Proteolytic signatures define unique thrombin-derived peptides present in human wound fluid in vivo.

ABSTRACT: The disease burden of failing skin repair and non-healing ulcers is extensive. There is an unmet need for new diagnostic approaches to better predict healing activity and wound infection. Uncontrolled and excessive protease activity, of endogenous or bacterial origin, has been described as a major contributor to wound healing impairments. Proteolytic peptide patterns could therefore correlate and "report" healing activity and infection. This work describes a proof of principle delineating a strategy by which peptides from a selected protein, human thrombin, are detected and attributed to proteolytic actions. With a particular focus on thrombin-derived C-terminal peptides (TCP), we show that distinct peptide patterns are generated in vitro by the human S1 peptidases human neutrophil elastas

SUBMITTER: Saravanan R 

PROVIDER: S-EPMC5640616 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature