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细胞表面半乳糖基转移酶（ＧａｌＴａｓｅ）是层粘连蛋白（ＬＮ）非整合素类受体，能与其上寡糖链的Ｎ－乙酰葡糖胺（ＧｌｃＮＡｃ）残基识别和结合。作者从妊娠第８．５天雌鼠子宫蜕膜中剥离胚胎，显微分离外胎盘锥（ＥＰＣ）后进行体外培养。用（１）ＬＮ预先半乳糖基化；（２）外源ＧｌｃＮＡｃ底物竞争；（３）ＧａｌＴａｓｅ抗体阻断；（４）α乳清蛋白处理等方法干扰滋养层细胞与ＬＮ的相互作用，均对ＥＰＣ粘附无影响，但抑制ＥＰＣ扩展和次生滋养层巨细胞（ＳＴＧＣｓ）迁移。证明ＧａｌＴａｓｅ虽不参与ＥＰＣ起初的粘附，但通过与ＬＮ寡糖链上ＧｌｃＮＡｃ的结合介导ＥＰＣ扩展和ＳＴＧＣｓ迁移。
Cell surface galactosyltransferase (GalTase) is a laminin (LN) non-integrin receptor that recognizes and binds to N-acetylglucosamine (GlcNAc) residues on the oligosaccharide chain. The embryos were detached from the decidua of uterus of female mice on the 8.5th day of gestation. The embryos were dissected microscopically and then cultured in vitro. Pre-galactosylation with (1) LN; (2) exogenous GlcNAc substrate competition; (3) GalTase antibody blocking; (4) alpha lactalbumin treatment interferes with the interaction of trophoblast cells with LN, No effect on EPC adhesion, but inhibition of EPC expansion and secondary trophoblastic giant cell (STGCs) migration. Although GalTase was not involved in the initial adhesion of EPC, it was demonstrated that GalTase mediated EPC expansion and STGCs migration by binding to GlcNAc on the oligosaccharide oligosaccharide chain.