A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini.

Ritter, Joseph K.; Fan, Chen; Sheen, Yhun Yhong; Tran, H. M.; Kimura, S.; Yeatman, Matthew T.; Owens, Ida S.

doi:10.1016/s0021-9258(19)50724-4

Cited by 428 publications

(32 citation statements)

References 13 publications

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“…Ayalew (2016) also reported a higher total phenol content ranged from 26.42-59.9 mg/g GAE for the leaves of Anchote accessions. According to the study by Ritter et al (1992), when the total polyphenol content in all the vegetables tested measured, there was a significant inverse correlation with Iron absorption. A number of vegetables associated with low Iron absorption turned bluish-black when Iron added to them, suggesting that the total polyphenol content in them was high.…”

Section: Total Phenol Contentsmentioning

confidence: 95%

Nutritional and phenolic profiles of leaves of fifteen Anchote (Coccinia abyssinica) accessions

Gemede

Merga

Dufera

et al. 2021

Cogent Food & Agriculture

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The purpose of this study was to evaluate the nutritional and phenolic compositions of leaves of Anchote (Coccinia abyssinica) accessions grown in East Wollega Zone (Nekemte), Ethiopia. Leaves of fifteen accessions of Anchote were collected from research farm of Wollega University Ethiopia. The dried leaves of each accession were grounded separately into fine powder following standard procedures. Thereafter, the proximate, mineral, and phenolic compositions were determined according to published official standard procedures with grade chemicals and reagents. Mineral ratios were considered to examine mineral-mineral interactions and antinutrient/mineral molar ratios were calculated to predict minerals bioavailability. Principal component analysis (PCA) and cluster analyses were conducted to characterize the accessions based on nutritional and mineral traits. Proximate compositions (% dwb) except moisture content were varied significantly (P < 0.05) and ranged: moisture 9.21-10.15, crude protein 16.88−29.84, crude fiber 8.52-12.07, crude fat 2.03-4.19, total ash 10.06-17.27, utilizable carbohydrate 37.45-46.36 and gross energy 272.67-293.11 kcal/100 g. PCA of proximate traits showed 74.15% variation for two principal components and the accessions categorized into three clusters. Mineral contents (mg/100 g dwb) were significantly varied (P < 0.05) and ranged: calcium (79.66-100.68), magnesium (31.18-68.47), sodium (41.32-71.95), potassium (71.79--111.13), phosphorus (42.07-66.9), Iron (3.68-11.51) and zinc (1.02-3.11). PCA of mineral traits showed 69.30% variation for two principal components and the accessions grouped into three clusters. Results of phenolic analyses were significantly varied Habtamu Fekadu Gemede

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Section: Total Phenol Contentsmentioning

confidence: 95%

Nutritional and phenolic profiles of leaves of fifteen Anchote (Coccinia abyssinica) accessions

Gemede

Merga

Dufera

et al. 2021

Cogent Food & Agriculture

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“…UGT1A6 is widely expressed in human tissues at variable levels, including the liver, kidney, GI tract (stomach, small intestine, colon), trachea, brain, adrenal, bladder, ovary, and lung (55,134,354,513,544,618). The UGT1A6 proximal promoter contains three TATA boxes that function in a cell type-specific manner (501,599): all three TATA boxes are active in human liver; however, differen- UGT1A7 is expressed in the aerodigestive tract (e.g., oral cavity, pharyngeal and laryngeal mucosa, esophagus, stomach, small intestine, colon) as well as cervix, trachea, kidney, and bladder (134,513,544,796,798); however, it is absent from the liver. The UGT1A7 proximal promoter has a functionally polymorphic TATA box with the rarer variant (MAF 0.29) showing~30% of the promoter activity of the common variant (386).…”

Section: Constitutive Expression Of Ugt1 Family Genesmentioning

confidence: 99%

The UDP-Glycosyltransferase (UGT) Superfamily: New Members, New Functions, and Novel Paradigms

