Di Jeso B, Gentile F
Centro di Endocrinologia e Oncologia Sperimentale del C.N.R., Naples, Italy.
Biochem Biophys Res Commun. 1992 Dec 30;189(3):1624-30. doi: 10.1016/0006-291x(92)90263-k.
FRTL-5 cells were cultured in media containing standard growth factors with or without TSH, plus labeled precursors of N-linked oligosaccharide chains. The thyroglobulin secreted in the medium was purified and fragmented with CNBr. Three peptides were identified by NH2-terminal sequencing, that were labeled mainly with D-[2-3H]mannose, independent of TSH. One of them, corresponding to the NH2-terminus of thyroglobulin, incorporated both more D-[2-3H]mannose and more D-[1-3H]galactose upon TSH addition. These data likely reflect a TSH-induced increment of N-linked glycosylation at the NH2-terminus of thyroglobulin, mostly with the maturation of high-mannose to complex chains.
FRTL-5细胞在含有标准生长因子的培养基中培养，添加或不添加促甲状腺激素（TSH），并加入N-连接寡糖链的标记前体。培养基中分泌的甲状腺球蛋白经纯化后用溴化氰裂解。通过氨基末端测序鉴定出三种肽，它们主要用D-[2-³H]甘露糖标记，与TSH无关。其中一种对应于甲状腺球蛋白的氨基末端，在添加TSH后，其结合的D-[2-³H]甘露糖和D-[1-³H]半乳糖都更多。这些数据可能反映了TSH诱导的甲状腺球蛋白氨基末端N-连接糖基化增加，主要是高甘露糖型向复杂型糖链的成熟。
