The cell adhesion and proliferation activities of a peptide derived from human tenascin-C are dependent on two Ile residues.
The cell adhesion and proliferation activities of a peptide derived from human tenascin-C are dependent on two Ile residues.
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源自人生腱蛋白-C 的肽的细胞粘附和增殖活性取决于两个 Ile 残基。
DOI：
10.1016/j.bmc.2012.06.036
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发表时间：
2012
影响因子：
3.5
通讯作者：
H. Kodama
中科院分区：
文献类型：
--
作者：
R. Hayashi;Shogo Miura;Yohei Saito;Satoshi Osada;T. Iyoda;F. Fukai;H. Kodama
Tenascin-C衍生的多肽(TnIIIA2多肽，1)通过与Syndecan-4结合，刺激β-1整合素介导的细胞黏附。为了了解其构效关系，我们合成了丙氨酸取代的多肽。碱性氨基酸取代的多肽具有较低的细胞黏附活性，但其增殖活性与多肽1相似或高于多肽1。相反，取代多肽1的Ile残基的多肽没有活性，表明Ile残基是多肽活性的关键。CD分析表明，ILE残基是形成与Syndecan-4结合所需的特定构象所必需的。
A tenascin-C derived peptide (TNIIIA2 peptide, 1) stimulated β1 integrin-mediated cell adhesion via binding to syndecan-4. Ala-substituted peptides were synthesized to understand the structure–activity relationship. Peptides in which basic amino acids were substituted showed reduced cell adhesion activity, but their proliferation activities were similar to or higher than those mediated by peptide 1. In contrast, peptides in which the Ile residues of peptide 1 were replaced were inactive, indicating that the Ile residues are critical for the peptide’s activity. CD analysis suggested that the Ile residues are necessary for the formation of a specific conformation required for binding to syndecan-4.
影响因子：
19
作者：
Woods, A;Couchman, JR
通讯作者：
Couchman, JR
影响因子：
7.5
作者：
Rapraeger, AC;Ott, VL
通讯作者：
Ott, VL