Screening of integrin-binding peptides from the laminin 伪4 and 伪5 chain G domain peptide library
- 作者：Fumihiko Katagiri ; Masaya Ishikawa ; Yuji Yamada ; Kentaro Hozumi ; Yamato Kikkawa ; Motoyoshi Nomizu ; nomizu@toyaku.ac.jp
- 关键词：Basement membrane ; Laminin ; Synthetic peptide ; Cell attachment ; Integrin
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2012
- 期刊代码：116_00039861
- 类别：ch
- 出版时间：May, 2012
- 卷：521
- 期：1-2
- 页码：32-42
- 文件大小：1581 K
摘要
Laminins, a multifunctional protein family of extracellular matrix, interact with various types of integrin. Here, integrin-mediated cell adhesive peptides have been systematically screened in the laminin 伪4 and 伪5 chain G domain peptide library consisting of 211 peptides by both the peptide-coated plastic plates and peptide-conjugated Sepharose bead assays using human dermal fibroblasts. Thirteen peptides promoted cell spreading and the activity was specifically inhibited by EDTA. Cell attachment to 11 peptides was inhibited by anti-integrin 尾1 antibody. Additionally, cell attachment to the A5G81 (AGQWHRVSVRWG) and A5G84 (TWSQKALHHRVP) peptides was specifically inhibited by anti-integrin 伪3 and 伪6 antibodies. These results suggest that the A5G81 and A5G84 peptides promote integrin 伪3尾1- and 伪6尾1-mediated cell attachment. Further, most of the integrin-mediated cell adhesive peptides are located in the loop regions in the G domains, suggesting that structure is important for the integrin specific recognition. Integrin binding peptides are useful for understanding laminin functions and have a potential to use for biomaterials and drug development.