Substrate adhesion of rat hepatocytes: Mechanism of attachment to collagen substrates
Substrate adhesion of rat hepatocytes: Mechanism of attachment to collagen substrates
复制标题
大鼠肝细胞的基质粘附：胶原蛋白基质的附着机制
DOI：
10.1016/0092-8674(81)90337-8
复制
发表时间：
1981
期刊：
影响因子：
64.5
通讯作者：
R. Timpl
中科院分区：
文献类型：
--
作者：
K. Rubin;M. Höök;B. Öbrink;R. Timpl
大鼠肝细胞与胶原蛋白的附着无需纤连蛋白的帮助，被发现是一种时间依赖性反应，其特征是在稳定附着键开始形成之前有 10-20 分钟的初始滞后期。增加胶原蛋白基质中的分子密度可提高细胞附着率。肝细胞与所有测试的胶原蛋白类型（I、II、III、IV 和 V 型）的附着力基本相同。细胞对天然胶原蛋白的初始附着速度比对变性胶原蛋白或 α1(I) 链的附着速度更快，这显然表明细胞对这些底物的亲和力不同。然而，如果细胞孵育 60 分钟或更长时间，α1(I) 链和所有测试的溴化氰处理肽（α1-CB2、α1-CB3、α1-CB4、α1-CB5、α1-CB6A、α1-CB7、α1-CB8、α2-CB2、α2-CB3 和 α2-CB4）会发生有效附着，但不会发生有效附着。 I型前胶原的氨基前肽。由具有胶原蛋白样结构 (Gly-Ala-Pro)n、(Gly-Pro-Pro)n 和 (Gly-Pro-Hyp)n 的合成肽制成的基质也发生了低但显着程度的附着，而没有观察到与聚脯氨酸的附着。我们认为胶原蛋白中的细胞结合位点具有简单的结构，并且沿着胶原蛋白分子以多个拷贝出现。在溶液中添加胶原蛋白会抑制初始细胞附着，这种效应在由 α1(I) 链制成的基质上比在变性胶原蛋白上持续的时间更长。收集的数据根据细胞与胶原蛋白粘附模型进行解释，其中稳定附着键的形成需要聚集在粘附位点的几个低亲和力受体与基质中的胶原蛋白分子结合。
Attachment of rat hepatocytes to collagen, which occurs without the aid of fibronectin, was found to be a time-dependent reaction characterized by an initial lag phase of 10–20 min before stable attachment bonds began to form. Increasing the density of molecules in the collagen substrates enhanced the rate of cell attachment. The hepatocytes attached essentially equally well to all the collagen types tested (types I, II, III, IV and V). The initial rate of cell attachment was more rapid to native collagen than to denatured collagen or α1(I) chains, apparently indicating different affinities of the cells for these substrates. However, if cells were incubated for 60 min or more, efficient attachment occurred to the α1(I) chain and to all cyanogen-bromide-treated peptides tested (α1-CB2, α1-CB3, α1-CB4, α1-CB5, α1-CB6A, α1-CB7, α1-CB8, α2-CB2, α2-CB3 and α2-CB4) but not to the aminopropeptide of type I procollagen. A low but significant degree of attachment also took place to substrates made of synthetic peptides with the collagen-like structures (Gly-Ala-Pro)n, (Gly-Pro-Pro)nand (Gly-Pro-Hyp)n, whereas no attachment was observed to polyproline. We suggest that the cell-binding sites in collagen have a simple structure and occur in multiple copies along the collagen molecule. Addition of collagen in solution inhibited intial cell attachment, an effect that persisted longer on substrates made of α1(I) chain than on denatured collagen. The collected data are interpreted in terms of a model for cell-to-collagen adhesion where the formation of stable attachment bonds requires the binding of several low-affinity receptors, clustered at the site of adhesion, to collagen molecules in the substrate.