The biological functions of MBL-associated serine proteases (MASPs)
The biological functions of MBL-associated serine proteases (MASPs)
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DOI：
10.1078/0171-2985-00147
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发表时间：
2002-09-01
期刊：
影响因子：
2.8
通讯作者：
Sim, RB
中科院分区：
文献类型：
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作者：
Hajela, K;Kojima, M;Sim, RB
甘露糖结合凝集素相关丝氨酸蛋白酶（MASPs）一直是深入研究的主题，特别是在过去10年中。首先，一个，然后两个，目前3个MASP已被表征。最初认为MBL + MASPs系统可能非常类似于补体经典途径的C1复合物，并且MASP1和MASP2可能具有与其经典途径同源物C1r和C1s相似的活性。MASP2确实具有与C1类似的活性，但MASP1不具有C1 r或C1 s的活性。MASP1被认为通过直接切割C3而作用于补体系统，但用重组和纯化的天然MASP1进行的研究表明，这种蛋白酶直接切割C3非常缓慢，并且可能没有生物学意义。MASP1和MASP2似乎不具有C1r和C1s那样狭窄的特异性，并且可能具有补体蛋白以外的重要底物。例如，MASP 1确实切割纤维蛋白原，释放纤维蛋白肽B（一种趋化因子），并且还切割和活化血浆转氨酶（因子XIII）。这些反应也与抵抗微生物有关，并且可能代表MASP1的生物学显著作用。
The Mannose-binding lectin-associated serine proteases (MASPs) have been the subject of intensive research particularly over the past 10 years. First one, then two, and currently 3 MASPs have been characterized. Initially it was thought likely that the MBL + MASPs system would resemble very closely the C1 complex of the complement classical pathway, and that MASP1 and MASP2 would have similar activities to their classical pathway homologues C1r and C1s. MASP2 does certainly have similar activities to C1s, but MASP1 does not have the activities of either C1r or C1s. MASP1 has been thought to act on the complement system by cleaving C3 directly, but work with recombinant and purified native MASP1 shows that direct C3 cleavage by this protease is very slow, and may not be biologically significant. MASP1 and MASP2 appear not to have such a narrow specificity as C1r and C1s, and may have significant substrates other than complement proteins. As an example, MASP1 does cleave fibrinogen, releasing fibrinopeptide B (a chemotactic factor) and also cleaves and activates plasma transglutaminase (Factor XIII). These reactions are also relevant to defence against microorganisms, and may represent a biologically significant action of MASP1.