By Henry G. Kunkel and Frank J. Dixon (Eds.)
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Extra info for Advances in Immunology, Vol. 29
1977). Activation and lysis were shown to be independent of antibody by use of either preabsorbed serum or hypogammaglobulinemic serum. The property of activating the alternative pathway appears to reside in Raji cell surface structures which are Epstein-Barr (EB) virus induced. , 1978). The precise mechanism of Raji cell killing was investigated by correlating cellular binding of radiolabeled proteins with the release from the cytoplasm of radioactive markers and by measuring the effect of inhibition of protein synthesis on both events.
1974). CVF forms with mammalian factor B a C3 and C 5 activating enzyme. It differs from the physiological C3/C5 convertase in that it is unusually stable and can act on C 5 in the absence of C3 (Medicus, 1977). CVF has been used extensively for experimental depletion of animals of circulating C3. There are marked similarities between the alternative and the classical pathways of complement activation. The initial enzymes of both pathways catalyze the formation of target-bound C3 convertase. Instead of C3b, the classical enzyme utilizes the homologous protein C4b as nonenzymic subunit.
1966a) and does not distinguish between activators and nonactivators of the pathway. The concept that initial deposition of C3b is a random event was advanced by Lachmann and associates (Lachmann and Nicol, 1973; Nicol and Lachmann, 1973; Lachmann and Halbwachs, 1975) in the form of the " tick-over" hypothesis. It predicts that low level C3b deposition occurs on host cells and foreign particles alike. Suggestive evidence to support this prediction is the finding of C3d antigenic determinants on freshly obtained human erythrocytes and of their increase upon storage of blood (Szymanski and Ogden, 1979).