Factor VII Activating Protease (FSAP) and Its Importance in Hemostasis-Part I: FSAP Structure, Synthesis and Activity Regulation: A Narrative Review

Factor VII activating protease (FSAP) was first isolated from human plasma less than 30 years ago. Since then, many research groups have described the biological properties of this protease and its role in hemostasis and other processes in humans and other animals. With the progress of knowledge abo...

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Bibliographic Details
Published in:International journal of molecular sciences 2023-03, Vol.24 (6), p.5473
Main Authors: Kwiatkowska, Iga, Żekanowska, Ewa, Lattanzi, Simona, Alexandre, Andrea M, Kister-Kowalska, Agata, Słomka, Artur
Format: Article
Language:English
Subjects:
Animals
Antigens
Biological properties
Blood coagulation factors
Blood plasma
Blood platelets
Cardiovascular Diseases
Chemical compounds
Coagulation factors
Cytokines
Endothelium
Factor VII - metabolism
Genes
Hemostasis
Hemostasis - physiology
Hemostatics
Humans
Hyaluronic acid
Peptide Hydrolases
Plasma
Protease
Proteases
Protein structure
Proteinase
Proteins
Review
Serine Endopeptidases - metabolism
Tumor necrosis factor-TNF
Veins & arteries
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Summary:Factor VII activating protease (FSAP) was first isolated from human plasma less than 30 years ago. Since then, many research groups have described the biological properties of this protease and its role in hemostasis and other processes in humans and other animals. With the progress of knowledge about the structure of FSAP, several of its relationships with other proteins or chemical compounds that may modulate its activity have been explained. These mutual axes are described in the present narrative review. The first part of our series of manuscripts on FSAP describes the structure of this protein and the processes leading to the enhancement and inhibition of its activities. The following parts, II and III, concern the role of FSAP in hemostasis and in the pathophysiology of human diseases, with particular emphasis on cardiovascular diseases.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms24065473