論文

国際誌
2018年6月4日

Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing.

Nature communications
  • Jun Ishihara
  • ,
  • Ako Ishihara
  • ,
  • Kazuto Fukunaga
  • ,
  • Koichi Sasaki
  • ,
  • Michael J V White
  • ,
  • Priscilla S Briquez
  • ,
  • Jeffrey A Hubbell

9
1
開始ページ
2163
終了ページ
2163
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/s41467-018-04525-w

Laminin, as a key component of the basement membrane extracellular matrix (ECM), regulates tissue morphogenesis. Here, we show that multiple laminin isoforms promiscuously bind to growth factors (GFs) with high affinity, through their heparin-binding domains (HBDs) located in the α chain laminin-type G (LG) domains. These domains also bind to syndecan cell-surface receptors, promoting attachment of fibroblasts and endothelial cells. We explore the application of these multifunctional laminin HBDs in wound healing in the type-2 diabetic mouse. We demonstrate that covalent incorporation of laminin HBDs into fibrin matrices improves retention of GFs and significantly enhances the efficacy of vascular endothelial cell growth factor (VEGF-A165) and platelet-derived growth factor (PDGF-BB) in promoting wound healing in vivo, under conditions where the GFs alone in fibrin are inefficacious. This laminin HBD peptide may be clinically useful by improving biomaterial matrices as both GF reservoirs and cell scaffolds, leading to effective tissue regeneration.

リンク情報
DOI
https://doi.org/10.1038/s41467-018-04525-w
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/29867149
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986797
ID情報
  • DOI : 10.1038/s41467-018-04525-w
  • PubMed ID : 29867149
  • PubMed Central 記事ID : PMC5986797

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