 000, whereas testosterone (the 17-hydroxy steroid) UDP-glucuronosyltransferase was eluted at about pH 8.4 and had a subunit Mr of 50 000. The transferase that conjugates both androsterone and testosterone was eluted at about pH 8.0, had subunit Mr values of 50 000 and 52 000, and appeared to be an aggregate or hybrid of androsterone and testosterone UDP-glucuronosyltransferases. In rats with the low-activity phenotype, androsterone UDP-glucuronosyltransferase was absent, whereas testosterone UDP-glucuronosyltransferase was eluted at around pH 8.5, with a subunit Mr of 50 000.

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2

Golovinsky, E., Z. Naydenova, and K. Grancharov. "UDP-Glucuronosyltransferase inhibitors." European Journal of Drug Metabolism and Pharmacokinetics 23, no. 4 (December 1998): 453–56. http://dx.doi.org/10.1007/bf03189994.

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3

Jackson, M. R., L. R. McCarthy, D. Harding, S. Wilson, M. W. H. Coughtrie, and B. Burchell. "Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA." Biochemical Journal 242, no. 2 (March 1, 1987): 581–88. http://dx.doi.org/10.1042/bj2420581.

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A cDNA clone (HLUG 25) encoding the complete sequence of a human liver UDP-glucuronosyltransferase was isolated from a lambda gt11 human liver cDNA library. The library was screened by hybridization to a partial-length human UDP-glucuronosyltransferase cDNA (pHUDPGT1) identified from a human liver pEX cDNA expression library by using anti-UDP-glucuronosyltransferase antibodies. The authenticity of the cDNA clone was confirmed by hybrid-select translation and extensive sequence homology to rat liver UDP-glucuronosyltransferase cDNAs. The sequence of HLUG 25 cDNA was determined to be 2104 base-pairs long, including a poly(A) tail, and contains a long open reading frame. The possible site of translation initiation of this sequence is discussed with reference to a rat UDP-glucuronosyltransferase cDNA clone (RLUG 38).

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4

Falany, C. N., M. D. Green, E. Swain, and T. R. Tephly. "Substrate specificity and characterization of rat liver p-nitrophenol, 3 α-hydroxysteroid and 17 β-hydroxysteroid UDP-glucuronosyltransferases." Biochemical Journal 238, no. 1 (August 15, 1986): 65–73. http://dx.doi.org/10.1042/bj2380065.

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Purified preparations of rat liver 17-hydroxysteroid, 3-hydroxyandrogen and p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferases were further characterized as to their substrate specificities, phospholipid-dependency and physical properties. The two steroid UDP-glucuronosyltransferases were shown to exhibit strict stereospecificity with respect to the conjugation of steroids and bile acids. These enzymes have been renamed 17 beta-hydroxysteroid and 3 alpha-hydroxysteroid UDP-glucuronosyltransferase to reflect this specificity for important endogenous substrates. An endogenous substrate has not yet been identified for the p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferase. The steroid UDP-glucuronosyltransferase activities were dependent on phospholipid for maximal catalytic activity. Complete delipidation rendered the UDP-glucuronosyltransferases inactive, and enzymic activity was not restored when phospholipid was added to the reaction mixture. After partial delipidation, phosphatidylcholine was the most efficient phospholipid for restoration of enzymic activity. Partial delipidation also altered the kinetic parameters of the 3 alpha-hydroxysteroid UDP-glucuronosyltransferase. The three purified UDP-glucuronosyltransferases are separate and distinct proteins, with different amino acid compositions and peptide maps generated by limited proteolysis with Staphylococcus aureus V8 proteinase. Some similarity was observed between the amino acid composition and limited proteolytic maps of the steroid UDP-glucuronosyltransferases, suggesting they are more closely related to each other than to the p-nitrophenol UDP-glucuronosyltransferase.

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5

Radominska-Pandya, A., J. Little, and P. Czernik. "Human UDP-Glucuronosyltransferase 2B7." Current Drug Metabolism 2, no. 3 (September 1, 2001): 283–98. http://dx.doi.org/10.2174/1389200013338379.

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6

Leaver, Michael J., Joy Wright, Paul Hodgson, Evridiki Boukouvala, and Stephen G. George. "Piscine UDP-glucuronosyltransferase 1B." Aquatic Toxicology 84, no. 3 (October 2007): 356–65. http://dx.doi.org/10.1016/j.aquatox.2007.06.015.

