Postsurgical wound progression monitored by temporal changes in the expression of matrix metalloproteinase-9

Abstract

It is important to monitor the early stages of postoperative wound repair in order to identify those problems associated with impaired healing. Many of the crucial cellular responses of early wound healing, such as inflammatory infiltration, angiogenesis and re-epithelialization, are made possible through the action of matrix metalloproteinases (MMPs). Expression of MMP-2 and MMP-9 is elevated in acute wounds, and still greater levels are found in chronic wounds, indicating that uncontrolled proteolysis is a characteristic of retarded healing. Therefore, comparative measurements of MMPs may be used to monitor the progression of early wound healing. To investigate this, wound fluids and sera were collected from mastectomy and colectomy patients throughout early stages of repair, and the temporal expression profile established. Wounds which were healing were expressed maximal levels of MMP-9 at 24 h, followed by a significant decline by 48 h. Persistent elevation of MMP-9 expression was associated with infected and chronic wounds, and was identified in postoperative wounds by the absence of the significant decline between 24 and 48 h. Measurement of MMP-9 in postoperative wound fluids, therefore, provides an early indicator of impaired healing, which may be evaluated non-invasively within 48 h of closure.

Coping style and depression influence the healing of diabetic foot ulcers: observational and mechanistic evidence

“…Levels of MMPs were normalised to the mass of fluid collected. The presence of MMP2 and -9 was detected in wound fluid samples using gelatine substrate SDS-polyacrylamide gel electrophoresis (zymography) as described previously [26][27][28].…”

The Role of Up-Regulated Serine Proteases and Matrix Metalloproteinases in the Pathogenesis of a Murine Model of Colitis

“…22 In brief, gelatin was co-polymerized in 10% polyacrylamide gels, and run in a BioRad Mini Protean II apparatus (Bio-Rad, Hemel Hempstead, Herts, UK), with samples, prestained molecular weight markers (sodium dodecyl sulfate-7B), and MMP-2 standard (Biogenesis, Bournmouth, Dorset, UK). MMP proteolysis buffer was prepared from 50 mmol/L Tris/HCl, pH7.8, 50 mmol/L CaCl 2 , 0.5 mol/L NaCl, and 1 mmol/L amino phenyl mercuric acetate, with addition of a cocktail of serine proteinase inhibitors, comprising phenylmethyl sulfonyl fluoride (PMSF), leupeptin, and soybean trypsin inhibitor, at the concentrations detailed below.…”

“…The identity of MMP-2 and -9 was further corroborated by demonstrating gelatin affinity, as previously described. 22 …”

“…20,21 The potential for evaluating such changes in protease expression as a means of monitoring normal tissue repair processes 22,23 and evaluating healing in chronic ulcers 24 has been demonstrated.…”

Interleukin-1α–induced proteolytic activation of metalloproteinase-9 by human skin

“…However, pro-MMP-9 is expressed quickly after cutaneous trauma, and concentrations decline with the progression of healing. [13][14][15][16] In chronic wounds, pro-MMP-9 is overexpressed persistently, along with the converted zymogen, active MMP-9 (82-kDa). 17-20 MMP-9 is almost always associated with inflammatory conditions.…”