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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >T-CELL-SPECIFIC DELETION OF A POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE GENE BY SITE-DIRECTED RECOMBINATION
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T-CELL-SPECIFIC DELETION OF A POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE GENE BY SITE-DIRECTED RECOMBINATION

机译：通过位点定向重组特异性去除多肽N-乙酰半乳糖胺基转移酶基因的T细胞

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摘要

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 the possibility of multiple polypeptide GalNAc-Ts, although attachment of saccharide units to polypeptide or lipid in generating oligosaccharide structures in vertebrates has been dependent upon the activity of single gene products. To address this issue and to determine the relevance of O-glycosylation variation in T-cell ontogeny; we have directed Cre/loxP mutagenic recombination to the polypeptide GalNAc-T locus in gene-targeted mice, Resulting deletion in the catalytic region of polypeptide GalNAc-T occurred to completion on both alleles in thymocytes and was found in peripheral T cells, but not among other cell types. Thymocyte O-linked oligosaccharide formation persisted in the absence of a functional targeted polypeptide GalNAc-T allele as determined by O-glycan-specific lectin binding, T-cell development and colonization of secondary lymphoid organs were also normal, These results indicate a complexity in vertebrate O-glycan biosynthesis that involves multiple polypeptide GalNAc-Ts, We infer the potential for protein-specific O-glycan formation governed by distinct polypeptide GalNAc-Ts.
机译：UDP-N-乙酰半乳糖胺（GalNAc）：多肽N-乙酰半乳糖胺基转移酶（多肽GalNAc-T）催化单糖GalNAc转移至丝氨酸和苏氨酸残基，从而启动O-连接寡糖的生物合成，先前的研究表明可能存在多个多肽GalNAc-的可能性Ts，尽管在脊椎动物中产生寡糖结构中糖单位附着于多肽或脂质上一直依赖于单一基因产物的活性。为了解决这个问题并确定T细胞个体发育中O-糖基化变异的相关性；我们已将Cre / loxP诱变重组定向到基因靶向小鼠中的多肽GalNAc-T基因座上，导致多肽GalNAc-T催化区域中的缺失在胸腺细胞的两个等位基因上完全发生，但在外周T细胞中发现了在其他细胞类型中。胸腺细胞O-连接寡糖的形成在没有功能性靶向多肽GalNAc-T等位基因的情况下持续存在，这是通过O-聚糖特异性凝集素结合确定的，T细胞发育和次级淋巴器官的定殖也很正常。这些结果表明，涉及多个多肽GalNAc-Ts的脊椎动物O-聚糖生物合成，我们推断了由不同多肽GalNAc-Ts调控的蛋白质特异性O-聚糖形成的潜力。

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