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The laminin‐211‐derived PPFEGCIWN motif accelerates wound reepithelialization and increases phospho‐FAK‐Tyr397 and Rac1‐GTP levels in a rat excisional wound splinting model
Author(s) -
Jo Seung Bin,
Park Cho Yeon,
Kang Hyun Ki,
Jung Sung Youn,
Min ByungMoo
Publication year - 2020
Publication title -
journal of tissue engineering and regenerative medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.835
H-Index - 72
eISSN - 1932-7005
pISSN - 1932-6254
DOI - 10.1002/term.3084
Subject(s) - wound healing , in vivo , microbiology and biotechnology , rac1 , chemistry , cell migration , in vitro , peptide , phosphorylation , wound closure , anatomy , biology , signal transduction , immunology , biochemistry
We previously reported that the PPFEGCIWN motif (Ln2‐LG3‐P2‐DN3), residues 2678–2686 of the human laminin α2 chain, promotes cell attachment of normal human epidermal keratinocytes (NHEKs) and dermal fibroblasts (NHDFs); however, its in vivo effects on cutaneous wound healing have not yet been examined. In this study, we sought to determine whether Ln2‐LG3‐P2‐DN3 could promote full‐thickness cutaneous wound healing by accelerating wound reepithelialization and wound closure in vivo. Ln2‐LG3‐P2‐DN3 had significantly higher cell attachment and spreading activities than vehicle or scrambled peptide control in both NHEKs and NHDFs in vitro. The wound area was significantly smaller in rats treated with Ln2‐LG3‐P2‐DN3 than in those treated with vehicle or scrambled peptide in the early phase of wound healing. Furthermore, Ln2‐LG3‐P2‐DN3 significantly accelerated wound reepithelialization relative to vehicle or scrambled peptide and promoted FAK‐Tyr397 phosphorylation and Rac1 activation. Collectively, our findings suggest that the PPFEGCIWN motif has potential as a therapeutic agent for cutaneous regeneration via the acceleration of wound reepithelization and wound closure.