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7

BÁNHEGYI, Gábor, László BRAUN, Paola MARCOLONGO, Miklós CSALA, Rosella FULCERI, József MANDL, and BENEDETTI BENEDETTI. "Evidence for an UDP-glucuronic acid/phenol glucuronide antiport in rat liver microsomal vesicles." Biochemical Journal 315, no. 1 (April 1, 1996): 171–76. http://dx.doi.org/10.1042/bj3150171.

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The transport of glucuronides synthesized in the luminal compartment of the endoplasmic reticulum by UDP-glucuronosyltransferase isoenzymes was studied in rat liver microsomal vesicles. Microsomal vesicles were loaded with p-nitrophenol glucuronide (5 mM), phenolphthalein glucuronide or UDP-glucuronic acid, by a freeze–thawing method. It was shown that: (i) the loading procedure resulted in millimolar intravesicular concentrations of the different loading compounds; (ii) addition of UDP-glucuronic acid (5 mM) to the vesicles released both intravesicular glucuronides within 1 min; (iii) glucuronides stimulated the release of UDP-glucuronic acid from UDP-glucuronic acid-loaded microsomal vesicles; (iv) trans-stimulation of UDP-glucuronic acid entry by loading of microsomal vesicles with p-nitrophenol glucuronide, phenolphthalein glucuronide, UDP-glucuronic acid and UDP-N-acetylglucosamine almost completely abolished the latency of UDP-glucuronosyltransferase, although mannose 6-phosphatase latency remained unaltered; (v) the loading compounds by themselves did not stimulate UDP-glucuronosyltransferase activity. This study indicates that glucuronides synthesized in the lumen of endoplasmic reticulum can leave by an antiport, which concurrently transports UDP-glucuronic acid into the lumen of the endoplasmic reticulum.

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8

Little, J. M., R. Lester, F. Kuipers, R. Vonk, P. I. Mackenzie, R. R. Drake, L. Frame, and A. Radominska-Pandya. "Variability of human hepatic UDP-glucuronosyltransferase activity." Acta Biochimica Polonica 46, no. 2 (June 30, 1999): 351–63. http://dx.doi.org/10.18388/abp.1999_4168.

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The availability of a unique series of liver samples from human subjects, both control patients (9) and those with liver disease (6; biliary atresia (2), retransplant, chronic tyrosinemia type I, tyrosinemia, Wilson's disease) allowed us to characterize human hepatic UDP-glucuronosyltransferases using photoaffinity labeling, immunoblotting and enzymatic assays. There was wide inter-individual variation in photoincorporation of the photoaffinity analogs, [32P]5-azido-UDP-glucuronic acid and [32P]5-azido-UDP-glucose and enzymatic glucuronidation of substrates specific to the two subfamilies of UDP-glucuronosyltransferases. However, the largest differences were between subjects with liver disease. Glucuronidation activities toward one substrate from each of the UDP-glucuronosyltransferases subfamilies, 1A and 2B, for control and liver disease, respectively, were 1.7-4.5 vs 0.4-4.7 nmol/mg x min for hyodeoxycholic acid (2B substrate) and 9.2-27.9 vs 8.1-75 nmol/mg x min for pchloro-m-xylenol (1A substrate). Microsomes from a patient with chronic tyrosinemia (HL32) photoincorporated [32P]5-azido-UDP-glucuronic acid at a level 1.5 times higher than the other samples, was intensely photolabeled by [32P]5-azido-UDP-glucose and had significantly higher enzymatic activity toward p-chloro-m-xylenol. Immunoblot analysis using anti-UDP-glucuronosyltransferase antibodies demonstrated wide inter-individual variations in UDP-glucuronosyltransferase protein with increased UDP-glucuronosyltransferase protein in HL32 microsomes, corresponding to one of the bands photolabeled by both probes. Detailed investigation of substrate specificity, using substrates representative of both the 1A (bilirubin, 4-nitrophenol) and 2B (androsterone, testosterone) families was carried out with HL32, HL38 (age and sex matched control) and HL18 (older control). Strikingly increased (5-8-fold) glucuronidation activity was seen in comparison to HL18 only with the phenolic substrates. The results indicate that one or more phenol-specific UDP-glucuronosyltransferase 1A isoforms are expressed at above normal levels in this tyrosinemic subject.