Meech

McKinnon

et al. 2019

Physiological Reviews

250

168

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UDP-glycosyltransferases (UGTs) catalyze the covalent addition of sugars to a broad range of lipophilic molecules. This biotransformation plays a critical role in elimination of a broad range of exogenous chemicals and by-products of endogenous metabolism, and also controls the levels and distribution of many endogenous signaling molecules. In mammals, the superfamily comprises four families: UGT1, UGT2, UGT3, and UGT8. UGT1 and UGT2 enzymes have important roles in pharmacology and toxicology including contributing to interindividual differences in drug disposition as well as to cancer risk. These UGTs are highly expressed in organs of detoxification (e.g., liver, kidney, intestine) and can be induced by pathways that sense demand for detoxification and for modulation of endobiotic signaling molecules. The functions of the UGT3 and UGT8 family enzymes have only been characterized relatively recently; these enzymes show different UDP-sugar preferences to that of UGT1 and UGT2 enzymes, and to date, their contributions to drug metabolism appear to be relatively minor. This review summarizes and provides critical analysis of the current state of research into all four families of UGT enzymes. Key areas discussed include the roles of UGTs in drug metabolism, cancer risk, and regulation of signaling, as well as the transcriptional and posttranscriptional control of UGT expression and function. The latter part of this review provides an in-depth analysis of the known and predicted functions of UGT3 and UGT8 enzymes, focused on their likely roles in modulation of levels of endogenous signaling pathways.

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“…exon-1 sequences is followed by common exons 2-5 [2]. UGT1A gene products are generated by a strategy of exon sharing, which combines the individual first exons and common exons 2-5 to form unique UGT transcripts [11]. The analysis of UGT1A gene products has led to the cloning of cDNAs that encode UGT1A1 [12], UGT1A3 [13], UGT1A4 [12], UGT1A6 [14] and UGT1A9 [15] from human liver.…”

Section: Introductionmentioning

confidence: 99%

Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus

Strassburg¹,

STRASSBURG²,

Nguyen³

et al. 1999

Biochem. J.

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Human UDP-glucuronosyltransferases (UGTs) are expressed in a tissue-specific fashion in hepatic and extrahepatic tissues [Strassburg, Manns and Tukey (1998) J. Biol. Chem. 273, 8719-8726]. Previous work suggests that these enzymes play a protective role in chemical carcinogenesis [Strassburg, Manns and Tukey (1997) Cancer Res. 57, 2979-2985]. In this study, UGT1 and UGT2 gene expression was investigated in human oesophageal epithelium and squamous-cell carcinoma in addition to the characterization of individual UGT isoforms using recombinant protein. UGT mRNA expression was characterized by duplex reverse transcriptase-PCR analysis and revealed the expression of UGT1A7, UGT1A8, UGT1A9 and UGT1A10 mRNAs. UGT1A1, UGT1A3, UGT1A4, UGT1A5 and UGT1A6 transcripts were not detected. UGT2 expression included UGT2B7, UGT2B10 and UGT2B15, but UGT2B4 mRNA was absent. UGT2 mRNA was present at significantly lower levels than UGT1 transcripts. This observation was in agreement with the analysis of catalytic activities in oesophageal microsomal protein, which was characterized by high glucuronidation rates for phenolic xenobiotics, all of which are classical UGT1 substrates. Whereas UGT1A9 was not regulated, differential regulation of UGT1A7 and UGT1A10 mRNA was observed between normal oesophageal epithelium and squamous-cell carcinoma. Expression and analysis in vitro of recombinant UGT1A7, UGT1A9, UGT1A10, UGT2B7 and UGT2B15 demonstrated that UGT1A7, UGT1A9 and UGT1A10 catalysed the glucuronidation of 7-hydroxybenzo(alpha)pyrene, as well as other environmental carcinogens, such as 2-hydroxyamino-1-methyl-6-phenylimidazo-(4, 5-beta)-pyridine. Although UGT1A9 was not regulated in the carcinoma tissue, the five-fold reduction in 7-hydroxybenzo(alpha)pyrene glucuronidation could be attributed to regulation of UGT1A7 and UGT1A10. These data elucidate an individual regulation of human UGT1A and UGT2B genes in human oesophagus and provide evidence for specific catalytic activities of individual human UGT isoforms towards environmental carcinogens that have been implicated in cellular carcinogenesis.

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A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini.

Cited by 428 publications

References 13 publications

Nutritional and phenolic profiles of leaves of fifteen Anchote (Coccinia abyssinica) accessions

Nutritional and phenolic profiles of leaves of fifteen Anchote (Coccinia abyssinica) accessions

The UDP-Glycosyltransferase (UGT) Superfamily: New Members, New Functions, and Novel Paradigms

Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus

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