SURFACE-GRAFTED CELL-BINDING PEPTIDES IN TISSUE ENGINEERING OF THE VASCULAR GRAFT
SURFACE-GRAFTED CELL-BINDING PEPTIDES IN TISSUE ENGINEERING OF THE VASCULAR GRAFT
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DOI：
10.1111/j.1749-6632.1992.tb42589.x
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发表时间：
1992-10-13
期刊：
影响因子：
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通讯作者：
DRUMHELLER, PD
中科院分区：
文献类型：
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作者：
HUBBELL, JA;MASSIA, SP;DRUMHELLER, PD
细胞与天然和合成底物的粘附通过细胞粘附蛋白与相应的细胞表面受体的相互作用介导。存在于体内细胞外基质中的细胞粘附蛋白包括纤连蛋白、玻连蛋白、胶原蛋白、血小板反应蛋白、血管性血友病因子和层粘连蛋白。这些蛋白质存在许多细胞表面受体，并且对特定粘附蛋白的特异性取决于特定受体，其中一些非常特异，而另一些则不那么特异。整合素家族是一组非常重要且具有良好特征的受体，其参与细胞-细胞和细胞-底物粘附。整合素是α亚基和β亚基的异二聚体，目前已知有12个α亚基和7个β亚基。已经观察到几种ap组合。一般而言，P1和β 3整联蛋白参与细胞与细胞外基质的粘附，而β 2整联蛋白参与细胞-细胞粘附。在整联蛋白家族中存在大量受体/配体重叠。例如，尽管经典的纤连蛋白受体是asp 1，纤连蛋白也结合到α 1 β、α 2 β 1、α 3 β、α 4 β 1、α 4 β 3和α 4 β。受体avp 3是经典的玻连蛋白受体，但它也结合纤维蛋白原、纤连蛋白、层粘连蛋白、血小板反应蛋白和血管性血友病因子。受体和配体重叠的原因之一是这些细胞粘附蛋白中的受体结合结构域是相当高度保守的，是在纤连蛋白、纤维蛋白原和von Willebrand因子中发现的Arg-Gly-Asp-Ser（RGDS）序列的变体。玻连蛋白含有RGDV;胶原蛋白I，RGDT;胶原蛋白VI，RGDX，其中X是变体;血小板反应蛋白，RGDA和层粘连蛋白，RGDN。纤连蛋白含有额外的RGDS样序列，即REDV（即所谓的3型连接片段的CSS肽，仅存在于某些纤连蛋白中）和LDV（即所谓的3型连接片段的CS 1肽）。~片段。含有RGDS和先前描述的变体序列的合成肽将以几乎整个蛋白质的亲和力结合它们各自的整联蛋白。在细胞粘附蛋白中有几个受体结合结构域不是来自RGDS序列。其中研究得最好的可能是
Cell adhesion to both natural and synthetic substrates is mediated by the interaction of cell adhesion proteins with corresponding cell-surface receptors. The cell adhesion proteins present in the extracellular matrix in vivo include fibronectin, vitronectin, collagen, thrombospondin, von Willebrand factor, and laminin. A host of cell-surface receptors are present for these proteins and the specificity for particular adhesion proteins depends upon the particular receptor, with some being very specific and others being less so.The integrin family is a very important and well-characterized group of receptors that is involved in both cell-cell and cell-substrate adhe~ ion. l-~ The integrins are heterodimers of an a subunit and a p subunit, and there are currently known to be 12 a subunits and 7 p subunits. Several ap combinations have been observed. In general, the PI and p3 integrins are involved in cell adhesion to the extracellular matrix, whereas the p2 integrins are involved in cell-cell adhesion. There is a great deal of receptor/ligand overlap in the integrin family. For example, whereas the classical fibronectin receptor is aspI, fibronectin also binds to a&, a $ l, ad&, avpl, avp3, and a&. The receptor avp3 is the classical vitronectin receptor, but it also binds fibrinogen, fibronectin, laminin, thrombospondin, and von Willebrand factor. One of the reasons for the overlap between receptors and ligands is that the receptor-binding domain among these cell adhesion proteins is rather highly conserved, being variants of the Arg-Gly-Asp-Ser (RGDS) sequence that is found in fibronectin, fibrinogen, and von Willebrand fa~ tor.~ Vitronectin contains RGDV; collagen I, RGDT; collagen VI, RGDX, where X is variant; thrombospondin, RGDA and laminin, RGDN. Fibronectin contains additional RGDS-like sequences, namely, REDV, which is the so-called CSS peptide of the type-3 connecting segment and is present only in some fibronectins, and LDV, which is the so-called CS1 peptide of the type-3 connecting~ egment.~ Synthetic peptides containing the RGDS and variant sequences previously described will bind to their respective integrin with nearly the affinity of the whole protein. There are several receptor-binding domains in cell adhesion proteins that are not derived from the RGDS sequence. Probably the best studied of these is the