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9

Mackenzie, P., P. Gregory, D. Gardner-Stephen, R. Lewinsky, B. Jorgensen, T. Nishiyama, Wen Xie, and A. Radominska-Pandya. "Regulation of UDP Glucuronosyltransferase Genes." Current Drug Metabolism 4, no. 3 (June 1, 2003): 249–57. http://dx.doi.org/10.2174/1389200033489442.

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10

Debinski, H. S., C. S. Lee, A. P. Dhillon, P. Mackenzie, J. Rhode, and P. V. Desmond. "UDP-Glucuronosyltransferase in gilbert’s syndrome." Pathology 28, no. 3 (1996): 238–41. http://dx.doi.org/10.1080/00313029600169064.

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11

Gould, S. J., and J. Guo. "Cytosylglucuronic acid synthase (cytosine: UDP-glucuronosyltransferase) from Streptomyces griseochromogenes, the first prokaryotic UDP-glucuronosyltransferase." Journal of Bacteriology 176, no. 5 (1994): 1282–86. http://dx.doi.org/10.1128/jb.176.5.1282-1286.1994.

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12

Roy Chowdhury, J., N. Roy Chowdhury, C. N. Falany, T. R. Tephly, and I. M. Arias. "Isolation and characterization of multiple forms of rat liver UDP-glucuronate glucuronosyltransferase." Biochemical Journal 233, no. 3 (February 1, 1986): 827–37. http://dx.doi.org/10.1042/bj2330827.

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UDP-glucuronosyltransferase (EC 2.4.1.17) activity was solubilized from male Wistar rat liver microsomal fraction in Emulgen 911, and six fractions with the transferase activity were separated by chromatofocusing on PBE 94 (pH 9.4 to 6.0). Fraction I was further separated into Isoforms Ia, Ib and Ic by affinity chromatography on UDP-hexanolamine-Sepharose 4B. UDP-glucuronosyltransferase in Fraction III was further purified by rechromatofocusing (pH 8.7 to 7.5). UDP-glucuronosyltransferases in Fractions IV and V were purified by UDP-hexanolamine-Sepharose chromatography. The transferase isoforms in Fractions II, III, IV and V were finally purified by h.p.l.c. on a TSK G 3000 SW column. Purified UDP-glucuronosyltransferase Isoforms Ia (Mr 51,000), Ib (Mr 52,000), Ic (Mr 56,000), II (Mr 52,000), IV (Mr 53,000) and V (Mr 53,000) revealed single Coomassie Blue-stained bands on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Isoform III enzyme showed two bands of Mr 52,000 and 53,000. Comparison of the amino acid compositions by the method of Cornish-Bowden [(1980) Anal. Biochem. 105, 233-238] suggested that all UDP-glucuronosyltransferase isoforms are structurally related. Reverse-phase h.p.l.c. of tryptic peptides of individual isoforms revealed distinct ‘maps’, indicating differences in primary protein structure. The two bands of Isoform III revealed distinct electrophoretic peptide maps after limited enzymic proteolysis. After reconstitution with phosphatidylcholine liposomes, the purified isoforms exhibited distinct but overlapping substrate specificities. Isoform V was specific for bilirubin glucuronidation, which was not inhibited by other aglycone substrates. Each isoform, except Ia, was identified as a glycoprotein by periodic acid/Schiff staining.

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13

Haque, Md Azizul, Laila Shamima Sharmin, Mohd Harun or Rashid, MA Alim, ARM Saifuddin Ekram, and Syed Ghulam Mogni Mowla. "Crigler-Najjar Syndrome Type 2 in a Young Adult." Journal of Medicine 12, no. 1 (January 21, 2011): 86–88. http://dx.doi.org/10.3329/jom.v12i1.6359.

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Crigler-Najjar syndrome type 2 in an autosomal recessive congenital non-hemolytic hyperbilirubinemia caused by UDP-glucuronosyltransferase deficiency. Only a few hundred cases have been described in the literature so far. We are reporting Crigler-Najjar syndrome type 2 in an 18 year old female born out of consanguineous marriage. Keyword: Crigler-Najjar syndrome; UDP-glucuronosyltransferase; Bangladesh DOI: 10.3329/jom.v12i1.6359J Medicine 2011; 12 : 81-85

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14

Pozzi, Enrique J. Sánchez, Viviana A. Catania, Marcelo G. Luquita, Marcelo G. Roma, Emilio A. Rodríguez Garay, and Aldo D. Mottino. "Effect of oral administration of ursodeoxycholic acid on rat hepatic and intestinal UDP-glucuronosyltransferase." Canadian Journal of Physiology and Pharmacology 72, no. 11 (November 1, 1994): 1265–71. http://dx.doi.org/10.1139/y94-181.

