ArticleScientific reports2019
Characterization of the enzymatic activity of the serine protease domain of Factor VII activating protease (FSAP).
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Factor VII-Activating Protease (FSAP) and Its Importance in Hemostasis-Part II: A Link Between FSAP, Blood Coagulation, and Fibrinolysis: A Narrative Review.International journal of molecular sciences · 2025Review
- von Willebrand factor-binding protein (vWbp)-activated factor XIII and transglutaminase 2 (TG2) promote cross-linking between FnBPA from Staphylococcus aureus and fibrinogen.Scientific reports · 2023Article
- Factor VII Activating Protease (FSAP) and Its Importance in Hemostasis-Part I: FSAP Structure, Synthesis and Activity Regulation: A Narrative Review.International journal of molecular sciences · 2023Review
- FSAP Protects against Histone-Mediated Increase in Endothelial Permeability In Vitro.International journal of molecular sciences · 2022Article
- Identification of a Phage Display-Derived Peptide Interacting with the N-Terminal Region of Factor VII Activating Protease (FSAP) Enables Characterization of Zymogen Activation.ACS chemical biology · 2022Article
- Proteolytic activation of the epithelial sodium channel (ENaC) by factor VII activating protease (FSAP) and its relevance for sodium retention in nephrotic mice.Pflugers Archiv : European journal of physiology · 2022Article
- Proteolytic activity of contact factor zymogens.Journal of thrombosis and haemostasis : JTH · 2021Review
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Factor VII (FVII) activating protease (FSAP) is a circulating serine protease. Human genetic studies, based on the Marburg I (MI) (Gly221Glu, chymotrypsin numbering system) polymorphism, implicate FSAP in the pathogenesis of many diseases. Here, we describe the molecular and functional changes caused by the Gly221Glu substitution in the 220 loop using recombinant proteins expressed in E. coli. The serine protease domain (SPD) of wild type (WT) FSAP displayed auto-catalytic activation whereas the MI isoform displayed very low autocatalytic activation and low proteolytic activity against the chromogenic substrate S-2288, Factor VII, tissue factor pathway inhibitor as well as pro-urokinase. Introduction of a thermolysin cleavage site in the activation position (Arg15Gln) led to cleavage of both WT- and MI-SPD and the resulting WT-SPD, but not the MI-SPD, was active. Mutating the Gly221 position to Asp, Gln and Leu led to a loss of activity whereas the Ala substitution was partially active. These results suggest a disturbance of the active site, or non-accessibility of the substrate to the active site in MI-SPD. With respect to regulation with metal ions, calcium, more than sodium, increased the enzymatic activity of WT-SPD. Thus, we describe a novel method for the production of recombinant FSAP-SPD to understand the role of the MI-single nucleotide polymorphism (SNP) in the regulation of its activity.
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