Molecular mechanisms of neural crest cell attachment and migration on types I and IV collagen.
Molecular mechanisms of neural crest cell attachment and migration on types I and IV collagen.
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发表时间：
1993-12
影响因子：
4
通讯作者：
R. Perris;J. Syfrig;M. Paulsson;M. Bronner‐Fraser
中科院分区：
文献类型：
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作者：
R. Perris;J. Syfrig;M. Paulsson;M. Bronner‐Fraser
我们已经研究了禽神经嵴细胞与I型和IV型胶原（Col I和IV）在体外粘附和迁移过程中相互作用的机制。为此目的，从鸡组织中纯化天然Col IV，其特征在于生化和超微结构。纯化的鸡Col I和Col IV，以及胶原蛋白的各种蛋白水解片段，与结构域特异性胶原蛋白抗体和禽类整联蛋白亚基抗体一起用于定量细胞附着和迁移测定。神经嵴细胞在其初始附着期间不区分Col I的不同大分子排列，但在其迁移期间这样做，显示出对聚合Col I的明显偏好。与Col I的相互作用由α 1 β 1整联蛋白介导，通过与由片段CNBr 3组成的α 1（I）链的片段结合。神经嵴细胞的附着和迁移涉及识别三螺旋区域和非胶原的羧基末端NC 1结构域内的构象依赖性位点。这种识别需要链间和链内二硫键的完整性以及分子的正确折叠。此外，也有证据表明，NC 1结构域内的相互作用位点可能是隐蔽的，由于细胞-基质接触延长，在完整胶原中的细胞迁移期间暴露。与Col I相反，神经嵴细胞与Col IV的相互作用由除α 1 β 1以外的β 1类整联蛋白介导。
We have examined the mechanisms involved in the interaction of avian neural crest cells with collagen types I and IV (Col I and IV) during their adhesion and migration in vitro. For this purpose native Col IV was purified from chicken tissues, characterized biochemically and ultrastructurally. Purified chicken Col I and Col IV, and various proteolytic fragments of the collagens, were used in quantitative cell attachment and migration assays in conjunction with domain-specific collagen antibodies and antibodies to avian integrin subunits. Neural crest cells do not distinguish between different macromolecular arrangements of Col I during their initial attachment, but do so during their migration, showing a clear preference for polymeric Col I. Interaction with Col I is mediated by the alpha 1 beta 1 integrin, through binding to a segment of the alpha 1(I) chain composed of fragment CNBr3. Neural crest cell attachment and migration on Col IV involves recognition of conformation-dependent sites within the triple-helical region and the noncollagenous, carboxyl-terminal NC1 domain. This recognition requires integrity of inter- and intrachain disulfide linkages and correct folding of the molecule. Moreover, there also is evidence that interaction sites within the NC1 domain may be cryptic, being exposed during migration of the cells in the intact collagen as a result of the prolonged cell-substratum contact. In contrast to Col I, neural crest cell interaction with Col IV is mediated by beta 1-class integrins other than alpha 1 beta 1.