Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA

Jackson, Michael R.; McCarthy, L.; Harding, David; Wilson, Samuel H.; Coughtrie, Michael W.H.; Burchell, Brian

doi:10.1042/bj2420581

Cited by 108 publications

(48 citation statements)

References 44 publications

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“…The comparison of lanes 1 and 2 with lane 3 revealed two additional faster migrating polypeptides of 50 and 52 kDa, when the translation was performed in the presence of dog pancreatic microsomes. They correspond to the cleaved protein and cleaved plus glycosylated protein, respectively, in agreement with the presence of a signal sequence and one potential N-glycosylation site identified from the nucleotide sequence of the eDNA [7]. Radiolabelled proteins immunoprecipitable with specific anti-UDPGT antisera could only be seen with HLUG25-RNA in the correct orientation (not shown).…”

Section: Expression Of Udpgtprotein In Vitro and In Cos-7 Cells In Cusupporting

confidence: 74%

“…A eDNA clone (HLUG25) encoding the complete sequence of a human liver UDPGT was isolated in this laboratory from a Agtl I human liver eDNA library as previously described [7].…”

Section: Cloning Of Full-length Cdna Hlug25mentioning

confidence: 99%

“…The human liver HLUG25 eDNA (2104 basepairs long) [7] was expressed in both in vivo and in vitro systems. HLUG25-RNA was transcribed from a Gemini vector and, when translated in vitro, produced a 53 kDa polypeptide ( fig.lA, lanes 1 and 2).…”

Section: Expression Of Udpgtprotein In Vitro and In Cos-7 Cells In Cumentioning

confidence: 99%

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Expression of a human liver cDNA encoding a UDP‐glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture

Fournel‐Gigleux¹,

Jackson²,

Wooster³

et al. 1989

FEBS Letters

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A cDNA encoding a human liver UDPGT (HLUG 25) transcribed and translated in vitro showed that the encoded protein was synthesized as a precursor and was cleaved and glycosylated when dog pancreatic microsomes were present during translation. The UDP(3T cDNA was transiently expressed in mammalian cell culture (COS-7 cells) resulting in the biosynthesis of a polypeptide of 52 kDa. This expressed UDPGT glycoprotein catalysed the glucuronidation of hyodcoxycholic acid forming an ether glucuronide. These results suggest that this UDPGT isoenzyme may be responsible for the glucuronidation of 6~-hydroxy bile acids in human liver.

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Section: Expression Of Udpgtprotein In Vitro and In Cos-7 Cells In Cusupporting

confidence: 74%

“…A eDNA clone (HLUG25) encoding the complete sequence of a human liver UDPGT was isolated in this laboratory from a Agtl I human liver eDNA library as previously described [7].…”

Section: Cloning Of Full-length Cdna Hlug25mentioning

confidence: 99%

See 1 more Smart Citation

Expression of a human liver cDNA encoding a UDP‐glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture

Fournel‐Gigleux¹,

Jackson²,

Wooster³

et al. 1989

FEBS Letters

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show abstract

“…98,144,148,155,[163][164][165][166][167][168][169] UGT2B4 is expressed in the liver and in a wide range of extrahepatic Pharmacogenomics of human UGT enzymes C Guillemette tissues. 98,144 One common polymorphism has been found in the UGT2B4 gene and the resulting variant allele is designated as UGT2B4 Asp 458 Glu (UGT2B4*2).…”

Section: Ugt2b4mentioning

confidence: 99%

Pharmacogenomics of human UDP-glucuronosyltransferase enzymes

2003

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UDP-glucuronosyltransferase (UGT) enzymes comprise a superfamily of key proteins that catalyze the glucuronidation reaction on a wide range of structurally diverse endogenous and exogenous chemicals. Glucuronidation is one of the major phase II drug-metabolizing reactions that contributes to drug biotransformation. This biochemical process is also involved in the protection against environmental toxicants, carcinogens, dietary toxins and participates in the homeostasis of numerous endogenous molecules, including bilirubin, steroid hormones and biliary acids. Over the years, significant progress was made in the field of glucuronidation, especially with regard to the identification of human UGTs, study of their tissue distribution and substrate specificities. More recently, the degree of allelic diversity has also been revealed for several human UGT genes. Some polymorphic UGTs have demonstrated a significant pharmacological impact in addition to being relevant to drug-induced adverse reactions and cancer susceptibility. This review focuses on human UGTs, the description of the nature of polymorphic variations and their functional impact. The pharmacogenomic implication of polymorphic UGTs is presented, more specifically the role of UGT polymorphisms in modifying cancer risk and their impact on individual risk to drug-induced toxicities.

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“…A cDNA clone (HLUG 25) encoding the complete sequence bilirubin UDPGTwas isolated from a 2gtl 1 human liver cDNA library (Jackson of a et al, 1987). ~fhe sequence of HLUG 25 cDNA was determined to be 2,104 basepair long, including a poly(A) tail a long open reading frame.…”

Section: ) Dna Probementioning

confidence: 99%

Gene mapping of human bilirubin UDP-glucuronosyl transferase on 1q21-q23 by a cell sorter andin situ hybridization

et al. 1991

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SummaryThe human liver bilirubin UDP-glucuronosyl transferase (bilirubin UDPGT) [EC 2.4.1.17] is responsible for the enzyme deficiency in Crigler-Najjar syndrome and/or Gilbert's syndrome. The UDPGT, former shows severe jaundice resulted from a complete absence of bilirubin while the latter has a mild manifestation due to a reduction of the enzyme activity. The gene locus of bilirubin UDPGT was mapped to chromosome 1 by spot-blot hybridization using a cell-sorter, and its regional locus was assigned to lq21-q23 by high resolution in situ hybridization.

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Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA

Cited by 108 publications

References 44 publications

Expression of a human liver cDNA encoding a UDP‐glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture

Expression of a human liver cDNA encoding a UDP‐glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture

Pharmacogenomics of human UDP-glucuronosyltransferase enzymes

Gene mapping of human bilirubin UDP-glucuronosyl transferase on 1q21-q23 by a cell sorter andin situ hybridization

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