Syndecan‐ and integrin‐binding peptides synergistically accelerate cell adhesion
Kentaro Hozumi, Kazuki Kobayashi, Fumihiko Katagiri, Yamato Kikkawa, Yuichi Kadoya, Motoyoshi Nomizu
Abstract
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Kentaro Hozumi, Kazuki Kobayashi, Fumihiko Katagiri, Yamato Kikkawa, Yuichi Kadoya, Motoyoshi Nomizu
Abstract
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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 alpha1 chain LG4 module, that promote cell attachment through syndecan- and alpha2beta1 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 alpha2beta1 integrin-binding peptides synergistically affect cells and accelerate cell adhesion.
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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 alpha1 chain LG4 module, that promote cell attachment through syndecan- and alpha2beta1 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 alpha2beta1 integrin-binding peptides synergistically affect cells and accelerate cell adhesion.
Key concepts: Integrin, Syndecan 1, Cell adhesion, Laminin, Extracellular matrix, Adhesion, Cell biology, Chemistry