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Artykuły w czasopismach na temat „UDP-glucuronosyltransferase”

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Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 lipca 2025

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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 (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

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2

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 (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-p

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3

Falany, C. N., M. D. Green, E. Swain та T. R. Tephly. "Substrate specificity and characterization of rat liver p-nitrophenol, 3 α-hydroxysteroid and 17 β-hydroxysteroid UDP-glucuronosyltransferases". Biochemical Journal 238, № 1 (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 endog

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4

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

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5

BÁNHEGYI, Gábor, László BRAUN, Paola MARCOLONGO, et al. "Evidence for an UDP-glucuronic acid/phenol glucuronide antiport in rat liver microsomal vesicles." Biochemical Journal 315, no. 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) glucuro

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6

Little, J. M., R. Lester, F. Kuipers, et al. "Variability of human hepatic UDP-glucuronosyltransferase activity." Acta Biochimica Polonica 46, no. 2 (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 U

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7

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

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8

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

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9

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 (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 isoform

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10

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 (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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11

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 (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

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12

Green, M. D., C. N. Falany, R. B. Kirkpatrick та T. R. Tephly. "Strain differences in purified rat hepatic 3 α-hydroxysteroid UDP-glucuronosyltransferase". Biochemical Journal 230, № 2 (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 Chromatofocusi

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13

Mackenzie, P., P. Gregory, D. Gardner-Stephen, et al. "Regulation of UDP Glucuronosyltransferase Genes." Current Drug Metabolism 4, no. 3 (2003): 249–57. http://dx.doi.org/10.2174/1389200033489442.

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14

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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15

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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16

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

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17

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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18

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

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19

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

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20

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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21

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

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22

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 (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

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23

Muñoz, Maria E., Alejandro Esteller, and Javier González. "Substrate induction of bilirubin conjugation and biliary excretion in the rat." Clinical Science 73, no. 4 (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 monoconjug

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24

Bossuyt, X., and N. Blanckaert. "Mechanism of stimulation of microsomal UDP-glucuronosyltransferase by UDP-N-acetylglucosamine." Biochemical Journal 305, no. 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 t

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25

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 (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 g

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26

Toide, Kenji, Shin-ichiro Umeda, Hiroshi Yamazaki, et al. "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

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 (2014): 421–58. http://dx.doi.org/10.3109/03602532.2014.973037.

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28

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

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29

Operaña, Theresa N., and Robert H. Tukey. "Oligomerization of the UDP-glucuronosyltransferase 1A Proteins." Journal of Biological Chemistry 282, no. 7 (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 UGT

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30

DEBINSKI, HENRY S., PETER I. MACKENZIE, C. SOON LEE, et al. "UDP glucuronosyltransferase in the cirrhotic rat liver." Journal of Gastroenterology and Hepatology 11, no. 4 (1996): 373–79. http://dx.doi.org/10.1111/j.1440-1746.1996.tb01386.x.

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31

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

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32

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

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33

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

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34

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 (2011): 159–66. http://dx.doi.org/10.1016/j.cbpa.2011.02.014.

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35

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

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36

Tian, Xiang-Ge, Chao Wang, Guang-Bo Ge, et al. "A highly selective probe for UDP-glucuronosyltransferase 2B7 (UGT2B7) in human microsomes: isoform specificity, kinetic characterization, and applications." RSC Advances 5, no. 8 (2015): 5924–27. http://dx.doi.org/10.1039/c4ra09819f.

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3-Epideacetycinobufagin (EDCB) was found to be a highly isoform-specific probe for 3-glucuronidation mediated by UDP-glucuronosyltransferase 2B7 (UGT2B7). The reaction was well-characterized, suggesting that EDCB can be used to measure the catalytic activity of UGT2B7.

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37

BOSSUYT, Xavier, and Norbert BLANCKAERT. "Uridine diphosphoxylose enhances hepatic microsomal UDP-glucuronosyltransferase activity by stimulating transport of UDP-glucuronic acid across the endoplasmic reticulum membrane." Biochemical Journal 315, no. 1 (1996): 189–93. http://dx.doi.org/10.1042/bj3150189.

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The UDP-glucuronosyltransferase (UGT) system fulfils a pivotal role in the biotransformation of potentially toxic endogenous and exogenous compounds. Here we report that the activity of UGT in rat liver is stimulated by UDP-xylose. This stimulation was found in native microsomal vesicles as well as in the intact endoplasmic reticulum (ER) membrane, as studied in permeabilized hepatocytes, indicating the potential physiological importance of UDP-xylose in the regulation of UGT. We present evidence that UDP-xylose enhances UGT activity by stimulation of (i) the uptake of UDP-glucuronic acid acro

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38

Dannenberg, A., M. Rotenberg, and D. Zakim. "Regulation of UDP-glucuronosyltransferase by lipid-protein interactions." Journal of Biological Chemistry 264, no. 1 (1989): 238–42. http://dx.doi.org/10.1016/s0021-9258(17)31249-8.

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39

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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40

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 (2011): 1486–94. http://dx.doi.org/10.1124/dmd.111.038620.

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41

Ando, Yuichi, Hiroshi Ueoka, Toru Sugiyama, Masao Ichiki, Kaoru Shimokata, and Yoshinori Hasegawa. "Polymorphisms of UDP-Glucuronosyltransferase and Pharmacokinetics of Irinotecan." Therapeutic Drug Monitoring 24, no. 1 (2002): 111–16. http://dx.doi.org/10.1097/00007691-200202000-00018.

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42

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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43

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

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44

Basu, N. K., M. Kovarova, A. Garza, et al. "Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity." Proceedings of the National Academy of Sciences 102, no. 18 (2005): 6285–90. http://dx.doi.org/10.1073/pnas.0407872102.

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45

Fladvad, Torill, Pål Klepstad, Mette Langaas, et al. "Variability in UDP-glucuronosyltransferase genes and morphine metabolism." Pharmacogenetics and Genomics 23, no. 3 (2013): 117–26. http://dx.doi.org/10.1097/fpc.0b013e32835ce485.

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46

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

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47

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

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48

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

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YANG, E. "Effect of dietary composition on bilirubin-UDP-glucuronosyltransferase." Hepatology 18, no. 4 (1993): A127. http://dx.doi.org/10.1016/0270-9139(93)92036-y.

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