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The emerging roles of mannose‐binding lectin‐associated serine proteases ( MASP s) in the lectin pathway of complement and beyond
Author(s) -
Dobó József,
Pál Gábor,
Cervenak László,
Gál Péter
Publication year - 2016
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/imr.12460
Subject(s) - mannan binding lectin , lectin , masp1 , proteases , lectin pathway , complement system , serine , ficolin , biology , mannose , complement (music) , c type lectin , cd69 , alternative complement pathway , immunology , microbiology and biotechnology , biochemistry , serine protease , immune system , enzyme , phenotype , protease , complementation , il 2 receptor , t cell , gene
Summary Mannose‐binding lectin ( MBL )‐associated serine proteases ( MASP s) are the enzymatic constituents of the lectin pathway of the complement system. They are complexed with large pattern recognition molecules ( PRM s) such as MBL , other collectins, and ficolins. The main function of two of the three MASP s has crystallized lately: MASP ‐1 autoactivates first, then it activates MASP ‐2, and finally both participate in the formation of the C4b2a convertase. In addition to this, both enzymes are involved in several other processes which are subject to intense research nowadays. Notably, MASP ‐1, as a promiscuous enzyme, has been implicated in the coagulation cascade, in the kinin generating contact system, and in cellular activation through protease‐activated receptor ( PAR ) cleavage on endothelial cells. The third protease MASP ‐3 has emerged recently as the protease responsible for pro‐factor D activation in resting blood, providing a fundamental link between two complement pathways. At present all three MASP s have at least one well‐defined role and several other possible functions were implicated. Defect or more likely over‐activation of MASP s may culminate into diseases such as ischemia–reperfusion injury ( IRI ); hence, MASP s are all potential targets of drug development.