Syndecan- and integrin-binding peptides synergistically accelerate cell adhesion |
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Authors: | Kentaro Hozumi Fumihiko Katagiri Yuichi Kadoya |
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Affiliation: | a Laboratory of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan b Department of Anatomy, Kitasato University School of Allied Health Sciences, Sagamihara, Kanagawa 228-8555, Japan |
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Abstract: | 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. |
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Keywords: | Basement membrane Cell adhesion Extracellular matrix Integrin Laminin Syndecan |
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