Complement-related serine proteases in tunicates and vertebrates.
Serum mannose-binding lectin binds to pathogens in association with a serine protease termed MASP, and in this form, plays a crucial role in innate immunity by activating complement in a manner similar to activation via the classical pathway. MASP, C1r and C1s belong to the same family of serine proteases. In addition to its presence in advanced species, MASP also exists in primitive life forms such as tunicates and may be an evolutionary prototype of this family.
Matsushita
M
M
Department of Biochemistry, Fukushima Medical College, Japan. mmatsu@cc.fmu.ac.jp
Endo
Y
Y
Nonaka
M
M
Fujita
T
T
D000818:Animals; D002352:Carrier Proteins / Q000276:immunology; D037222:Collectins; D003165:Complement System Proteins / Q000276:immunology*; D006801:Humans; D037102:Lectins / Q000276:immunology; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases / Q000737:chemistry / Q000276:immunology*; D014561:Urochordata / Q000276:immunology*; D014714:Vertebrates / Q000276:immunology*
D002352:Carrier Proteins; D037222:Collectins; D037102:Lectins; D003165:Complement System Proteins; C105296:MASP2 protein, human; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases