胚胎着床过程中，滋养层细胞与母体子宫内膜上皮细胞间的分子识别和黏附是胚胎成功着床的关键。膜上功能蛋白糖基化方式在这一过程中起着重要作用，但机制尚不清楚。糖基转移酶催化产生不同糖残基，其中N-乙酰氨基葡萄糖转移酶III（GnT-III）是蛋白糖基化调控的关键酶。本项目在我们前期研究基础上，通过比较不同组织和细胞GnT-III、α5β1整合素、E-钙黏素和bis-GlcNAc糖支链的表达和分布差异，建立GnT-III基因沉默和过表达细胞模型，运用蛋白印迹、免疫共沉淀和细胞侵袭等技术，分析GnT-III对α5β1整合素、E-钙黏素上bis-GlcNAc糖支链表达的影响以及糖基化作用对细胞黏附、侵袭的生物学效应，并对相关信号通路的影响进行评价。旨在阐明GnT-III通过功能蛋白N-糖基化对滋养细胞侵袭能力的调控可能是胚胎着床的分子机制之一，为临床不孕症和自然流产等疾病诊治探寻新的分子靶点。

During embryo implantation, embryonic trophectoderm cells become closely identified and attached to the uterine luminal epithelium is crucial for successful implantation. This process is established through a series of precisely choreographed cellular and molecular events, such as protein glycosylation. It has been certified that glycosylation of membrane protein plays an important role in the trophectoderm recognition and attachment. However, the molecular mechanisms remain poorly understood. .During glycosylation, different sugar residues result from glycosyltransferase catalysis. N-Acetyglucosaminyltransferase III (GnT-III) is one of the most important glycosyltransferases. In this project , by comparison of the expression and location of GnT-III, α5β1, E-Cadherin, bis-GlcNAc in different tissues and cells and establishment of cell model in which GnT-III is overexpressed or silenced, the effect of GnT-III on the bis-GlcNAc expression of α5β1, E-Cadherin and glycosylation on cell adhesion and invasion as well as some signaling molecules involved in adhesion and invasion were analyzed by western blot, co-immunoprecipitation, invasion assay and some molecular biology techniques. This study will elucidate that trophectoderm cells invasion could be regulated by glycosylation of membrane protein mediated by GnT-III. It may be one of the mechanisms involved in embryo implantation. This will help to find a new target for infertility and spontaneous abortion.