Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development.

1. PTX-3 and MASP-3 enhanced prediction of myocardial infarction compared to the traditional Framingham risk score alone PMID: 28216633
2. Study proposes that RaRF may be a factor in the resistance mechanism and thus a potential target for leukemia therapy using retinoic acid. PMID: 28945224
3. We present the first case with an intragenic MASP1 deletion featuring 3MC syndrome. Our patient features typical 3MCS symptoms and a characteristic face but no cleft lip/palate. PMID: 29407414
4. Studies results provide evidence that Crohn's disease patients have an impairment in mannose-binding lectin-mannose-associated serine protease functional activity and that this defect is associated with mannose-binding lectin 2 and NOD2 variants. PMID: 27404661
5. These results indicate that PLTP and MASP-1 can serve as plasma biomarkers for the early diagnosis and treatment of Age-related macular degeneration , which is critical for preventing Age-related macular degeneration -related blindness. PMID: 27605007
6. MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked. PMID: 27535802
7. a strong influence of MASP-1, complement activation and pathway-specific inhibition on coagulation in a microvascular flow system PMID: 29324883
8. The complement lectin pathway serine proteases, MASP-1 and MASP-2, can be associated with ischaemic stroke development risk and may participate in pathological events leading to post-ischaemic brain damage. Moreover rs3203210 and rs147270785 single nucleotide polymorphisms in the MASP1 and MASP2 genes, respectively, are strongly associated with ischaemic stroke. PMID: 28720568
9. Our finding suggests that complement MASP-1 can increase adhesion between neutrophils and endothelial cells in a direct fashion PMID: 27219453
10. Study discovered novel and independent associations of prediabetes and related traits with MASP1, and some evidence for associations with THBS1, GPLD1 and ApoA-IV, suggesting a role for these proteins in the pathophysiology of type 2 diabetes. PMID: 27344311
11. MASP-1 plasma levels were higher among patients with type 2 diabetes and diabetic mice PMID: 28318015
12. MASP-1 was not associated with adverse cardiovascular outcomes in diabetics. PMID: 27055907
13. high serum CL-L1 concentration in critically ill children upon PICU admission is associated with an increased risk of infection and prolonged need of intensive care, and counteracts the protective effect of having a high MASP-3 concentration PMID: 27057739
14. Our study provided novel evidence that genetic variations in complement genes C6 and MASP1were associated with preeclampsia risk, and that the risk varied by preeclampsia subtypes PMID: 27405496
15. The exclusion of the MASP1 and COLEC11 Loci in two individuals from different consanguineous families and the absence of mutations in four further individuals sequenced for both genes raises the possibility that that there is further genetic heterogeneity of 3MC syndrome PMID: 26789649
16. Plasma MASP-1 concentration at the early stage of Kawasaki disease is predictive of length of time of recovery from coronary artery lesions. PMID: 26536449
17. MASP-1 and MASP-2 are activated during blood clotting. This activation is triggered by activated platelets and by the generation of fibrin during thrombotic reactions in vitro and in vivo, and may represent a novel activation/amplification mechanism in thromboinflammation. PMID: 26614707
18. described for the first time a detailed model of prothrombin activation by MASP-1 PMID: 26645987
19. Fusion of MAP-1 with FH domains represents a novel therapeutic approach for selective targeting upstream and central complement activation at sites of inflammation PMID: 26260032
20. The levels of MASP-1 and MASP-1/C1-INH complexes are reduced in HAE patients compared with controls. Both MASP-1 and MASP-1/C1-INH complexes are related to the degree of complement C4 consumption PMID: 26371246
21. Polymorphisms in MASP1 and MASP2 genes are associated with the susceptibility or protection to infectious diseases. (Review) PMID: 25862418
22. Because MASP-1 and MASP-2 have been shown to interact directly with blood coagulation, elevated levels of these proteins may play a role in the enhanced thrombotic environment and consequent vascular complications in diabetes. PMID: 25533914
23. MASP-1 cleaves prothrombin and identified its cleavage sites, suggesting that MASP-1 gives rise to an alternative active form of thrombin by cleaving at the cleavage site R393. PMID: 25745807
24. MASP-1 may activate neutrophils indirectly via endothelial cells. PMID: 24489848
