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Platelet rich plasma promotes skeletal muscle cell migration in association with up‐regulation of FAK, paxillin, and F‐Actin formation
Author(s) -
Tsai WenChung,
Yu TungYang,
Lin LiPing,
Lin MioaSui,
Tsai TingTa,
Pang JongHwei S.
Publication year - 2017
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.23547
Subject(s) - paxillin , focal adhesion , microbiology and biotechnology , actin , cell migration , small interfering rna , actin cytoskeleton , western blot , skeletal muscle , chemistry , cell , transfection , gene knockdown , cytoskeleton , biology , signal transduction , anatomy , biochemistry , apoptosis , gene
Platelet rich plasma (PRP) contains various cytokines and growth factors which may be beneficial to the healing process of injured muscle. The aim of this study was to investigate the effect and molecular mechanism of PRP on migration of skeletal muscle cells. Skeletal muscle cells intrinsic to Sprague–Dawley rats were treated with PRP. The cell migration was evaluated by transwell filter migration assay and electric cell‐substrate impedance sensing. The spreading of cells was evaluated microscopically. The formation of filamentous actin (F‐actin) cytoskeleton was assessed by immunofluorescence staining. The protein expressions of paxillin and focal adhesion kinase (FAK) were assessed by Western blot analysis. Transfection of paxillin small‐interfering RNA (siRNAs) to muscle cells was performed to validate the role of paxillin in PRP‐mediated promotion of cell migration. Dose‐dependently PRP promotes migration of and spreading and muscle cells. Protein expressions of paxillin and FAK were up‐regulated dose‐dependently. F‐actin formation was also enhanced by PRP treatment. Furthermore, the knockdown of paxillin expression impaired the effect of PRP to promote cell migration. It was concluded that PRP promoting migration of muscle cells is associated with up‐regulation of proteins expression of paxillin and FAK as well as increasing F‐actin formation. © 2017 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 35:2506–2512, 2017.