Open AccessTopical application of recombinant platelet‐derived growth factor increases the rate of healing and the level of proteins that regulate this response
Author(s) -
Gowda Santosh,
Weinstein David A,
Blalock Timothy D,
Gandhi Kavita,
Mast Bruce A,
Chin Gloria,
Schultz Gregory S
Publication year - 2015
Publication title -
international wound journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.867
H-Index - 63
eISSN - 1742-481X
pISSN - 1742-4801
DOI - 10.1111/iwj.12165
Subject(s) - medicine , mmp9 , wound healing , ischemia , mmp2 , platelet derived growth factor , platelet derived growth factor receptor , matrix metalloproteinase , growth factor , tumor necrosis factor alpha , necrosis , recombinant dna , surgery , downregulation and upregulation , biochemistry , receptor , biology , cancer , gene , metastasis
Abstract A bipedicle ischaemic rat skin flap model was used to study the effects of daily topical applications of platelet‐derived growth factor ( PDGF ) on the healing of ischaemic wounds. Levels of tumour necrosis factor‐alpha ( TNFA ), interleukin 1‐beta ( IL1B ) and both the latent and active forms of matrix metalloproteinase 2 ( MMP2 ) and 9 ( MMP9 ) were measured. Full‐thickness wounds were made on a total of 72 adult male Sprague–Dawley rats. Each group of 18 rats with normal and ischaemic wounds received either vehicle or 0·01% recombinant PDGF‐BB . Additional applications were made on the wounds on a daily basis. Wound areas were measured at 0, 1, 3, 5, 7 9 and 13 days after wounding. Ischaemia caused a delay in wound healing as well as an increase in TNFA , IL1B and both the pro and active forms of MMP2 and MMP9 . PDGF accelerated the rate of wound healing in both normal and ischaemic wounds and negated the effect of ischaemia. PDGF reduced the TNFA concentration in both normal and ischaemic wounds, and the rate of wound healing closely resembled the pattern of TNFA protein expression. PDGF also reduced both the magnitude and duration of the increases in IL1B and both the pro and active forms of MMP2 and MMP9 induced by ischaemia.