T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination

摘要: Abstract UDP-N-acetylgalactosamine (GalNAc): polypeptide N-acetylgalactosaminyltransferase (polypeptide GalNAc-T) catalyzes transfer of the monosaccharide GalNAc to serine and threonine residues, thereby initiating O-linked oligosaccharide biosynthesis. Previous studies have suggested possibility multiple GalNAc-Ts, although attachment saccharide units or lipid in generating structures vertebrates has been dependent upon activity single gene products. To address this issue determine relevance Oglycosylation variation T-cell ontogeny, we directed Cre/loxP mutagenic recombination GalNAc-T locus gene-targeted mice. Resulting deletion catalytic region occurred completion on both alleles thymocytes was found peripheral T cells, but not among other cell types. Thymocyte formation persisted absence a functional targeted allele as determined by O-glycan-specific lectin binding. development colonization secondary lymphoid organs were also normal. These results indicate complexity vertebrate O-glycan biosynthesis that involves GalNAc-Ts. We infer potential for protein-specific governed distinct