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The effect of oral administration of the bile acid ursodeoxycholic acid on rat hepatic and intestinal microsomal UDP-glucuronosyltransferase was studied. The bile acid was administered during 8 days at a daily dose of 500 mg/kg body weight. Enzyme activity was assessed in native and activated microsomes, using bilirubin and p-nitrophenol as substrates. Activation was achieved either by including UDP-N-acetylglucosamine in the incubation mixture or by preincubating native microsomes with an optimal concentration of Lubrol Px. Irrespective of activation status of the microsomes, ursodeoxycholic acid treatment increased enzyme activities toward both substrates in intestine, but not in liver. The analysis of the degree of activation by Lubrol Px revealed that, at least for bilirubin, ursodeoxycholic acid decreased the latency of the intestinal enzyme. The analysis of the lipid composition of microsomes showed several changes in response to ursodeoxycholic acid in intestine but not in liver. Thus, a decrease in cholesterol/phospholipid ratio and an increase in the unsaturation index of total-lipid fatty acids, which correlated well with a membrane "fluidification," were observed. These modifications appear to be related to the lower latency of bilirubin UDP-glucuronosyltransferase in intestine from treated rats and could be responsible, at least in part, for the improvement of enzyme activity in this group. Whatever the mechanism involved, the increment of intestinal UDP-glucuronosyltransferase activities toward both substrates may be relevant as a complement to the hepatic enzymes in those liver diseases in which ursodeoxycholic acid is used as a therapeutic agent.Key words: bilirubin, p-nitrophenol, ursodeoxycholic acid, UDP-glucuronosyltransferase, microsomal lipids.

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15

Green, M. D., C. N. Falany, R. B. Kirkpatrick, and T. R. Tephly. "Strain differences in purified rat hepatic 3 α-hydroxysteroid UDP-glucuronosyltransferase." Biochemical Journal 230, no. 2 (September 1, 1985): 403–9. http://dx.doi.org/10.1042/bj2300403.

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Qualitative and quantitative differences of purified hepatic 3 α-hydroxysteroid UDP-glucuronosyltransferase were investigated in Wistar and Sprague-Dawley rats. Individual differences in the glucuronidation rate of androsterone and chenodeoxycholic acid were observed in hepatic microsomal fractions from Wistar but not Sprague-Dawley rats. No individual variation was observed in the glucuronidation of testosterone, p-nitrophenol or oestrone. The 3 α-hydroxysteroid UDP-glucuronosyltransferases from livers of Wistar and Sprague-Dawley rats were isolated and highly purified by using Chromatofocusing and affinity chromatography. The amount of 3 α-hydroxysteroid UDP-glucuronosyltransferase in the liver of Wistar rats exhibiting low rates for androsterone glucuronidation is about 10% or less than that found in hepatic microsomal fractions obtained from Wistar rats having high rates for androsterone glucuronidation. The apparent Km for androsterone with purified 3 α-hydroxysteroid UDP-glucuronosyltransferase from Wistar rats with high glucuronidation activity (6 microM) was not different from that observed for the enzyme purified from Sprague-Dawley animals, whereas that for the enzyme purified from Wistar rats with low glucuronidation activity was substantially higher (120 microM). Despite the differences in apparent Km values for androsterone, the apparent Km for UDP-glucuronic acid (0.3 mM) was not different in the different populations of rats.

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16

Lee, C. S., H. S. Debinski, S. Smid, P. McKenzie, J. Rode, and A. P. Dhillon. "Decreased UDP glucuronosyltransferase in Gilbert's syndrome." Pathology 25 (1993): 13. http://dx.doi.org/10.1016/s0031-3025(16)35753-1.

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17

Coffman, Birgit L., Gladys R. Rios, and Thomas R. Tephly. "Measurements of UDP- Glucuronosyltransferase (UGT) Activities." Current Protocols in Toxicology 00, no. 1 (May 1999): 4.3.1–4.3.15. http://dx.doi.org/10.1002/0471140856.tx0403s13.

