Abstract
Different leukocytes (Raji, Daudi, Rael lymphoid cells; human peripheral blood lymphocytes, and guinea pig granulocytes), which had been coated with C3 by incubation of 37 degrees C for 20 min in a C3 solution, were demonstrated to form rosettes with erythrocytes coated with complement components (EAC142). The percentage of rosettes was dependent of the amount of C3 present on the cells. Loading of the lymphoid cells with C3 was a time- and temperature-dependent process. C3b was unable to serve the same purposes, although C3 and C3b occupied the C3 receptors on the lymphoid cells to a comparable degree. C3 functions in a similar manner. The C42 enzyme can be replaced by trypsin, so that bridging units may consist of C3 + C42, C5 + C42 OR C3 + trypsin, and C5 + trypsin. Bridging units can be constructed also from C4 + C1. It is suggested that enzymes on one cell liberate labile binding groups of complement components on adjacent cells, thus inducing coupling of the two cells. The possibility is raised that this type of cell interlinkage may play a role in vivo, since there is accumulating evidence that complement components are expressed in the plasma membrane of different cells.
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- Bokisch V. A., Dierich M. P., Mūller-Eberhard H. J. Third component of complement (C3): structural properties in relation to functions. Proc Natl Acad Sci U S A. 1975 Jun;72(6):1989–1993. doi: 10.1073/pnas.72.6.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bokisch V. A., Müller-Eberhard H. J., Cochrane C. G. Isolation of a fragment (C3a) of the third component of human complement containing anaphylatoxin and chemotactic activity and description of an anaphylatoxin inactivator of human serum. J Exp Med. 1969 May 1;129(5):1109–1130. doi: 10.1084/jem.129.5.1109. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bokisch V. A., Sobel A. T. Receptor for the fourth component of complement on human B lymphocytes and cultured human lymphoblastoid cells. J Exp Med. 1974 Nov 1;140(5):1336–1347. doi: 10.1084/jem.140.5.1336. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brade V., Nicholson A., Bitter-Suermann D., Hadding U. Formation of the C3-cleaving properdin enzyme on zymosan. Demonstration that factor D is replaceable by proteolytic enzymes. J Immunol. 1974 Dec;113(6):1735–1743. [PubMed] [Google Scholar]
- Cooper N. R., Polley M. J., Müller-Eberhard H. J. The second component of human complement (C2): quantitative molecular analysis of its reactions in immune hemolysis. Immunochemistry. 1970 Apr;7(4):341–356. doi: 10.1016/0019-2791(70)90237-5. [DOI] [PubMed] [Google Scholar]
- Dierich M. P., Bokisch V. A. Receptor-binding sites on C3 and C3b. J Immunol. 1977 Jun;118(6):2145–2150. [PubMed] [Google Scholar]
- Dierich M. P., Reisfeld R. A. C3-mediated cytoadherence. Formation of C3 receptor aggregates as prerequisite for cell attachment. J Exp Med. 1975 Jul 1;142(1):242–247. doi: 10.1084/jem.142.1.242. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Edelman G. M. Surface modulation in cell recognition and cell growth. Science. 1976 Apr 16;192(4236):218–226. doi: 10.1126/science.769162. [DOI] [PubMed] [Google Scholar]
- Füst G., Erdei A., Sármay G., Medgyesi G. A., Gergely J. Functionally active C1 on the surface of human peripheral lymphocytes: its role in the complement-mediated inhibition of the Fc receptor of B lymphocytes. Clin Immunol Immunopathol. 1976 May;5(3):377–387. doi: 10.1016/0090-1229(76)90047-7. [DOI] [PubMed] [Google Scholar]
- Goldlust M. B., Shin H. S., Hammer C. H., Mayer M. M. Studies of complement complex C5b,6 eluted from--EAC-6: reaction of C5b,6 with EAC4b,3b and evidence on the role of C2a and C3b in the activation of C5. J Immunol. 1974 Sep;113(3):998–1007. [PubMed] [Google Scholar]
- Goldstein I. M., Weissmann G. Generation of C5-derived lysosomal enzyme-releasing activity (C5a) by lysates of leukocyte lysosomes. J Immunol. 1974 Nov;113(5):1583–1588. [PubMed] [Google Scholar]
- Halbwachs L., Lachmann P. J. Factor B of the alternative complement pathway on human lymphocytes. Scand J Immunol. 1976;5(6-7):697–704. doi: 10.1111/j.1365-3083.1976.tb03019.x. [DOI] [PubMed] [Google Scholar]
- Kalina M., Ginsburg H., Wolman M. Ultrastructural aspects of the adherence to target cells of in vitro differentiated lymphocytes. Proc Soc Exp Biol Med. 1975 Jul;149(3):796–799. doi: 10.3181/00379727-149-38901. [DOI] [PubMed] [Google Scholar]
- Kurth R. Surface alterations in cells infected by avian leukosis-sarcoma viruses. Biomembranes. 1976;8:167–233. doi: 10.1007/978-1-4684-9087-9_5. [DOI] [PubMed] [Google Scholar]
- Lerner R. A., Hodge L. D. Gene expression in synchronized lymphocytes: studies on the control of synthesis of immunoglobulin polypeptides. J Cell Physiol. 1971 Apr;77(2):265–276. doi: 10.1002/jcp.1040770215. [DOI] [PubMed] [Google Scholar]
- McConahey P. J., Dixon F. J. A method of trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol. 1966;29(2):185–189. doi: 10.1159/000229699. [DOI] [PubMed] [Google Scholar]
- Polley M. J., Müller-Eberhard H. J. Enharncement of the hemolytic activity of the second component of human complement by oxidation. J Exp Med. 1967 Dec 1;126(6):1013–1025. doi: 10.1084/jem.126.6.1013. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenthal A. S., Lipsky P. E., Shevach E. M. Macrophage-lymphocyte interaction and antigen recognition. Fed Proc. 1975 Jul;34(8):1743–1748. [PubMed] [Google Scholar]
- Ross G. D., Polley M. J. Specificity of human lymphocyte complement receptors. J Exp Med. 1975 May 1;141(5):1163–1180. doi: 10.1084/jem.141.5.1163. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schorlemmer H. U., Allison A. C. Effects of activated complement components on enzyme secretion by macrophages. Immunology. 1976 Nov;31(5):781–788. [PMC free article] [PubMed] [Google Scholar]
- Snyderman R., Shin H., Dannenberg A. M., Jr Macrophage proteinase and inflammation: the production of chemotactic activity from the fifth complement by macrophage proteinase. J Immunol. 1972 Oct;109(4):896–898. [PubMed] [Google Scholar]
- Tack B. D., Prahl J. W. Third component of human complement: purification from plasma and physicochemical characterization. Biochemistry. 1976 Oct 5;15(20):4513–4521. doi: 10.1021/bi00665a028. [DOI] [PubMed] [Google Scholar]
- Theofilopoulos A. N., Bokisch V. A., Dixon F. J. Receptor for soluble C3 and C3b on human lymphoblastoid (RAJI) cells. Properties and biologocal significance. J Exp Med. 1974 Mar 1;139(3):696–711. doi: 10.1084/jem.139.3.696. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vogt W., Dieminger L., Lynen R., Schmidt G. Alternative pathway for the activation of complement in human serum. Formation and composition of the complex with cobra venom factor that cleaves the third component of complement. Hoppe Seylers Z Physiol Chem. 1974 Feb;355(2):171–183. doi: 10.1515/bchm2.1974.355.1.171. [DOI] [PubMed] [Google Scholar]