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XB-ART-49967
Comp Biochem Physiol B Biochem Mol Biol February 1, 2015; 180 40-7.
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Biological and biochemical properties of two Xenopus laevis N-acetylgalactosaminyltransferases with contrasting roles in embryogenesis.

Voglmeir J , Laurent N , Flitsch SL , Oelgeschläger M , Wilson IB .


Abstract
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-β/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-β/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.

PubMed ID: 25447273
PMC ID: PMC4291152
Article link: Comp Biochem Physiol B Biochem Mol Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: actl6a acvr2b galnt1 galnt16 ncoa3 nog odc1 six3


Article Images: [+] show captions
References [+] :
Bennett, Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. 2012, Pubmed