Abstract
It is known that human complement is more efficient at lysing erythrocytes of other species than at lysing homologous erythrocytes. This phenomenon has been called homologous species restriction (Hänsch et al. 1981) of complement- mediated hemolysis. Human complement is restricted by at least three proteins known so far. Decay accelerating factor (Nicholson-Weller et al. 1982) is a powerful regulator of cell bound C3/C5 convertase. At the end of the complement cascade, two separate proteins seem to act. The lower molecular weight protein was first isolated as P18 (Sugita et al. 1988) and is also known as IF5 or HRF20 (Okada et al. 1989), MIRL (Holguin et al. 1989), and CD59 (Davies et al. 1989). The other higher molecular weight protein is homologous restriction factor (Zalman et al. 1986a), also known as C8 binding protein (Schönermark et al. 1986) and MIP (Watts et al. 1990). This review will focus on homologous restriction factor.
Keywords
- Human Erythrocyte
- Paroxysmal Nocturnal Hemoglobinuria
- Human Erythrocyte Membrane
- Paroxysmal Nocturnal Hemoglobinuria Patient
- Homologous Restriction
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
Dacie JV, Richardson N (1943) The influence of pH on in vitro haemolysis in nocturnal hemoglobinuria. J Pathol Bacteriol 55: 375
Davé SJ, Sodetz JM (1990) Regulation of the membrane attack complex of complement-evidence that C8γ is not the target of homologous restriction factors. J Immunol 144: 3087–3090
Davies A, Simmons DL, Hale G, Harrison RA, Tighe H, Lachmann PJ, Waldmann H (1989) CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells. J Exp Med 170: 637–654
Davitz MA, Low MG, Nussenzweig V (1986) Release of decay-accelerating factor (DAF) from the cell membrane by phosphotidyl-inositol specific phospholipase C (PIPLC). J Exp Med 163: 1150–1161
Götze O, Müller-Eberhard HJ (1970) Lysis of erythrocytes by complement in the absence of antibody. J Exp Med 132: 898–903
Hänsch GM (1988) The homologous species restriction of the complement attack: structure and function of the C8 binding protein. In: Podack ER (ed) Cytotoxic effector mechanisms. Springer, Berlin Heidelberg New York, pp 109–118 (Current topics in microbiology and immunology, vol 140)
Hänsch GM, Hammer CH, Vanguin P, Shin ML (1981) Homologous species restriction in lysis of erythrocytes by terminal complement proteins. Proc Natl Acad Sci USA 78: 5118–5121
Hänsch GM, Schönermark S, Roelcke D (1987) Paroxysmal nocturnal hemoglobinuria type III-lack of an erythrocyte membrane protein restriction the lysis by C5b-9. J Clin Invest 80: 7–12
Hänsch GM, Wella PF, Nicholson-Weller A (1988) Release of C8 binding protein (C8bp) from the cell membrane by phosphotidyl-inositol-specific phospholipase C. Blood 72: 1089–1092
Holguin MH, Fredrick LR, Bernshaw NJ, Wilcox LA, Parker LJ (1989) Isolation and characterization of a membrane protein from normal human erythrocytes that inhibits reactive lysis of the erythrocytes of paroxysmal nocturnal hemoglobinuria. J Clin Invest 34: 7–17
Hollander H, Shin ML, Rosse WF, Springer TA (1989) Distinct restriction of complement- and cell-mediated lysis. J Immunol 142: 3913–3916
Hu VW, Nicholson-Weller A (1985) Enhanced complement-mediated lysis of type III paroxysmal nocturnal hemoglobinuria erythrocytes involves increased C9 binding and polymerization. Proc Natl Acad Sci USA 82: 5520–5524
Jiang S, Persechini PM, Zychlinsky A, Chau-Ching L, Perussia B, Young JD-E (1988) Resistance of cytolytic lymphocytes to perforin-mediated killing-lack of correlation with complement- associated homologous species restriction. J Exp Med 168: 2207–2219
Jung G, Honsik CJ, Reisfeld RA, Müller-Eberhard HJ (1986) Activation of human peripheral blood mononuclear cells by anti-T3: killing of tumor target cells coated with anti-target-T3 conjugates. Proc Natl Acad Sci USA 83: 4479–4483
Jung G, Martin DE, Müller-Eberhard HJ (1987) Induction of cytotoxicity in human peripheral blood mononuclear cells by monoclonal antibody OKT3. J Immunol 139: 639–644
Krähenbühl OP, Peter HH, Tschopp J (1989) Absence of homologous restriction factor does not affect CTL-mediated cytolysis. Eur J Immunol 19: 217–219
Lachmann PJ, Thompson RA (1970) Reactive lysis: the complement lysis of unsensitized cells II: the characterization of activated reactor as C56 and the participation of C8 and C9. J Exp Med 131: 643–657
Lichtenheld MG, Olsen KP, Lu P, Lowry D, Hameed A, Hengartner H, Podack ER (1988) Structure and function of human perforin. Nature 335: 448–551
Martin DE, Zalman LS, Müller-Eberhard HJ (1988) Induction of expression of cell-surface homologous restriction factor upon anti-CD3 stimulation of human peripheral lymphocytes. Proc Natl Acad Sci USA 85: 213–217
Medof ME, Walter El, Rutgers JL, Knowles DM, Nussenzweig V (1987) Identification of the complement decay-accelerating factor (DAF) on epithelium and glandular cells and in body fluids. J Exp Med 165: 848–864
Nicholson-Weller A, Burger J, Fearon DT, Weller PF, Austen KF (1982) Isolation of human erythrocyte membrane glycoprotein with decay-accelerating activity for C3-convertases of the complement system. J Immunol 129: 184–189
Nicholson-Weller A, March JP, Rosenfeld SI, Austen KF (1983) Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay-accelerating factor. Proc Natl Acad Sci USA 80: 5066–5070
Okada N, Harada R, Fujita T, Okada H (1989) A novel membrane glycoprotein capable of inhibiting membrane attack by homologous complement. Int Immunol 1: 205–208
Packman CH, Rosenfeld SI, Jenkins DE, Thiem PA, Leddy JP (1979) Complement lysis of human erythrocytes. Differing susceptibility of two types of paroxysmal nocturnal hemoglobinuria cells to C5b-9. J Clin Invest 64: 428–433
Pangburn MK, Schreiber RD, Müller-Eberhard HJ (1983a) Deficiency of an erythrocyte membrane protein with complement regulatory activity in paroxysmal nocturnal hemoglobinuria. Proc Natl Acad Sci USA 80: 5430–5434
Pangburn MK, Schrieber RD, Trombold JS, Müller-Eberhard HJ (1983b) Paroxysmal nocturnal hemoglobinuria: deficiency in factor H-like functions of the abnormal erythrocytes. J Exp Med 57: 1971
Podack ER, Preissner KT, Müller-Eberhard HJ (1984) Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein. Acta Pathol Microbiol Immunol Scand [C] 284: 89–96
Rosenfeld SI, Jenkins DE, Leddy SP (1985) Enhanced reactive lysis of paroxysmal nocturnal hemoglobinuria erythrocytes by C5b-9 does not involve increased C7 binding on cell-bound C3b. J Immunol 134: 506–511
Rosse WF (1973) Variations in the red cells in paroxysmal nocturnal hemoglobinuria. Br J Hematol 24: 327–342
Schönermark S, Rauterberg EW, Shin ML, Löke S, