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Oral Abstracts (Session 1 of 5)
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Moderator: Patricia M. Mertz, BA (Presentation 32.4) Proteolytic differences between acute and chronic wounds: the role of serine proteases and their inhibitors Breda Cullen, PhD, Johnson & Johnson Wound Management, Gargrave, United Kingdom; Raymond Dunn, MD, University of Massachusetts Medical School, Worcester, Mass; Janice Lalikos, MD, University of Massachusetts Medical School, Worcester, Mass; Lorraine Nisbet, BSc, Johnson & Johnson Wound Management, Gargrave, United Kingdom; Alicia Essler, BSc, Johnson & Johnson Wound Management, Gargrave, United Kingdom; Paul Damiani, BS, University of Massachusetts Medical School, Worcester, Mass; Tim Roth, MS, University of Massachusetts Medical School, Worcester, Mass Abstract: The role of proteases in chronic wounds has been the subject of many investigations in recent years. These studies describe biochemical differences between chronic and acute wound fluids, in particular an elevation in the matrix metalloproteinases (MMPs) in chronic wounds. The resultant effect is that the chronic wound environment is hostile and not conducive to wound repair. In this study, fluid and tissue from chronic and acute wounds were collected and both MMP and serine protease activities measured. Using ELISA, samples were also assessed for levels of inhibitors and growth factors. Our results show that serine proteases were predominant and significantly elevated in chronic wound fluid. The serpins designed to control these proteases were unchanged compared to acute controls, resulting in excessive proteolytic activity. An increase in serine protease production without a concurrent increase in inhibitors may account for the observed reduction in growth factor levels in these chronic wound samples. This work indicates that there is an imbalance in serine protease activity due to an up regulation of protease production in chronic wounds. We also conclude that misregulation of serine proteases may be primarily responsible for this hostile environment, as these proteases readily degrade growth factors, reducing their efficacy. |
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