Mannose-binding lectin-associated serine protease 1 (MASP-1) (MASP-1)

Mannose-binding lectin-associated serine protease 1 (MASP-1) is a key enzymatic component of the lectin pathway of the complement system, which is a critical part of the innate immune response [UniProt: P48740]. It is primarily synthesized in the liver and circulates in the blood as a zymogen in complex with pattern recognition molecules such as mannose-binding lectin (MBL) or ficolins [PubMed: 22106290]. Upon binding to pathogen-associated molecular patterns, MASP-1 undergoes autoactivation and subsequently activates MASP-2, which is essential for the formation of the C3 convertase [PubMed: 21148351]. Beyond its role in immunity, MASP-1 exhibits significant cross-talk with the coagulation cascade by cleaving fibrinogen and activating thrombin-activatable fibrinolysis inhibitor (TAFI) [PubMed: 24613984]. Mutations in the MASP1 gene are associated with 3MC syndrome, a rare developmental disorder characterized by craniofacial abnormalities [PubMed: 21258315]. Therapeutic targeting of MASP-1 is being explored for the treatment of complement-mediated diseases and thrombotic microangiopathies [ClinicalTrials.gov].

Other names

MASP1Serine protease 5Complement-activating component of Ra-reactive factorCRARFPRSS5Ra-reactive factor serine protease p100Mannan-binding lectin-associated serine protease 1

Inhibition of the serine protease activity of MASP-1 to prevent the activation of the lectin pathway and reduce pro-thrombotic signaling.