The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte
Open accessAbstract
A human erythrocyte membrane glycoprotein of 205,000 mol wt (gp205) has been identified as the C3b receptor of the erythrocyte, polymorphonuclear leukocyte (PMN), B lymphocyte, and monocyte. Initially, gp205 was sought and characterized as a constituent of the human erythrocyte membrane that can impair activation of the alternative complement pathway by inducing loss of function of the properdin-stabilized amplification C3 convertase (C3b,Bb,P) through displacement of Bb from C3b and by promoting cleavage-inactivation of C3b by C3b inactivator. These inhibitory activities of gp205 suggested that this membrane glyeoprotein had an affinity for C3b and prompted an analysis of its possible identity as the C3b receptor of human peripheral blood cells. The F(ab')2 fragment of rabbit IgG anti-gp205 inhibited the formation of rosettes with sheep EC3b of human erythroeytes, B lymphocytes, monocytes and PMN in a dose-response manner; the 50 percent inhibitory doses were 0.13/μg/ml, 0.90 μg/ml, 1.25 μg/ml, and 1.20 μg/ml of F(ab')2, respectively. Anti-gp205 did not impair the formation of rosettes by monocytes and B lymphocytes with sheep EC3bi or with EC3d. Scatchard analysis of the number of specific (125)I-F(ab')(2) anti-gp205 binding sites/cell revealed 950 sites/erythrocyte, 21,000 sites/cell of B lymphocyte preparation, 57,000 sites/PMN, and 48,000 sites/monocyte, indicating that the higher concentrations of antibody that had been required for inhibition of rosette formation by the nucleated cells reflected larger numbers of receptors on these cells. Direct evidence for the identity of gp205 as the C3b receptor of the four cell types was obtained when detergent-solubilized membrane proteins of the surface-radioiodinated cells were reacted with anti- gp205 and the immunoprecipitate was analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. In each instance, the antigenic material reacting with anti-gp205 represented a single protein with an apparent 205,000 mol wt. Thus, gp205 is the C3b receptor of human erythrocytes, PMN, B lymphocytes, and monocytes.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Cited by
Complement and its role in innate and adaptive immune responses
Dunkelberger, J. R., & Song, W.-C. (2010) · Cell Research · doi:10.1038/cr.2009.139 · Cited by 1,932
Epstein-Barr virus receptor of human B lymphocytes is the C3d receptor CR2.
Fingeroth, J. D., Weis, J. J., Tedder, T. F., Strominger, J. L., Biro, P. A., & Fearon, D. T. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.14.4510 · Cited by 939
Self-citationWright, S. D., & Silverstein, S. C. (1982) · The Journal of experimental medicine · doi:10.1084/jem.156.4.1149 · Cited by 435
The Role of Complement and Its Receptor in the Elimination of Immune Complexes
Epstein, F. H., Schifferli, J. A., Ng, Y. C., & Peters, D. K. (1986) · New England Journal of Medicine · doi:10.1056/nejm198608213150805 · Cited by 396
Iida, K., Mornaghi, R., & Nussenzweig, V (1982) · The Journal of experimental medicine · doi:10.1084/jem.155.5.1427 · Cited by 339
Metadata
- Authors
- Fearon, D.
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 1980-07-01
- Volume
- 152
- Issue
- 1
- Pages
- 20-30
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2129764349
- Cited by
- 644
- References
- 1
- FWCI
- 15.47
- Type
- journal article
- Language
- en
- Open access
- green
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- Fearon, D. (1980). Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte. The Journal of Experimental Medicine. https://doi.org/10.1084/jem.152.1.20
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