The initiating proteases of the complement system: Controlling the cleavage

被引：24

作者：

Duncan, Renee C. ^{[1
]}

Wijeyewickrema, Lakshmi C. ^{[1
]}

Pike, Robert N. ^{[1
]}

机构：

[1] Monash Univ, Dept Biochem & Mol Biol, Clayton, Vic 3800, Australia

来源：

BIOCHIMIE | 2008年 / 90卷 / 02期

关键词：

complement system; Cls; Clr; MASP-2; protease; serpin; C1-inhibitor;

D O I：

10.1016/j.biochi.2007.07.023

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The complement system is a vital component of the host immune system, but when dysregulated, can also cause disease. The system is activated by three pathways: classical, lectin and alternative. The initiating proteases of the classical and lectin pathways have similar domain structure and employ similar mechanisms of activation. The Clr, Cls and MASP-2 proteases have the most defined roles in the activation of the system. This review focuses on the mechanisms whereby their interaction with substrates and inhibitors is regulated. (c) 2007 Elsevier Masson SAS. All rights reserved.

引用

页码：387 / 395

页数：9

共 73 条

[21] Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent selpin-proteinase complex [J].

Futamura, A ;

Stratikos, E ;

Olson, ST ;

Gettins, PGW .

BIOCHEMISTRY, 1998, 37 (38) :13110-13119

[22] Structure and activation of the C1 complex of complement: unraveling the puzzle [J].

Gaboriaud, C ;

Thielens, NM ;

Gregory, LA ;

Rossi, V ;

Fontecilla-Camps, JC ;

Arlaud, GJ .

TRENDS IN IMMUNOLOGY, 2004, 25 (07) :368-373

[23] Crystal structure of the catalytic domain of human complement C1s: a serine protease with a handle [J].

Gaboriaud, C ;

Rossi, V ;

Bally, I ;

Arlaud, GJ ;

Fontecilla-Camps, JC .

EMBO JOURNAL, 2000, 19 (08) :1755-1765

[24] A true autoactivating enzyme -: Structural insight into mannose-binding lectin-associated serine protease-2 activations [J].

Gál, P ;

Harmat, V ;

Kocsis, A ;

Bián, T ;

Barna, L ;

Ambrus, G ;

Végh, B ;

Balczer, J ;

Sim, RB ;

Náray-Szabó, G ;

Závodszky, P .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (39) :33435-33444

[25] Structure and function of complement activating enzyme complexes:: C1 and MBL-MASPs [J].

Gál, P ;

Ambrus, G .

CURRENT PROTEIN & PEPTIDE SCIENCE, 2001, 2 (01) :43-59

[26] The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin [J].

Gregory, LA ;

Thielens, NM ;

Matsushita, M ;

Sorensen, R ;

Arlaud, GJ ;

Fontecilla-Camps, JC ;

Gaboriaud, C .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (28) :29391-29397

[27] X-ray structure of the Ca2+-binding interaction domain of C1s [J].

Gregory, LA ;

Thielens, NM ;

Arlaud, GJ ;

Fontecilla-Camps, JC ;

Gaboriaud, C .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (34) :32157-32164

[28] The biological functions of MBL-associated serine proteases (MASPs) [J].

Hajela, K ;

Kojima, M ;

Ambrus, G ;

Wong, KHN ;

Moffatt, BE ;

Ferluga, J ;

Hajela, S ;

Gál, P ;

Sim, RB .

IMMUNOBIOLOGY, 2002, 205 (4-5) :467-475

[29] The structure of MBL-associated serine protease-2 reveals that identical substrate Specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions [J].

Harmat, V ;

Gál, P ;

Kardos, J ;

Szilágyi, K ;

Ambrus, G ;

Végh, B ;

Náray-Szabó, G ;

Závodszky, P .

JOURNAL OF MOLECULAR BIOLOGY, 2004, 342 (05) :1533-1546

[30] The alternative pathway of complement in disease: opportunities for therapeutic targeting [J].

Holers, VM ;

Thurman, JM .

MOLECULAR IMMUNOLOGY, 2004, 41 (2-3) :147-152

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