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18

Burchell, Brian. "Genetic Variation of Human UDP-Glucuronosyltransferase." American Journal of PharmacoGenomics 3, no. 1 (2003): 37–52. http://dx.doi.org/10.2165/00129785-200303010-00006.

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19

Guillemette, C. "Pharmacogenomics of human UDP-glucuronosyltransferase enzymes." Pharmacogenomics Journal 3, no. 3 (January 2003): 136–58. http://dx.doi.org/10.1038/sj.tpj.6500171.

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20

Mackenzie, Peter I. "The regulation of UDP glucuronosyltransferase expression." Drug Metabolism and Pharmacokinetics 32, no. 1 (January 2017): S21. http://dx.doi.org/10.1016/j.dmpk.2016.10.094.

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21

Wang, Laurene H., David Zakim, Abraham M. Rudolph, and Leslie Z. Benet. "Developmental alterations in hepatic UDP-glucuronosyltransferase." Biochemical Pharmacology 35, no. 18 (September 1986): 3065–70. http://dx.doi.org/10.1016/0006-2952(86)90387-4.

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22

Bossuyt, X., and N. Blanckaert. "Mechanism of stimulation of microsomal UDP-glucuronosyltransferase by UDP-N-acetylglucosamine." Biochemical Journal 305, no. 1 (January 1, 1995): 321–28. http://dx.doi.org/10.1042/bj3050321.

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We propose the existence in rat liver endoplasmic reticulum (ER) of two asymmetric carrier systems. One system couples UDP-N-acetylglucosamine (UDPGlcNAc) transport to UDP-glucuronic acid (UDPGlcA) transport. When UDPGlcNAc was presented at the cytosolic side of the ER, it then acted as a weak inhibitor of UDPGlcA uptake. By contrast, UDPGlcNAc produced a forceful trans-stimulation of microsomal UDPGlcA uptake when it was present within the lumen of the ER. Likewise, cytosolic UDPGlcA strongly trans-stimulated efflux of intravesicular UDPGlcNAc, whereas cytosolic UDPGlcNAc was ineffective in trans-stimulating efflux of UDPGlcA. A second asymmetric carrier system couples UDPGlcNAc transport to UMP transport. Microsomal UDPGlcNAc influx was markedly stimulated by UMP present inside the microsomes. Such stimulation was only apparent when microsomes had been preincubated and thereby preloaded with UMP, indicating that UMP exerted its effect on UDPGlcNAc uptake by trans-stimulation from the lumenal side of the ER membrane. Contrariwise, extravesicular UMP only minimally trans-stimulated efflux of intramicrosomal UDPGlcNAc. It is widely accepted that UDPGlcNAc acts as a physiological activator of hepatic glucuronidation, but the mechanism of this effect has remained elusive. Based on our findings, we propose a model in which the interaction of two asymmetric transport pathways, i.e. UDPGlcA influx coupled to UDPGlcNAc efflux and UDPGlcNAc influx coupled to UMP efflux, combined with intravesicular metabolism of UDPGlcA, forms a mechanism that leads to stimulation of glucuronidation by UDPGlcNAc.

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23

Hu, Dong Gui, Robyn Meech, Ross A. McKinnon, and Peter I. Mackenzie. "Transcriptional regulation of human UDP-glucuronosyltransferase genes." Drug Metabolism Reviews 46, no. 4 (October 22, 2014): 421–58. http://dx.doi.org/10.3109/03602532.2014.973037.

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24

Maruo, Yoshihiro, Masaru Iwai, Asami Mori, Hiroshi Sato, and Yoshihiro Takeuchi. "Polymorphism of UDP-Glucuronosyltransferase and Drug Metabolism." Current Drug Metabolism 6, no. 2 (April 1, 2005): 91–99. http://dx.doi.org/10.2174/1389200053586064.

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25

Grancharov, K. "Natural and synthetic inhibitors of UDP-glucuronosyltransferase." Pharmacology & Therapeutics 89, no. 2 (February 2001): 171–86. http://dx.doi.org/10.1016/s0163-7258(00)00109-1.

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26

Toide, Kenji, Shin-ichiro Umeda, Hiroshi Yamazaki, Yoshiki Takahashi, Yoshiaki Terauchi, Toshihiko Fujii, and Tetsuya Kamataki. "A Major Genotype in UDP-glucuronosyltransferase 2B15." Drug Metabolism and Pharmacokinetics 17, no. 2 (2002): 164–66. http://dx.doi.org/10.2133/dmpk.17.164.

