Testing the influence of surfactant‐based wound dressings on proteinase activity. Issue 5 (8th December 2016)

• Record Type: Journal Article
• Authors: Jeong, Sunyoung; Schultz, Gregory S; Gibson, Daniel J
• Is Part Of: International wound journal. Volume 14:Issue 5(2017)
• Page Start: 786
• Page End: 790
• Publication Date: 2016-12-08
• Subjects: Autolytic debridement -- MMPs -- Proteinases -- Surfactant gel dressing; Wounds and injuries -- Treatment -- Periodicals; Wounds and injuries -- Periodicals; Wound healing -- Periodicals; 617.1005
• DOI: 10.1111/iwj.12697
• Languages: English
• ISSNs: 1742-4801

Abstract

ABSTRACT: Proteinases are enzymes that can digest other proteins. In chronic wounds, a sub‐class of these enzymes with the ability to degrade the extracellular matrix (matrix metalloproteinases, MMPs) have been found to both inhibit healing and to be able to aid in enzymatically debriding a wound. Enzymatic debridement using the enzymes present in a wound is generally called autolytic debridement. Clinicians seeking to employ autolytic debridement typically use occlusive materials such as medical honey, alginate dressings and other occlusive dressings. A relatively new class of gel dressings comprised of surfactants are now available for clinical use. A variety of surfactants are used in the study of MMP biochemistry. Surfactants can deactivate MMPs or can enhance their activity, depending on the surfactant. In order to begin to understand how the MMPs found in chronic wounds would respond to these new dressings, we tested a serial dilution series of two of the currently available surfactant‐based dressings to determine their effects on four separate MMPs. The dose–response versus MMP activity of bacterial collagenase, host‐derived MMP‐8 and MMPs‐2 and ‐9 was assessed using a simple mix‐and‐read fluorescent peptide activity assay. The enzyme's native activity in the absence of the gel was used to compare against the surfactant‐treated samples. We found that the surfactant affected the proteinase activity differently for each enzyme. The activity of the bacterial collagenase was increased at low concentrations but slightly inhibited as the concentrations increased. The host MMP‐8 collagenase responded similarly in that it was inhibited at higher concentrations. Interestingly, both MMP gelatinases presented with substantially increased activities, with MMP‐2 increased to 200% of native activity, while MMP‐9 presented with an increase of 300% activity over the same concentration range. MMPs appear to respond to a surfactant‐based gel dressing differentially, with the MMP most commonly elevated in chronic wounds having the highest boost to activity. In wounds with elevated MMPs, our data suggest that the use of these surfactant‐based dressings would be expected to enhance the activity of MMPs 2 and 9 gelatinases while simultaneously inhibiting MMP‐8 collagenase. Hypothetically, this imbalanced effect would support a protection of the native dermal collagen and removal of denatured materials. However, the demonstration of these anticipated consequences is still being investigated.