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UDP-glucuronosyltransferase 1a enzymes are present and active in the mouse blastocyst.
Collier, Abby C; Yamauchi, Yasuhiro; Sato, Brittany L M; Rougée, Luc R A; Ward, Monika A.
Afiliação
  • Collier AC; Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, British Columbia, Canada (A.C.C.); Department of Tropical Medicine, Medical Microbiology, and Pharmacology (A.C.C., B.L.M.S., L.R.A.R.), and Institute for Biogenesis Research (Y.Y., M.A.W.), John A. Burns School of Medici
  • Yamauchi Y; Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, British Columbia, Canada (A.C.C.); Department of Tropical Medicine, Medical Microbiology, and Pharmacology (A.C.C., B.L.M.S., L.R.A.R.), and Institute for Biogenesis Research (Y.Y., M.A.W.), John A. Burns School of Medici
  • Sato BL; Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, British Columbia, Canada (A.C.C.); Department of Tropical Medicine, Medical Microbiology, and Pharmacology (A.C.C., B.L.M.S., L.R.A.R.), and Institute for Biogenesis Research (Y.Y., M.A.W.), John A. Burns School of Medici
  • Rougée LR; Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, British Columbia, Canada (A.C.C.); Department of Tropical Medicine, Medical Microbiology, and Pharmacology (A.C.C., B.L.M.S., L.R.A.R.), and Institute for Biogenesis Research (Y.Y., M.A.W.), John A. Burns School of Medici
  • Ward MA; Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, British Columbia, Canada (A.C.C.); Department of Tropical Medicine, Medical Microbiology, and Pharmacology (A.C.C., B.L.M.S., L.R.A.R.), and Institute for Biogenesis Research (Y.Y., M.A.W.), John A. Burns School of Medici
Drug Metab Dispos ; 42(11): 1921-5, 2014 Nov.
Article em En | MEDLINE | ID: mdl-25200869
The UDP-glucuronosyltransferase (UGT) enzymes are critical for regulating nutrients, hormones, and endobiotics, as well as for detoxifying xenobiotics. Human and murine fetuses are known to express glucuronidation enzymes, but there are currently no data prior to implantation. Here we addressed this gap in knowledge and tested whether Ugt enzymes are already present in preimplantation-stage embryos. Blastocysts were obtained after in vitro fertilization with gametes from B6D2F1 hybrid mice and from embryo culture. Protein expression and localization were determined using pan-specific UGT1A and UGT2B, as well as anti-human isoform-specific antibodies. Immunofluorescence analysis showed that blastocysts expressed Ugt1a globally, in the cytoplasm and nuclei of all of the cells. Western blots demonstrated the presence of Ugt1a6 but not Ugt1a1, Ugt1a3, Ugt1a4, or Ugt1a9. The Ugt2b proteins were not detected by either assay. The level of Ugt activity in murine blastocysts was comparable with that of the adult human liver (per milligram of protein), but the activity of ß-glucuronidase, an Ugt-partnering enzyme responsible for substrate regeneration, was lower. Altogether, these data confirm that Ugt1a proteins are present and active in preimplantation murine embryos and point to a potential role for these proteins in implantation and early embryonic and fetal development.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Blastocisto / Glucuronosiltransferase Limite: Animals Idioma: En Revista: Drug Metab Dispos Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Blastocisto / Glucuronosiltransferase Limite: Animals Idioma: En Revista: Drug Metab Dispos Ano de publicação: 2014 Tipo de documento: Article