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27

Augustin, Christa, Lutz von Meyerinck, and Achim Schmoldt. "Monoclonal antibodies against 4-hydroxybiphenyl-UDP-glucuronosyltransferase." Biochemical Pharmacology 44, no. 4 (August 1992): 836–38. http://dx.doi.org/10.1016/0006-2952(92)90426-j.

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28

DEBINSKI, HENRY S., PETER I. MACKENZIE, C. SOON LEE, M. LAURENCE MASHFORD, JANINE A. DANKS, THOMAS R. TEPHLY, MITCHELL GREEN, and PAUL V. DESMOND. "UDP glucuronosyltransferase in the cirrhotic rat liver." Journal of Gastroenterology and Hepatology 11, no. 4 (April 1996): 373–79. http://dx.doi.org/10.1111/j.1440-1746.1996.tb01386.x.

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29

Zakim, D., M. Cantor, and H. Eibl. "Phospholipids and UDP-glucuronosyltransferase. Structure/function relationships." Journal of Biological Chemistry 263, no. 11 (April 1988): 5164–69. http://dx.doi.org/10.1016/s0021-9258(18)60694-5.

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30

Operaña, Theresa N., and Robert H. Tukey. "Oligomerization of the UDP-glucuronosyltransferase 1A Proteins." Journal of Biological Chemistry 282, no. 7 (December 19, 2006): 4821–29. http://dx.doi.org/10.1074/jbc.m609417200.

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UDP-glucuronosyltransferases (UGTs) are membrane-bound proteins localized to the endoplasmic reticulum and catalyze the formation of β-d-glucopyranosiduronic acids (glucuronides) using UDP-glucuronic acid and acceptor substrates such as drugs, steroids, bile acids, xenobiotics, and dietary nutrients. Recent biochemical evidence indicates that the UGT proteins may oligomerize in the membrane, but conclusive evidence is still lacking. In the present study, we have used fluorescence resonance energy transfer (FRET) to study UGT1A oligomerization in live cells. This technique demonstrated that UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 self-oligomerize (homodimerize). Heterodimer interactions were also explored, and it was determined that UGT1A1 was capable of binding with UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10. In addition to the in vivo FRET analysis, UGT1A protein-protein interactions were demonstrated through co-immunoprecipitation experiments. Co-expression of hemagglutinin-tagged and cyan fluorescent protein-tagged UGT1A proteins, followed by immunoprecipitation with anti-hemagglutinin beads, illustrated the potential of each UGT1A protein to homodimerize. Co-immunoprecipitation results also confirmed that UGT1A1 was capable of forming heterodimer complexes with all of the UGT1A proteins, corroborating the FRET results in live cells. These preliminary studies suggest that the UGT1A family of proteins form oligomerized complexes in the membrane, a property that may influence function and substrate selectivity.

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31

Pretheeban, Manoja, Geoff Hammond, Stelvio Bandiera, Wayne Riggs, and Dan Rurak. "Ontogenesis of UDP-glucuronosyltransferase enzymes in sheep." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 159, no. 2 (June 2011): 159–66. http://dx.doi.org/10.1016/j.cbpa.2011.02.014.

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32

Boutin, Jean A., Jacques Thomassin, Gerard Siest, and Alain Cartier. "Heterogeneity of hepatic microsomal UDP-glucuronosyltransferase activities." Biochemical Pharmacology 34, no. 13 (July 1985): 2235–49. http://dx.doi.org/10.1016/0006-2952(85)90777-4.

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33

Lizák, Beáta, Ibolya Czegle, Miklós Csala, Angelo Benedetti, József Mandl, and Gábor Bánhegyi. "Translocon pores in the endoplasmic reticulum are permeable to small anions." American Journal of Physiology-Cell Physiology 291, no. 3 (September 2006): 511–17. http://dx.doi.org/10.1152/ajpcell.00274.2005.

