By J. E. Volanakis (auth.), John D. Lambris Ph. D. (eds.)
The 3rd section of supplement, C3, is without doubt one of the such a lot flexible proteins and an immense player in immune surveillance and immune reaction pathways. Its multifunctio nality is predicated on its skill to have interaction particularly with a number of serum supplement proteins, mobilephone floor receptors, and mem brant;-associated regulatory proteins. considered one of its such a lot exciting thoughts of interplay with mobile surfaces is the covalent binding of activated C3 in the course of the inner thioester. the sector has improved over the last 10 years and a wealth of knowledge has amassed. C3 from a number of species and lots of of the human C3 binding proteins were cloned and expressed. a variety of mobile responses mediated by way of the diffe lease fragments of C3 were defined. The findings that C3 interacts in a ligand-receptor-like model with proteins of nonself starting place equivalent to the gC of herpes simplex virus, a 70-kDa protein from Candida albicans, proteins from Epstein-Barr virus, and so forth. has opened a brand new box of research. The papers assembled during this quantity summarize the wealth of information at the numerous points of the C3 interactions; jointly they create to the reader new details at the chemistry, molecular gene tics, biology, and pathophysiology of C3 and C3-binding proteins. Emphasis is given to structural positive aspects as they relate to features. Spring 1989 JOHN D. LAMBRIS, HANS J. MULLER-EBERHARD desk of Contents J. E. VOLANAKIS: Participation of C3 and Its Ligands in supplement Activation . . . . . . . . . . . 1 S. R. BARNUM, G. FEY, and B. F. TACK: Biosynthesis and Genetics of C3 . . . . . . . . . . . . .
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Additional resources for The Third Component of Complement: Chemistry and Biology
1987) size reported for mouse liver C3. It should be noted that these analyses utilized agarose gel electrophoresis, which may not completely denature all RNA species due to secondary structure features, and therefore the sizes reported are not absolute. 3 kb in size from poly(At mRNA (WARREN et al. 1987; G. DARLINGTON and R. STRUNK, personal communication). Peripheral blood monocytes (WARREN et al. 1987; STRUNK et al. 1985) and the monocyte-like cell line U937 (W. 2 kb. 2 kb message in an amount one-fifth that of monocytes and 1% that of hepatocytes (WARREN et al.
Mol Immunol 24: 1105-1111 Morris KM, Aden DP, Knowles BB, Colten HR (1982b) Complement biosynthesis by the human hepatoma-derived cell line HepG2. 1 Clin Invest 70: 906-913 Morris KM, Goldberger G, Colten HR, Aden DP, Knowles BB (1982a) Biosynthesis and processing of a human precursor complement, pro-C3, in a hepatoma-derived cell line. Science 215: 399-400 Mount SM (1982) A catalogue of splice junction sequences Nucleic Acids Res 10: 459-472 Muller-Eberhard Hl, Schreiber RD (1980) Molecular biology and chemistry of the alternative pathway of complement.
Eur J Immunol 11: 140-146 Whitehead AS, Solomon E, Chambers S, Bodmer WF, Povey S, Fey G (1982) Assignment of the structural gene for the third component of human complement to chromosome 19. Proc Nat! Acad Sci USA 79: 5021-5025 Wieacker P, Fey G, Vorculescu I, Roper HH (1983) Exclusion of the C3 gene from the 19q133 to 19qter region by Southern analysis of human rodent somatic cell hybrids employing a cloned genomic C3 fragment. Acta Anthropogenet 7: 107-112 Wiebauer K, Domdey H, Diggelmann H, Fey G (1982) Isolation and analysis of genomic DNA clones encoding the third component of mouse complement.