Complementary expression of HIP, a cell-surface heparan sulfate binding protein, and perlecan at the human fetal-maternal interface.
Complementary expression of HIP, a cell-surface heparan sulfate binding protein, and perlecan at the human fetal-maternal interface.
复制标题
HIP（一种细胞表面硫酸乙酰肝素结合蛋白）和基底膜聚糖在人胎儿-母体界面上的互补表达。
DOI：
10.1095/biolreprod58.4.1075
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发表时间：
1998
影响因子：
3.6
通讯作者：
Carson,DD
中科院分区：
文献类型：
--
作者：
Rohde,LH;Janatpore,MJ;McMaster,MT;Fisher,S;Zhou,Y;Lim,KH;French,M;Hoke,D;Julian,J;Carson,DD
人血绒膜胎盘是细胞滋养层细胞侵入子宫形成的结构。我们实验室以前的研究已经证明了硫酸乙酰肝素蛋白聚糖（HSPGs）及其结合蛋白在体外人滋养层细胞和子宫细胞系之间的相互作用中的作用。在这项研究中，一种新的细胞表面肝素/硫酸乙酰肝素相互作用蛋白（HIP）的mRNA和蛋白质在人滋养层细胞系（即，在整个妊娠期间，检查人细胞滋养层细胞的EAE、JEG和BeWo-和。人胎儿-母体界面的免疫组织化学显示，细胞滋养层细胞中有丰富的HIP表达，合胞体滋养层细胞染色较少，周围基质或蜕膜细胞染色很少或没有。基底膜HSPG抗体染色，串珠素，表现出一种与HIP互补的染色模式。子宫间质中的细胞滋养层，不附连绒毛，显示不太强烈的沉积串珠素。125 I-串珠素与HIP的17个氨基酸合成肽序列的体外结合研究表明，串珠素以高亲和力（KDapp= 0.6 nM）和肝素可降解的方式与HIP肽结合，HIP对肝素/硫酸乙酰肝素具有高亲和力和特异性。此外，HIP抗体在使用正常人细胞滋养层细胞的原代培养物的测定中抑制61-88%的滋养层细胞的体外侵袭。与此相一致的是，在先兆子痫细胞滋养层中，化学检测的HIP表达大大降低，这是一种滋养层浸润异常浅的情况。有人建议，HIP加强人类细胞滋养层与HSPGs的相互作用，在体内，并促进滋养层侵入过程。
The human hemochorial placenta is a structure formed by the invasion of cytotrophoblasts into the uterus. Previous studies from our laboratory have demonstrated a role for heparan sulfate proteoglycans (HSPGs) and their binding proteins in interactions between human trophoblastic and uterine cell lines in vitro. In this study, expression of both mRNA and protein of a novel, cell surface, heparin/heparan sulfate interacting protein (HIP), by human trophoblastic cell lines—i.e., JAR, JEG, and BeWo—and by human cytotrophoblast was examined throughout gestation. Immunohistochemistry of the human fetal-maternal interface demonstrated abundant HIP expression in cytotrophoblast cells, with lesser staining in syncytiotrophoblast and little or no staining in surrounding stromal or decidual cells. Staining with antibodies to the basement membrane HSPG, perlecan, demonstrated a pattern of staining complementary to that of HIP. Cytotrophoblasts in the uterine stroma, not affiliated with attached villi, displayed a less intense deposition of perlecan. In vitro binding studies of125I-perlecan to a 17-amino acid synthetic peptide sequence of HIP, which has a high affinity and specificity for heparin/heparan sulfate, indicates that perlecan binds to the HIP peptide with high affinity (KDapp= 0.6 nM) and in a heparin-inhibitable manner. Furthermore, HIP antibodies inhibited by 61-88% in vitro invasion by trophoblasts in assays using primary cultures of normal human cytotrophoblasts. Consistent with this was the observation that immunohistochemically detectable HIP expression was greatly reduced in pre-eclamptic cytotrophoblasts, a condition in which trophoblast invasion is abnormally shallow. It is suggested that HIP potentiates human cytotrophoblast interactions with HSPGs, in vivo, and facilitates trophoblast invasion processes.