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Syndecan‐ and integrin‐binding peptides synergistically accelerate cell adhesion
Author(s) -
Hozumi Kentaro,
Kobayashi Kazuki,
Katagiri Fumihiko,
Kikkawa Yamato,
Kadoya Yuichi,
Nomizu Motoyoshi
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.06.032
Subject(s) - integrin , syndecan 1 , cell adhesion , laminin , extracellular matrix , adhesion , microbiology and biotechnology , chemistry , cell , cell adhesion molecule , biochemistry , biology , organic chemistry
Integrins and syndecans mediate cell adhesion to extracellular matrix and their synergistic cooperation is implicated in cell adhesion processes. We previously identified two active peptides, AG73 and EF1, from the laminin α1 chain LG4 module, that promote cell attachment through syndecan‐ and α2β1 integrin‐binding, respectively. Here, we examined time‐dependent cell attachment on the mixed peptides AG73/EF1. The AG73/EF1 promoted stronger and more rapid cell attachment, spreading, FAK phosphorylation that reached a maximum at 20 min than that on AG73 (40 min) or EF1 (90 min) supplied singly. Thus, the syndecan‐ and α2β1 integrin‐binding peptides synergistically affect cells and accelerate cell adhesion.