25. Data indicate that MASP-1 and MASP-2 can readily form heterodimers after dissociation and re-association, however, in the presence of Ca(2+) exchange of subunits is slow between the homodimers. PMID: 24424083
26. Data show that among the components of the mannose-binding lectin (MBL) and associated serine proteases (MASPs) only MASP-1 is able to trigger response in endothelial cells (HUVECs) and the proteolytic activity of MASP-1 is essential. PMID: 24472859
27. We found that rMAP-1 can engage in heterocomplexes with rMASP-1 and rMASP-3 in a calcium-dependent manner PMID: 24683193
28. Polymorphisms in the MASP1 gene are associated with serum levels of MASP-1, MASP-3, and MAp44 PMID: 24023860
29. The serine protease domain of MASP-3 exerts weak enzymatic activity. PMID: 23861840
30. Studies indicate that initiation of lectin compleme pathway leads to activation of the serine proteases MASP-1 and MASP-2 resulting in deposition of C4 on the activator and assembly of the C3 convertase. PMID: 23911397
31. accelerates fibrosis progression in hepatitis C virus-induced liver disease PMID: 23841802
32. collectin-11 associates with all the known MBL-associated serine proteases (MASP-1, MASP-2 and MASP-3) as well as the lectin complement pathway regulator MAP-1. PMID: 23220946
33. insights into the function of MASP-3 reveal how a mutation in this enzyme causes it to be inactive and thus contribute to the 3MC syndrome. PMID: 23792966
34. In this study, we demonstrate that, although MASPs do not directly form heterodimers, the addition of mannan-binding lectin or ficolins allows the formation of MASP-1-MASP-2 co-complexes. PMID: 23785123
35. autoactivation of MASP-1 is crucial for the activation of MBL/ficolin.MASP complexes, and in the proenzymic phase zymogen MASP-1 controls the process PMID: 23386610
36. MASP-1 seems to be involved in activation of both the lectin and alternative complement pathways--{review} PMID: 23402018
37. A crucial role of MASP-1 is demonstrated in the activation of MASP-2, as well as of MASP-3, based on a patient harboring a nonsense mutation in the common part of the MASP1 gene. PMID: 22966085
38. MAP-1 competes with all three MASPs for ligand binding and is able to mediate a strong dose-dependent inhibitory effect on the lectin pathway activation, as measured by levels of C3 and C9. PMID: 22854970
39. Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2. PMID: 22511776
40. MASP-1 activates MASP-2 and, moreover, inhibition of MASP-1 prevents autoactivation of MASP-2 PMID: 22691502
41. MASP-1, in concerted action with other complement and coagulation proteins, may play a role in fibrin clot formation. PMID: 22536427
42. MASP-1 was present at adult level at 1 year of age, while it was 60% at birth. The present data prepare the ground for studies on the associations of MASP-1 levels with disease. PMID: 22670777
43. The interaction of mannan-binding lectin (MBL) with its associated serine proteases (MASPs) was investigated using recombinant (r) MBL, plasma-derived (pd) MBL, rMASP-3 and rMAp19. rMASP-3 and rMAp19 bound to free available sites on rMBL and pdMBL. PMID: 22607836
44. showed that MASP-1 was able to cleave HK resulting in BK production. MASP-2 could also cleave HK but could not release BK. The cleavage pattern of MASPs is similar but not strictly identical to that of kallikrein PMID: 21625439
45. these findings demonstrate a role for complement pathway factors in fundamental developmental processes and in the etiology of 3MC syndrome. PMID: 21258343
46. MBL-associated serine protease-3 down-regulate Ficolin-3 mediated complement activation through the lectin pathway. PMID: 19939495
47. These results implicate mutations of MASP1 as the cause of a human malformation syndrome and demonstrate the involvement of MASP1 in facial, umbilical, and ear development during the embryonic period. PMID: 21035106
48. MBL-associated serine protease 3 (MASP-3) also inhibited binding between MBL and CD91, suggesting that the site of interaction is located at or near the MASP-MBL interaction site. PMID: 21054788
49. We present a novel, phylogenetically conserved protein, MAp44, which is found in human serum at 1.4 microg/ml in Ca(2+)-dependent complexes with the soluble pattern recognition molecules. PMID: 19917686
50. MASP-1 has a crucial role in the initiation steps of lectin pathway activation most probably by activating MASP-2 PMID: 20817870

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Secreted.

Peptidase S1 family

Protein of the plasma which is primarily expressed by liver.

HGNC: 6901

OMIM: 257920

KEGG: hsa:5648

UniGene: Hs.89983