Purification, measurement of concentration, and functional complement assay of human ficolins.
Ficolins constitute a group of lectins involved in innate immunity. L-Ficolin, H-ficolin, and M-ficolin are present in human serum. The human ficolins differ in carbohydrate-binding specificity, but they have in common the ability to recognize the acetyl group. L-Ficolin and H-ficolin are associated with serine proteases termed MASPs (MBL-associated serine proteases) and their truncated proteins, and the complexes (L/H-ficolin-MASP) activate the lectin pathway of complement upon binding to their ligands. Recombinant M-ficolin is also able to form a complex with MASP, resulting in complement activation. L-Ficolin and H-ficolin can be purified as a complex with MASP from serum by utilizing their binding specificities. These ficolin-MASP complexes have an ability to activate C4. Human ficolins are quantified by ELISA using specific antibodies or ligands.
Department of Applied Biochemistry, Tokai University, Hiratsuka, Japan.
Misao
M
Matsushita
David
D
Kilpatrick
Hiroshi
H
Shiraki
Yu
Y
Liu
Koichiro
K
Tateishi
Mitsushi
M
Tsujimura
Yuichi
Y
Endo
Teizo
T
Fujita
D003167:Complement Activation / Q000276:immunology; D003165:Complement System Proteins / Q000276:immunology* / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D050606:Mannose-Binding Protein-Associated Serine Proteases / Q000378:metabolism; D000097604:Ficolins
D003165:Complement System Proteins; D037102:Lectins; D050606:Mannose-Binding Protein-Associated Serine Proteases; D000097604:Ficolins