論文

査読有り 国際誌
2019年9月10日

Characterization of dystroglycan binding in adhesion of human induced pluripotent stem cells to laminin-511 E8 fragment.

Scientific reports
  • Yumika Sugawara
  • ,
  • Keisuke Hamada
  • ,
  • Yuji Yamada
  • ,
  • Jun Kumai
  • ,
  • Motoi Kanagawa
  • ,
  • Kazuhiro Kobayashi
  • ,
  • Tatsushi Toda
  • ,
  • Yoichi Negishi
  • ,
  • Fumihiko Katagiri
  • ,
  • Kentaro Hozumi
  • ,
  • Motoyoshi Nomizu
  • ,
  • Yamato Kikkawa

9
1
開始ページ
13037
終了ページ
13037
記述言語
英語
掲載種別
DOI
10.1038/s41598-019-49669-x

Human induced pluripotent stem cells (hiPSCs) grow indefinitely in culture and have the potential to regenerate various tissues. In the development of cell culture systems, a fragment of laminin-511 (LM511-E8) was found to improve the proliferation of stem cells. The adhesion of undifferentiated cells to LM511-E8 is mainly mediated through integrin α6β1. However, the involvement of non-integrin receptors remains unknown in stem cell culture using LM511-E8. Here, we show that dystroglycan (DG) is strongly expressed in hiPSCs. The fully glycosylated DG is functionally active for laminin binding, and although it has been suggested that LM511-E8 lacks DG binding sites, the fragment does weakly bind to DG. We further identified the DG binding sequence in LM511-E8, using synthetic peptides, of which, hE8A5-20 (human laminin α5 2688-2699: KTLPQLLAKLSI) derived from the laminin coiled-coil domain, exhibited DG binding affinity and cell adhesion activity. Deletion and mutation studies show that LLAKLSI is the active core sequence of hE8A5-20, and that, K2696 is a critical amino acid for DG binding. We further demonstrated that hiPSCs adhere to hE8A5-20-conjugated chitosan matrices. The amino acid sequence of DG binding peptides would be useful to design substrata for culture system of undifferentiated and differentiated stem cells.

リンク情報
DOI
https://doi.org/10.1038/s41598-019-49669-x
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/31506597
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6737067

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