Using self-assembled monolayers to understand α8β1-mediated cell adhesion to RGD and FEI motifs in nephronectin.

Using self-assembled monolayers to understand α8β1-mediated cell adhesion to RGD and FEI motifs in nephronectin.
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使用自组装的单层来理解肾上腺素素中对RGD和FEI基序的α8β1介导的细胞粘附。

DOI:
10.1021/cb200186j
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发表时间:
2011-10-21
影响因子:
4
通讯作者:
Mrksich, Milan
Mrksich, Milan
中科院分区:
生物学2区
文献类型:
--
作者:
Sanchez-Cortes, Juan;Mrksich, Milan

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肾粘连蛋白是一种细胞外基质蛋白,与α8β1整联蛋白受体相互作用,并在组织和器官发育中发挥作用,尽管介导与受体粘附的基序仍不清楚。本文描述了使用自组装单分子膜研究α8β1呈递细胞与肾连蛋白中的RGD和DLFEIFEIER配体的粘附,发现这两种配体可以通过整合素上的非重叠结合位点独立地介导细胞粘附。肽截短实验表明FEI是DLFEIFEIER序列内的最小结合序列,并且用包括RGD和FEI序列的肽进行的粘附实验证明这两种肽协同结合受体。最后,肽阵列被用来建立一个严格的要求,谷氨酸残基的FEI和其他芳香族和疏水性残基的第一和第三位的耐受性,分别。这项工作加深了对肾连蛋白与α8β1结合的了解,并鉴定了可用于靶向α8β1整联蛋白的肽配体。
Nephronectin is an extracellular matrix protein that interacts with the α8β1 integrin receptor and plays a role in tissue and organ development, though the motifs that mediate adhesion to the receptor remain unclear. This paper describes the use of self-assembled monolayers to study the adhesion of α8β1-presenting cells to the RGD and DLFEIFEIER ligands in nephronectin and found that both ligands can independently mediate cell adhesion through nonoverlapping binding sites on the integrin. Peptide truncation experiments showed FEI to be the minimal binding sequence within the DLFEIFEIER sequence, and adhesion experiments with peptides that include both the RGD and FEI sequences demonstrate that the two peptides bind synergistically to the receptor. Finally, a peptide array was used to establish a strict requirement for the glutamate residue of FEI and tolerance of other aromatic and hydrophobic residues in the first and third positions, respectively. This work provides an enhanced understanding of the binding of nephronectin with α8β1 and identifies a peptide ligand that can be used for targeting the α8β1 integrin.
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