title: Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation.
abstract: MASP-1 is a versatile serine protease that cleaves a number of substrates in human blood. In recent years it became evident that besides playing a crucial role in complement activation MASP-1 also triggers other cascade systems and even cells to mount a more powerful innate immune response. In this review we summarize the latest discoveries about the diverse functions of this multi-faceted protease. Recent studies revealed that among MBL-associated serine proteases, MASP-1 is the one responsible for triggering the lectin pathway via its ability to rapidly autoactivate then cleave MASP-2, and possibly MASP-3. The crystal structure of MASP-1 explains its more relaxed substrate specificity compared to the related complement enzymes. Due to the relaxed specificity, MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling.
authors.affiliation: Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt. 2, H-1113 Budapest, Hungary.
authors.forename: József
authors.initials: J
authors.lastname: Dobó
authors.affiliation: Department of Clinical Research, University of Bern, and University Clinic of Haematology, University Hospital, Bern, Switzerland.
authors.forename: Verena
authors.initials: V
authors.lastname: Schroeder
authors.affiliation: Department of Clinical Research, University of Bern, and University Clinic of Haematology, University Hospital, Bern, Switzerland.
authors.forename: Lorenz
authors.initials: L
authors.lastname: Jenny
authors.affiliation: 3rd Department of Internal Medicine, Semmelweis University, Kútvölgyi út 4, H-1125 Budapest, Hungary.
authors.forename: László
authors.initials: L
authors.lastname: Cervenak
authors.affiliation: Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt. 2, H-1113 Budapest, Hungary.
authors.forename: Péter
authors.initials: P
authors.lastname: Závodszky
authors.affiliation: Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt. 2, H-1113 Budapest, Hungary. Electronic address: gal.peter@ttk.mta.hu.
authors.forename: Péter
authors.initials: P
authors.lastname: Gál
mesh_terms: D000818:Animals; D001777:Blood Coagulation / Q000502:physiology*; D001779:Blood Coagulation Factors / Q000378:metabolism; D037582:Complement Pathway, Mannose-Binding Lectin / Q000502:physiology; D006801:Humans; D007113:Immunity, Innate / Q000502:physiology*; D050606:Mannose-Binding Protein-Associated Serine Proteases / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D001779:Blood Coagulation Factors; C084067:MASP1 protein, human; D050606:Mannose-Binding Protein-Associated Serine Proteases
keywords: Blood coagulation; Bradykinin; Complement system; Endothelial cell; Lectin pathway; Serine protease