Complement Receptor Type 1
This review will focus on the complement receptor type 1 (CR1, CD35) expressed by erythrocytes and will cover its structure, molecular biology, and function as a membrane inhibitor of complement activation. The CR1 present on phagocytic cells and lymphocytes has similar functions in regulation of complement activation and serves as a receptor responsible for triggering cellular activation events such as phagocytosis or Ig synthesis. These latter receptor functions of CR1 are not covered in this review, and the reader is referred to several past reviews about leukocyte CR1 for this information (Ross and Medof 1985; Wright and Griffin 1985; Fearon and Ahearn 1989; Ross et al. 1989). Erythrocyte CR1 has three functions in regulation of complement activation that are covered in this review: (a) inhibition of the C3 and C5 convertases of the classical and alternative pathways of complement activation; (b) factor I cofactor activity for cleavage of C3b and iC3b; (c) adsorption of soluble immune complexes, thereby inhibiting complement-mediated inflammation. Table 1 summarizes the attributes of CR1 on all cell types.
KeywordsSystemic Lupus Erythematosus Complement Receptor Cofactor Activity Short Consensus Repeat Soluble Immune Complex
Unable to display preview. Download preview PDF.
- Bartow TJ, Klickstein LB, Fearon DT (1989) Localization of monoclonal antibody epitopes on CR1 by deletion mutagenesis. Compl Inflamm 6: 312 (abstract)Google Scholar
- Fearon DT, Ahearn JM (1989) Complement receptor type 1 (C3b/C4b receptor, CD35) and complement receptor type 2 (C3d/Epstein-Barr virus receptor; CD21). In: Lambris JD (ed) The third component of complement. Chemistry and biology. Springer, Berlin Heidelberg New York, pp 83–98 (Current topics in microbiology and immunology, vol 153)Google Scholar
- Fielder AHL, Walport MJ, Batchelor JR, Rynes Rl, Black CM, Dodi IA, Hughes GRV (1983) Family study of the major histocompatibility complex in patients with systemic lupus erythematosus: importance of null alleles of C4A and C4B in determining disease susceptibility. Br Med J 286: 425–428CrossRefGoogle Scholar
- Medof ME, Gottlieb A, Kinoshita T, Hall S, Silber R, Nussenzweig V, Rosse WF (1987) Relationship between decay accelerating factor deficiency, diminished acetylcholinesterase activity, and defective terminal complement pathway restriction in paroxysmal nocturnal hemoglobinuria erythrocytes. J Clin Invest 80: 165–174PubMedCrossRefGoogle Scholar
- Nourshargh S, Rampart M, Hellewell PG, Jose PJ, Harlan JM, Edwards AJ, Williams TJ (1989) Accumulation of 111ln-neutrophils in rabbit skin in allergic and non-allergic inflammatory reactions in vivo. Inhibition by neutrophil pretreatment in vitro with a monoclonal antibody recognizing the CD18 antigen. J Immunol 142: 3193–3198PubMedGoogle Scholar
- Ross GD, Newman SL, Lambris JD, Devery-Pocius JE, Cain JA, Lachmann PJ (1983) Generation of three different fragments of bound C3 with purified factor I or serum. II. Location of binding sites in the C3 fragments for factors B and H, complement receptors, and bovine conglutinin. J Exp Med 158: 334–352PubMedCrossRefGoogle Scholar
- Ross GD, Yount WJ, Walport MJ, Winfield JB, Parker CJ, Fuller CR, Taylor RP, Myones BL, Lachmann PJ (1985) Disease-associated loss of erythrocyte complement receptors (CR1, C3b-receptors) in patients with systemic lupus erythematosus and other diseases involving autoantibodies and/or complement activation. J Immunol 135: 2005–2014PubMedGoogle Scholar
- Ross GD, Walport MJ, Hogg N (1989) Receptors for IgG Fc and fixed C3. In: Asherson GL, Zembala M (eds) Human monocytes. Academic, London, pp 123–139Google Scholar
- Wallace JM, Wormall A (1931) Red-cell adhesion in trypanosomiasis of man and other animals; some experiments on mechanism of reaction. Parasitology 23: 346–359Google Scholar
- Weisman HF, Bartow T, Leppo MK, Marsh HC Jr, Carson GR, Concino MF, Boyle MP, Roux KH, Weisfeldt ML, Fearon DT (1990) Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis. Science 249: 146–151PubMedCrossRefGoogle Scholar
- Wong WW, Cahill JM, Rosen MD, Kennedy CA, Bonaccio ET, Morris MJ, Wilson JG, Klickstein LB, Fearon DT (1989) Structure of the human CR1 gene. Molecular basis of the structural and quantitative polymorphisms and identification of a new CR1 -like allele. J Exp Med 169: 847–863PubMedCrossRefGoogle Scholar