Degradation of extracellular matrix components by defined proteinases from the greenbottle larva Lucilia sericata used for the clinical debridement of non-healing wounds
✍ Scribed by L. Chambers; S. Woodrow; A.P. Brown; P.D. Harris; D. Phillips; M. Hall; J.C.T. Church; D.I. Pritchard
- Book ID
- 104460393
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 402 KB
- Volume
- 148
- Category
- Article
- ISSN
- 0007-0963
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✦ Synopsis
Background:
Larvae of the greenbottle fly lucilia sericata are used routinely for the clinical treatment of difficult necrotic and infected wounds. degradation by proteinases contained in larval excretory/secretory (es) products is thought to contribute to wound debridement by removal of dead tissue. however, proteinase activity may also affect host tissue remodelling processes.
Objectives:
To identify proteolytic enzymes derived from l. sericata es products with activities against fibrin and extracellular matrix (ecm) components.
Methods:
Larval proteinase activities were assayed in vitro using class-specific substrates and inhibitors. their action against fibrin and ecm components was examined using sodium dodecyl sulphate-polyacrylamide gel electrophoresis.
Results:
Three classes of proteolytic enzyme were detected in the secretions using fluorescein isothiocyanate-labelled casein as a model substrate. the predominant activity belonged to serine proteinases (ph optima 8-9) of two different subclasses (trypsin-like and chymotrypsin-like), with a weaker aspartyl proteinase (ph 5) and a metalloproteinase (ph 9) with exopeptidase characteristics also present. using skin-relevant ecm components as substrates l. sericata es products solubilized fibrin clots and degraded fibronectin, laminin and acid-solubilized collagen types i and iii. hydrolysis of ecm macromolecules was inhibited by preincubating es products with phenylmethylsulphonyl fluoride but not 4-amidinophenylmethylsulphonyl fluoride, indicating that degradation was due to the 'chymotrypsin-like' serine proteinase.
Conclusions:
These data suggest that a combination of l. sericata es proteinases involving chymotrypsin-like and trypsin-like activities could potentially influence wound healing events when maggots are introduced into necrotic and infected wounds, with the chymotrypsin-like activity involved in the remodelling of ecm components.