A neuroectoderm-associated ganglioside participates in fibronectin receptor-mediated adhesion of germinal cells to fibronectin.
A neuroectoderm-associated ganglioside participates in fibronectin receptor-mediated adhesion of germinal cells to fibronectin.
复制标题
神经外胚层相关神经节苷脂参与纤连蛋白受体介导的生发细胞与纤连蛋白的粘附。
DOI：
10.1016/0012-1606(89)90218-2
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发表时间：
1989
影响因子：
2.7
通讯作者：
Ruoslahti,E
中科院分区：
文献类型：
--
作者：
Stallcup,WB;Pytela,R;Ruoslahti,E
以前的研究表明，与大鼠神经细胞系的D1.1神经节苷脂，O-乙酰化衍生物的GD 3，是参与细胞粘附到fibronectin.In体内，D1.1是存在于发育中的大鼠中枢神经系统的生发细胞，但不是有丝分裂后的细胞迁移远离生发区。这些观察结果表明，D1.1可以参与在生发带内的粘附相互作用，并且D1.1的丢失可能涉及开始迁移的决定。在支持这一假设，免疫荧光组织化学显示，纤连蛋白和纤连蛋白受体与D1.1共定位在脑室区的胚胎大鼠大脑和出生后小脑的外部颗粒细胞层。用抗D1.1单克隆抗体包被的培养皿从胚胎第14天的大脑和出生后第6天的小脑中分离出D1.1阳性的生发细胞。这些细胞能够通过一种机制粘附到纤连蛋白包被的培养皿上，该机制可被含有纤连蛋白的arg-gly-asp细胞识别序列的合成六肽所识别。粘附也部分地被抗纤连蛋白受体的抗体抑制，并且被抗D1.1抗体减慢，这暗示受体和神经节苷脂都参与粘附过程。在3天的培养过程中，这些D1.1阳性，纤连蛋白受体阳性细胞表现出神经元表型，通过形态学和破伤风毒素染色判断。这进一步证实了细胞的神经上皮起源。这些细胞不能合成可检测量的纤连蛋白，因此在组织切片的生发带中观察到的纤连蛋白的来源不明。免疫沉淀实验表明，这些细胞上存在的纤连蛋白受体是异源二聚体。在非还原条件下，免疫沉淀物含有150-160 kDa的α亚基和115-125 kDa的β亚基。
Previous studies with a rat neural cell line have shown that the D1.1 ganglioside, an O-acetylated derivative of GD3, is involved in cellular adhesion to fibronectin.In vivo, D1.1 is present on germinal cells of the developing rat central nervous system, but not on postmitotic cells that migrate away from the germinal zones. These observations suggest that D1.1 could participate in adhesive interactions within germinal zones and that the loss of D1.1 could be involved in the decision to begin migration. In support of this hypothesis, immunofluorescence histochemistry shows that both fibronectin and fibronectin receptor are colocalized with D1.1 in the ventricular zones of the embryonic rat brain and in the external granule cell layer of the postnatal cerebellum. Dishes coated with monoclonal antibody against D1.1 were used to isolate D1.1-positive germinal cells from Embryonic Day 14 cerebrum and from Postnatal Day 6 cerebellum. These cells are able to adhere to fibronectin-coated dishes by a mechanism that is inhibitable by a synthetic hexapeptide containing the arg-gly-asp cell recognition sequence of fibronectin. Adhesion is also partially inhibited by antibody against fibronectin receptor and is slowed by anti-D1.1 antibody, implicating both the receptor and the ganglioside in the adhesion process. During 3 days in culture these D1.1-positive, fibronectin receptor-positive cells exhibit a neuronal phenotype, as judged by morphology and staining with tetanus toxin. This further confirms the neuroepithelial origin of the cells. The cells do not synthesize detectable amounts of fibronectin, thus leaving unidentified the source of the fibronectin seen in the germinal zones in tissue sections. Immunoprecipitation experiments show that the fibronectin receptors present on these cells are heterodimers. Under nonreducing conditions, the immunoprecipitates contain an α-subunit of 150–160 kDa and a β-subunit of 115–125 kDa.