A novel serine protease secreted by medicinal maggots enhances plasminogen activator-induced fibrinolysis
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A novel serine protease secreted by medicinal maggots enhances plasminogen activator-induced fibrinolysis. / van der Plas, Mariena J A; 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; Nibbering, Peter H.
I: PloS one, Bind 9, Nr. 3, 2014, s. e92096.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - A novel serine protease secreted by medicinal maggots enhances plasminogen activator-induced fibrinolysis
AU - van der Plas, Mariena J A
AU - Andersen, Anders S
AU - Nazir, Sheresma
AU - van Tilburg, Nico H
AU - Oestergaard, Peter R
AU - Krogfelt, Karen A
AU - van Dissel, Jaap T
AU - Hensbergen, Paul J
AU - Bertina, Rogier M
AU - Nibbering, Peter H
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
KW - Amino Acid Sequence
KW - Animals
KW - Blood Coagulation
KW - Diptera
KW - Fibrinolysin
KW - Fibrinolysis
KW - Humans
KW - Larva
KW - Molecular Sequence Data
KW - Plasminogen
KW - Plasminogen Activators
KW - Serine Proteases
KW - Time Factors
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1371/journal.pone.0092096
DO - 10.1371/journal.pone.0092096
M3 - Journal article
C2 - 24647546
VL - 9
SP - e92096
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 3
ER -
ID: 186451101