Cranial and trunk neural crest cells use different mechanisms for attachment to extracellular matrices.
Cranial and trunk neural crest cells use different mechanisms for attachment to extracellular matrices.
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发表时间：
1992-11
期刊：
影响因子：
4.6
通讯作者：
T. Lallier;G. Leblanc;K. Artinger;M. Bronner‐Fraser
中科院分区：
文献类型：
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作者：
T. Lallier;G. Leblanc;K. Artinger;M. Bronner‐Fraser
我们已经使用了定量细胞附着试验比较颅和躯干神经嵴细胞与细胞外基质（ECM）分子纤连蛋白，层粘连蛋白和胶原蛋白I型和IV型的相互作用。在所有测试条件下，整联蛋白β 1亚基的抗体抑制附着，表明整联蛋白介导神经嵴细胞与这些ECM分子的相互作用。HNK-1抗体对表面碳水化合物表位在一定条件下抑制颅和躯干神经嵴细胞附着层粘连蛋白，但不纤连蛋白。α 1整合素的抗血清抑制附着的躯干，但不颅，神经嵴细胞层粘连蛋白和胶原蛋白I型，虽然与纤连蛋白或胶原蛋白IV型的相互作用不受影响。躯干和颅神经嵴细胞的表面性质在几个方面不同。首先，躯干神经嵴细胞附着于I型和IV型胶原，但颅神经嵴细胞没有。其次，它们与ECM分子连接的二价阳离子要求不同。对于纤连蛋白基质，躯干神经嵴细胞需要二价阳离子的附件，而颅神经嵴细胞结合在没有二价阳离子。然而，颅神经嵴细胞失去了这种阳离子独立的附着后，几天的文化。对于层粘连蛋白基质，干细胞使用两种整联蛋白，一种是二价阳离子依赖性的，另一种是二价阳离子非依赖性的（Lallier，T. E.和Bronner-Fraser，M.（1991）Development 113，1069-1081）。与此相反，颅神经嵴细胞附着层粘连蛋白使用一个单一的，二价阳离子依赖性受体系统。用HNK-1、α 1整联蛋白和β 1整联蛋白抗体对表面标记的神经嵴细胞进行免疫沉淀和免疫印迹表明，颅神经嵴细胞和躯干神经嵴细胞具有生物化学上不同的整联蛋白。我们的研究结果表明，颅和躯干细胞的粘附机制不同，选定的ECM组件，这表明他们是非重叠的细胞群体就其粘附性能。
We have used a quantitative cell attachment assay to compare the interactions of cranial and trunk neural crest cells with the extracellular matrix (ECM) molecules fibronectin, laminin and collagen types I and IV. Antibodies to the beta 1 subunit of integrin inhibited attachment under all conditions tested, suggesting that integrins mediate neural crest cell interactions with these ECM molecules. The HNK-1 antibody against a surface carbohydrate epitope under certain conditions inhibited both cranial and trunk neural crest cell attachment to laminin, but not to fibronectin. An antiserum to alpha 1 intergrin inhibited attachment of trunk, but not cranial, neural crest cells to laminin and collagen type I, though interactions with fibronectin or collagen type IV were unaffected. The surface properties of trunk and cranial neural crest cells differed in several ways. First, trunk neural crest cells attached to collagen types I and IV, but cranial neural crest cells did not. Second, their divalent cation requirements for attachment to ECM molecules differed. For fibronectin substrata, trunk neural crest cells required divalent cations for attachment, whereas cranial neural crest cells bound in the absence of divalent cations. However, cranial neural crest cells lost this cation-independent attachment after a few days of culture. For laminin substrata, trunk cells used two integrins, one divalent cation-dependent and the other divalent cation-independent (Lallier, T. E. and Bronner-Fraser, M. (1991) Development 113, 1069-1081). In contrast, cranial neural crest cells attached to laminin using a single, divalent cation-dependent receptor system. Immunoprecipitations and immunoblots of surface labelled neural crest cells with HNK-1, alpha 1 integrin and beta 1 integrin antibodies suggest that cranial and trunk neural crest cells possess biochemically distinct integrins. Our results demonstrate that cranial and trunk cells differ in their mechanisms of adhesion to selected ECM components, suggesting that they are non-overlapping populations of cells with regard to their adhesive properties.