THE L2/HNK-1 CARBOHYDRATE MEDIATES ADHESION OF NEURAL CELLS TO LAMININ
THE L2/HNK-1 CARBOHYDRATE MEDIATES ADHESION OF NEURAL CELLS TO LAMININ
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DOI：
10.1111/j.1460-9568.1993.tb00202.x
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发表时间：
1993-01-01
影响因子：
3.4
通讯作者：
SCHMITZ, B
中科院分区：
文献类型：
--
作者：
HALL, H;LIU, L;SCHMITZ, B
多个神经粘附分子共享的L2/HNK-1碳水化合物表位与细胞间和细胞与层粘连蛋白的粘附有关（Keilhauer等，Nature 316, 728 - 730,1985； Kunemund等，J. Cell Biol.）。， 106, 213 - 223, 1988)。正如先前对鸡视网膜神经节细胞所证明的那样(Cole等人，神经科学。列托人。（93,170 - 175,1988），大脑皮质星形胶质细胞或小脑神经元不能粘附于底物结合的L2/HNK-1碳水化合物。然而，细胞结合的L2/HNK-1碳水化合物是星形细胞和神经元细胞粘附层粘连蛋白的有效介质，在携带L2/HNK-1碳水化合物的糖脂或针对它的单克隆抗体Fab片段存在时，层粘连蛋白被强烈降低。在带负电荷的神经节苷或硫化物的存在下，不能观察到粘附的抑制，但在肝素的存在下。为了研究L2/HNK-1碳水化合物和肝素是否在层粘连蛋白上使用相同或不同的结合位点，在肝素和单克隆L2抗体Fab片段存在的情况下，测定了细胞对层粘连蛋白的粘附，与单一化合物引起的抑制相比，这提供了一个附加的抑制值。这一结果，以及在肝素存在下L2/HNK-1糖脂与层粘连蛋白结合的研究表明，L2/HNK-1碳水化合物和肝素在神经细胞粘附层粘连蛋白的不同方面都有牵连。
The L2/HNK-1 carbohydrate epitope shared by several neural adhesion molecules has been implicated in cell-to-cell and cell-to-laminin adhesion (Keilhauer et al., Nature 316, 728 - 730, 1985; Kunemund et al, J. Cell Biol., 106, 213 - 223, 1988). As demonstrated previously for chicken retinal ganglion cells (Cole et al., Neurosci. Lett., 93, 170 - 175, 1988), cerebral cortex astrocytes or cerebellar neurons could not be shown to adhere to the substrate-bound L2/HNK-1 carbohydrate. The cell-bound L2/HNK-1 carbohydrate, however, was a potent mediator of astrocytic and neuronal cell adhesion to laminin, which was strongly reduced in the presence of the L2/HNK-1 carbohydrate-carrying glycolipids or Fab fragments of a monoclonal antibody against it. Inhibition of adhesion could not be observed in the presence of the negatively charged gangliosides or sulphatide, but in the presence of heparin. To investigate whether the L2/HNK-1 carbohydrate and heparin use the same or different binding sites on laminin, adhesion of cells to laminin was determined in the presence of heparin and Fab fragments of a monoclonal L2 antibody, which gave an additive value of inhibition as compared to the inhibition caused by the single compounds. This result, as well as studies of the binding of the L2/HNK-1 glycolipids to laminin in the presence of heparin, indicates that the L2/HNK-1 carbohydrate and heparin are implicated in different aspects of neural cell adhesion to laminin.