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Contribution of translocon peptide channels to the permeation of low molecular mass anions was investigated in rat liver microsomes. Puromycin, which purges translocon pores of nascent polypeptides, creating additional empty pores, raised the microsomal uptake of radiolabeled UDP-glucuronic acid, while it did not increase the uptake of glucose-6-phosphate or glutathione. The role of translocon pores in the transport of small anions was also investigated by measuring the effect of puromycin on the activity of microsomal enzymes with intraluminal active sites. The mannose-6-phosphatase activity of glucose-6-phosphatase and the activity of UDP-glucuronosyltransferase were elevated upon addition of puromycin, but glucose-6-phosphatase and β-glucuronidase activities were not changed. The increase in enzyme activities was due to a better access of the substrates to the luminal compartment rather than to activation of the enzymes. Antibody against Sec61 translocon component decreased the activity of UDP-glucuronosyltransferase and antagonized the effect of puromycin. Similarly, the addition of the puromycin antagonist anisomycin or treatments of microsomes, resulting in the release of attached ribosomes, prevented the puromycin-dependent increase in the activity. Mannose-6-phosphatase and UDP-glucuronosyltransferase activities of smooth microsomal vesicles showed higher basal latencies that were not affected by puromycin. In conclusion, translationally inactive, ribosome-bound translocons allow small anions to cross the endoplasmic reticulum membrane. This pathway can contribute to the nonspecific substrate supply of enzymes with intraluminal active centers.

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34

Muñoz, Maria E., Alejandro Esteller, and Javier González. "Substrate induction of bilirubin conjugation and biliary excretion in the rat." Clinical Science 73, no. 4 (October 1, 1987): 371–75. http://dx.doi.org/10.1042/cs0730371.

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1. The effect of high bilirubin loads (60 μmol/kg twice daily for 2 days) on glucuronosyltransferase activity and biliary excretion of bilirubin was studied in Wistar rats. 2. The concentration of bilirubin in serum increased from 1.1 μmol/l in controls to 5.5 μmol/l after bilirubin pretreatment. 3. Bilirubin pretreatment led to a 25% increase in hepatic UDP-glucuronosyltransferase activity. Bilirubin Tm, was increased by 22% and correlated positively with glucuronosyltransferase activity. 4. The output of conjugated bilirubin in bile was enhanced but no changes in the proportion of monoconjugates to diconjugates were observed. 5. Our data suggest that prolonged treatment with bilirubin can increase biliary bilirubin excretion by inducing glucuronosyltransferase activity.

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Volkov, A. N. "Population genetic research of the mutation in ugt1a1 gene associated with reduced activity of liver UDP-glucuronosyltransferase A1." Fundamental and Clinical Medicine 5, no. 3 (September 30, 2020): 59–65. http://dx.doi.org/10.23946/2500-0764-2020-5-3-59-65.

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Aim. To explore allele and genotype frequencies of the rs8175347 polymorphism within the UGT1A1 gene in Kemerovo Region. Materials and Methods. The study sample included 64 male and 68 female inhabitants of the Kemerovo Region. Upon DNA isolation from the peripheral blood leukocytes, we conducted allele-specific polymerase chain reaction followed by electrophoretic detection of the genotype. Results. The frequency of minor allele *28 of rs8175347 polymorphism, which is associated with the downregulation of UDP-glucuronosyltransferase А1 in the liver, was 33.3%, while the frequency of *28/*28 genotype was 13.6% and did not significantly differ in the examined men and women. Conclusion. High frequency of the *28/*28 genotype in the studied sample suggests a high prevalence of reduced UDP-glucuronosyltransferase А1 activity and associated conditions including Gilbert’s syndrome and adverse drug reactions.

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Noort, D., N. C. R. van Straten, G. J. P. H. Boons, G. A. van der Marel, X. Bossuyt, N. Blanckaert, G. J. Mulder, and J. H. van Boom. "Synthesis of a potential inhibitor of UDP-glucuronosyltransferase." Bioorganic & Medicinal Chemistry Letters 2, no. 6 (June 1992): 583–88. http://dx.doi.org/10.1016/s0960-894x(01)81202-6.

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Ishii, Yuji, Arief Nurrochmad, and Hideyuki Yamada. "Modulation of UDP-Glucuronosyltransferase Activity by Endogenous Compounds." Drug Metabolism and Pharmacokinetics 25, no. 2 (2010): 134–48. http://dx.doi.org/10.2133/dmpk.25.134.

