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Synthesis of Complement Components C5, C6, C7, C8 and C9 in Vitro by Human Monocytes and Assembly of the Terminal Complement Complex
Author(s) -
HETLAND G.,
JOHNSON E.,
FALK R. J.,
ESKELAND T.
Publication year - 1986
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1986.tb02130.x
Subject(s) - complement system , agarose , polyclonal antibodies , complement membrane attack complex , monoclonal antibody , sepharose , antibody , in vitro , alternative complement pathway , chemistry , microbiology and biotechnology , classical complement pathway , complement component 5 , activator (genetics) , biochemistry , biology , immunology , enzyme , receptor
Monocytes cultured under serum‐free conditions secreted protein which bound covalently and non‐covalently to agarose beads, an activator of the alternative pathway of complement. There was a significant binding of monoclonal anti‐C3c antibodies, polyclonal anti‐C5, anti‐C6, anti‐C7, anti‐C8, and anti‐C9 antibodies, and of a monoclonal antibody against a neoantigen of polymerized C9 to agarose beads incubated with the monocytes for 24, 48, 72 or 96 h. From these results, we conclude that monocytes produce C5, C6, C7, C8 and C9 that assemble as the terminal complement complex on the surface of the agarose beads. Activation by agarose of the alternative pathway with generation of particle bound C3 and C5 convertases is a prerequisite for the subsequent formation of the terminal complement complex. Whether SC5b‐9 or the membrane attack of complement (C5b‐9) is formed on the beads will be examined.