生物
整合素
细胞生物学
合胞滋养细胞
滋养层
焦点粘着
细胞粘附
细胞迁移
细胞外基质
信号转导
胎盘
细胞
生物化学
胎儿
遗传学
怀孕
作者
Wen‐Chieh Liao,Chi‐Hau Chen,Chiung‐Hui Liu,M.-J. Huang,Chia‐Chang Chen,Ji‐Shiang Hung,Cheng‐Chung Chou,Chi‐Hau Chen,Mei‐Ieng Che,Horng-Rong Chang,Chyn‐Tair Lan,Hsiu‐Chin Huang,Guo‐Fang Tseng,Ming‐Kwang Shyu,Min‐Chuan Huang
出处
期刊:Placenta
[Elsevier]
日期:2012-12-01
卷期号:33 (12): 1005-1011
被引量:23
标识
DOI:10.1016/j.placenta.2012.08.007
摘要
Extravillus trophoblast (EVT) invasion plays a critical role in placental development. Integrins bind to extracellular matrix (ECM) proteins to mediate EVT cell adhesion, migration, and invasion. Changes in O-glycans on β1-integrin have been found to regulate cancer cell behavior. We hypothesize that O-glycosyltransferases can regulate EVT invasion through modulating the glycosylation and function of β1-integrin. Here, we found that the GALNT1 and GALNT2 mRNA were highly expressed in HTR8/SVneo and first trimester EVT cells. Immunohistochemstry and immunofluorescence staining showed that GALNT2 was expressed in subpopulations of EVT cells in deciduas, but not in syncytiotrophoblasts and cytotrophoblasts of placental villi. The percentage of GALNT2-positive EVT cells increased with gestational ages. Overexpression of GALNT2 in HTR8/SVneo cells significantly enhanced cell-collagen IV adhesion, but suppressed cell migration and invasion. Notably, we found that GALNT2 increased the expression of Tn antigen (GalNAc-Ser/Thr) on β1-integrin as revealed by Vicia Villosa agglutinin (VVA) binding. Furthermore, GALNT2 suppressed the phosphorylation of focal adhesion kinase (FAK), a crucial downstream signaling molecule of β1-integrin. Our findings suggest that GALNT2 is a critical initiating enzyme of O-glycosylation for regulating EVT invasion.
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