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De Sandro, Virginie, Rachel Catinot, William Kriszt, André Cordier, and Lysiane Richert. "Male rat hepatic udp-glucuronosyltransferase activity toward thyroxine." Biochemical Pharmacology 43, no. 7 (April 1992): 1563–69. http://dx.doi.org/10.1016/0006-2952(92)90215-5.

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Strassburg, Christian P., Nghia Nguyen, Michael P. Manns, and Robert H. Tukey. "UDP-glucuronosyltransferase activity in human liver and colon." Gastroenterology 116, no. 1 (January 1999): 149–60. http://dx.doi.org/10.1016/s0016-5085(99)70239-8.

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Yokota, Hiroshi, Futoshi Ando, Hidetomo Iwano, and Akira Yuasa. "Inhibitory effects of uridine diphosphate on udp-glucuronosyltransferase." Life Sciences 63, no. 19 (October 1998): 1693–99. http://dx.doi.org/10.1016/s0024-3205(98)00441-x.

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Mackenzie, Peter, Joanna M. Little, and Anna Radominska-Pandya. "Glucosidation of hyodeoxycholic acid by UDP-glucuronosyltransferase 2B7." Biochemical Pharmacology 65, no. 3 (February 2003): 417–21. http://dx.doi.org/10.1016/s0006-2952(02)01522-8.

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Basu, N. K., M. Kovarova, A. Garza, S. Kubota, T. Saha, P. S. Mitra, R. Banerjee, J. Rivera, and I. S. Owens. "Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity." Proceedings of the National Academy of Sciences 102, no. 18 (April 21, 2005): 6285–90. http://dx.doi.org/10.1073/pnas.0407872102.

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VARGAS, M., and M. R. FRANKLIN*. "Intestinal UDP-glucuronosyltransferase activities in rat and rabbit." Xenobiotica 27, no. 5 (January 1997): 413–21. http://dx.doi.org/10.1080/004982597240406.

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Loureiro, Ana I., Carlos Fernandes-Lopes, Maria J. Bonifácio, Lyndon C. Wright, and Patricio Soares-da-Silva. "Hepatic UDP-Glucuronosyltransferase Is Responsible for Eslicarbazepine Glucuronidation." Drug Metabolism and Disposition 39, no. 9 (June 14, 2011): 1486–94. http://dx.doi.org/10.1124/dmd.111.038620.

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Soars, M. G., D. J. Smith, R. J. Riley, and B. Burchell. "Cloning and Characterization of a Canine UDP-Glucuronosyltransferase." Archives of Biochemistry and Biophysics 391, no. 2 (July 2001): 218–24. http://dx.doi.org/10.1006/abbi.2001.2383.

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Mojarrabi, Behnaz, and Peter I. Mackenzie. "The Human UDP Glucuronosyltransferase, UGT1A10, Glucuronidates Mycophenolic Acid." Biochemical and Biophysical Research Communications 238, no. 3 (September 1997): 775–78. http://dx.doi.org/10.1006/bbrc.1997.7388.

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YANG, EUN K., KHOSROW KASHFI, JAYANTA ROY CHOWDHURY, NAMITA ROY CHOWDHURY, and ANDREW J. DANNENBERG. "Phenolic Antioxidants Induce UDP-glucuronosyltransferase in Rat Livera." Annals of the New York Academy of Sciences 768, no. 1 (September 1995): 231–36. http://dx.doi.org/10.1111/j.1749-6632.1995.tb12128.x.

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Fladvad, Torill, Pål Klepstad, Mette Langaas, Ola Dale, Stein Kaasa, Augusto Caraceni, and Frank Skorpen. "Variability in UDP-glucuronosyltransferase genes and morphine metabolism." Pharmacogenetics and Genomics 23, no. 3 (March 2013): 117–26. http://dx.doi.org/10.1097/fpc.0b013e32835ce485.

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Congiu, Mario, Maurice L. Mashford, John L. Slavin, and Paul V. Desmond. "UDP Glucuronosyltransferase mRNA Levels in Human Liver Disease." Drug Metabolism and Disposition 30, no. 2 (February 1, 2002): 129–34. http://dx.doi.org/10.1124/dmd.30.2.129.

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MARUO, Yoshihiro, and Hiroshi SATO. "Proteins in Response to Environmental Stress. UDP-glucuronosyltransferase." Nippon Eiseigaku Zasshi (Japanese Journal of Hygiene) 56, no. 4 (2002): 629–33. http://dx.doi.org/10.1265/jjh.56.629.

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