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A novel serine protease secreted by medicinal maggots enhances plasminogen activator-induced fibrinolysis

Van Der Plas, Mariena J A LU ; Andersen, Anders S. ; Nazir, Sheresma ; Van Tilburg, Nico H. ; Oestergaard, Peter R. ; Krogfelt, Karen A. ; Van Dissel, Jaap T. ; Hensbergen, Paul J. ; Bertina, Rogier M. and Nibbering, Peter H. (2014) In PLoS ONE 9(3).
Abstract

Maggots of the blowfly Lucilia sericata are used for the treatment of chronic wounds. As haemostatic processes play an important role in wound healing, this study focused on the effects of maggot secretions on coagulation and fibrinolysis. The results showed that maggot secretions enhance plasminogen activator-induced formation of plasmin and fibrinolysis in a dose- and time-dependent manner. By contrast, coagulation was not affected by secretions. Biochemical studies indicated that a novel serine protease within secretions, designated Sericase, cleaved plasminogen to several fragments. Recombinant Sericase degraded plasminogen leading amongst others to the formation of the mini-plasminogen like fragment Val454-plasminogen. In addition,... (More)

Maggots of the blowfly Lucilia sericata are used for the treatment of chronic wounds. As haemostatic processes play an important role in wound healing, this study focused on the effects of maggot secretions on coagulation and fibrinolysis. The results showed that maggot secretions enhance plasminogen activator-induced formation of plasmin and fibrinolysis in a dose- and time-dependent manner. By contrast, coagulation was not affected by secretions. Biochemical studies indicated that a novel serine protease within secretions, designated Sericase, cleaved plasminogen to several fragments. Recombinant Sericase degraded plasminogen leading amongst others to the formation of the mini-plasminogen like fragment Val454-plasminogen. In addition, the presence of a non-proteolytic cofactor in secretions was discovered, which plays a role in the enhancement of plasminogen activator-induced fibrinolysis by Sericase. We conclude from our in vitro studies that the novel serine protease Sericase, with the aid of a non-proteolytic cofactor, enhances plasminogen activator-induced fibrinolysis.

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author
; ; ; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
PLoS ONE
volume
9
issue
3
article number
e92096
publisher
Public Library of Science (PLoS)
external identifiers
  • pmid:24647546
  • scopus:84898612013
ISSN
1932-6203
DOI
10.1371/journal.pone.0092096
language
English
LU publication?
no
id
07960333-c1e8-4318-9a77-bd99dcc78973
date added to LUP
2018-01-15 10:54:24
date last changed
2024-08-05 11:14:05
@article{07960333-c1e8-4318-9a77-bd99dcc78973,
  abstract     = {{<p>Maggots of the blowfly Lucilia sericata are used for the treatment of chronic wounds. As haemostatic processes play an important role in wound healing, this study focused on the effects of maggot secretions on coagulation and fibrinolysis. The results showed that maggot secretions enhance plasminogen activator-induced formation of plasmin and fibrinolysis in a dose- and time-dependent manner. By contrast, coagulation was not affected by secretions. Biochemical studies indicated that a novel serine protease within secretions, designated Sericase, cleaved plasminogen to several fragments. Recombinant Sericase degraded plasminogen leading amongst others to the formation of the mini-plasminogen like fragment Val454-plasminogen. In addition, the presence of a non-proteolytic cofactor in secretions was discovered, which plays a role in the enhancement of plasminogen activator-induced fibrinolysis by Sericase. We conclude from our in vitro studies that the novel serine protease Sericase, with the aid of a non-proteolytic cofactor, enhances plasminogen activator-induced fibrinolysis.</p>}},
  author       = {{Van Der Plas, Mariena J A and Andersen, Anders S. and Nazir, Sheresma and Van Tilburg, Nico H. and Oestergaard, Peter R. and Krogfelt, Karen A. and Van Dissel, Jaap T. and Hensbergen, Paul J. and Bertina, Rogier M. and Nibbering, Peter H.}},
  issn         = {{1932-6203}},
  language     = {{eng}},
  month        = {{03}},
  number       = {{3}},
  publisher    = {{Public Library of Science (PLoS)}},
  series       = {{PLoS ONE}},
  title        = {{A novel serine protease secreted by medicinal maggots enhances plasminogen activator-induced fibrinolysis}},
  url          = {{http://dx.doi.org/10.1371/journal.pone.0092096}},
  doi          = {{10.1371/journal.pone.0092096}},
  volume       = {{9}},
  year         = {{2014}},
}