Tissue-Specific 2,3,7,8-Tetrachlorodibenzo-p-dioxin-Inducible Expression of Human UDP-Glucuronosyltransferase UGT1A6

Münzel, Peter A.; Bookjans, Gerhard; Mehner, Gernot; Lehmköster, Tobias; Bock, Karl Walter

doi:10.1006/abbi.1996.0499

Cited by 50 publications

(21 citation statements)

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“…at ASPET Journals on May 11, 2018 dmd.aspetjournals.org identified in many tissues such as liver, kidney (Ouzzine et al, 1994), brain (Martinasevic et al, 1998;Gradinaru et al, 1999), lung (Münzel et al, 1996), and intestine (Strassburg et al, 2000). Expression of UGT1A6 has been demonstrated in human liver and in the intestine with large interindividual differences (Münzel et al, 1993).…”

Section: Pal Glucuronidation By Ugt1a6mentioning

confidence: 99%

UDP-Glucuronosyltransferase 1A6 Is the Major Isozyme Responsible for Protocatechuic Aldehyde Glucuronidation in Human Liver Microsomes

Liu

Liu²,

Jiangwei³

et al. 2008

Drug Metab Dispos

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Section: Pal Glucuronidation By Ugt1a6mentioning

confidence: 99%

UDP-Glucuronosyltransferase 1A6 Is the Major Isozyme Responsible for Protocatechuic Aldehyde Glucuronidation in Human Liver Microsomes

Liu

Liu²,

Jiangwei³

et al. 2008

Drug Metab Dispos

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“…The low activity and UGT1A6 protein content in the pooled intestinal microsomes indicate that UGT1A6 expression in intestine is much lower than in liver (averaging less than 5% that of liver). Expression of UGT1A6 has been demonstrated in human duodenum with large interindividual differences in the level of mRNA (Munzel et al, 1996). Compared with liver, significantly lower UGT1A6 activity has been shown in intestinal microsomes on a per milligram of microsomal protein basis (Fisher et al, 2000).…”

Section: Enzyme Kinetics Of Serotonin Glucuronidation By Representatimentioning

confidence: 99%

“…UGT1A6 is an important UGT isoform known to catalyze the glucuronidation of planar and short aromatic molecules, including drugs such as acetaminophen and potential carcinogens chemically related to hydroxylated polycyclic aryl hydrocarbons (Bock et al, 1993). In humans, UGT1A6 is expressed in liver, kidney (Ouzzine et al, 1994), brain (Martinasevic et al, 1998;Gradinaru et al, 1999), lung (Munzel et al, 1996), and intestine . The expression of UGT1A6 in human liver has been reported to be extremely variable as shown by assays using specific antibodies (Ouzzine et al, 1994).…”

mentioning

confidence: 99%

Validation of Serotonin (5-Hydroxtryptamine) as an in Vitro Substrate Probe for Human UDP-Glucuronosyltransferase (UGT) 1A6

Krishnaswamy¹,

Duan²,

Moltke³

et al. 2003

Drug Metab Dispos

104

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ABSTRACT:Investigation of human UDP-glucuronosyltransferase (UGT) isoforms has been limited by a lack of specific substrate probes. In this study serotonin was evaluated for use as a probe substrate for human UGT1A6 using recombinant human UGTs and tissue microsomes. Of the 10 commercially available recombinant UGT isoforms, only UGT1A6 catalyzed serotonin glucuronidation. Serotonin-UGT activity at 40 mM serotonin concentration varied more than 40-fold among human livers (n ‫؍‬ 54), ranging from 0.77 to 32.

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“…In general, glucuronidation is thought to serve as an inactivating or protective function by terminating or attenuating the activity of many endogenous, dietary and clinically administered drugs as well as environmental chemicals that have been shown to result in toxicity or carcinogenesis [2]. However, glucuronidation also can result in the generation of bioactive or even toxic compounds, including those of estrogens, morphine, retinoids, bile acids, and heterocyclic aromatic amines [3][4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Identification of UDP-glucuronosyltransferase 1A10 in non-malignant and malignant human breast tissues

2008

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UGT1A10 was recently identified as the major isoform that conjugates estrogens. In this study, realtime PCR revealed high levels of UGT1A10 and UGT2B7 in human breast tissues. The expression of UGT1A10 in breast was a novel finding. UGT1A10 and UGT2B7 mRNAs were differentially expressed among normal and malignant specimens. Their overall expression was significantly decreased in breast carcinomas as compared to normal breast specimens (UGT1A10: 68 ± 26 vs. 252 ± 86, respectively; p < 0.05) and (UGT2B7: 1.4 ± 0.7 vs. 12 ± 4, respectively; p < 0.05). Interestingly, in African American women, UGT1A10 expression was significantly decreased in breast carcinomas in comparison to normals (57 ± 35 vs. 397 ± 152, respectively; p < 0.05). Among Caucasian women, UGT2B7 was significantly decreased in breast carcinomas in comparison to normals (1.1 ± 0.5 vs. 13.5 ± 6, respectively; p < 0.05). Glucuronidation of 4-OHE 1 was significantly reduced in breast carcinomas compared to normals (30 ± 15 vs. 106 ± 31, respectively; p < 0.05). Differential downregulation of UGT1A10 and UGT2B7 mRNA, protein, and activity in breast carcinomas compared to the adjacent normal breast specimens from the same donor were also found. These data illustrate the novel finding of UGT1A10 in human breast and confirm the expression of UGT2B7. Significant individual variation and down-regulation of expression in breast carcinomas of both isoforms was also demonstrated. These findings provide evidence that decreased UGT expression and activity could result in the promotion of carcinogenesis.

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Tissue-Specific 2,3,7,8-Tetrachlorodibenzo-p-dioxin-Inducible Expression of Human UDP-Glucuronosyltransferase UGT1A6

Cited by 50 publications

References 0 publications

UDP-Glucuronosyltransferase 1A6 Is the Major Isozyme Responsible for Protocatechuic Aldehyde Glucuronidation in Human Liver Microsomes

UDP-Glucuronosyltransferase 1A6 Is the Major Isozyme Responsible for Protocatechuic Aldehyde Glucuronidation in Human Liver Microsomes

Validation of Serotonin (5-Hydroxtryptamine) as an in Vitro Substrate Probe for Human UDP-Glucuronosyltransferase (UGT) 1A6

Identification of UDP-glucuronosyltransferase 1A10 in non-malignant and malignant human breast tissues

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