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Biological and biochemical properties of two Xenopus laevis N-acetylgalactosaminyltransferases with contrasting roles in embryogenesis.
Voglmeir, Josef; Laurent, Nicolas; Flitsch, Sabine L; Oelgeschläger, Michael; Wilson, Iain B H.
Afiliación
  • Voglmeir J; Department für Chemie, Universität für Bodenkultur, Wien, Austria; Manchester Interdisciplinary Biocentre, University of Manchester, UK.
  • Laurent N; Manchester Interdisciplinary Biocentre, University of Manchester, UK.
  • Flitsch SL; Manchester Interdisciplinary Biocentre, University of Manchester, UK.
  • Oelgeschläger M; Max-Planck-Institut für Immunbiologie, Freiburg, Germany.
  • Wilson IB; Department für Chemie, Universität für Bodenkultur, Wien, Austria. Electronic address: iain.wilson@boku.ac.at.
Article en En | MEDLINE | ID: mdl-25447273
The biosynthesis of mucin-type O-linked glycans in animals is initiated by members of the large family of polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts), which play important roles in embryogenesis, organogenesis, adult tissue homeostasis and carcinogenesis. Until now, the mammalian forms of these enzymes have been the best characterized. However, two N-acetylgalactosaminyltransferases (xGalNAc-T6 and xGalNAc-T16) from the African clawed frog (Xenopus laevis), which are most homologous to those encoded by the human GALNT6 and GALNT16 (GALNTL1) genes, were shown to have contrasting roles in TGF-ß/BMP signaling in embryogenesis. In this study we have examined these two enzymes further and show differences in their in vivo function during X. laevis embyrogenesis as evidenced by in situ hybridization and overexpression experiments. In terms of enzymatic activity, both enzymes were found to be active towards the EA2 peptide, but display differential activity towards a peptide based on the sequence of ActR-IIB, a receptor relevant to TGF-ß/BMP signaling. In summary, these data demonstrate that these two enzymes from different branches of the N-acetylgalactosaminyltransferase do not only display differential substrate specificities, but also specific and distinct expression pattern and biological activities in vivo.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Xenopus laevis / N-Acetilgalactosaminiltransferasas Límite: Animals / Humans Idioma: En Revista: Comp Biochem Physiol B Biochem Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2015 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Xenopus laevis / N-Acetilgalactosaminiltransferasas Límite: Animals / Humans Idioma: En Revista: Comp Biochem Physiol B Biochem Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2015 Tipo del documento: Article Pais de publicación: Reino Unido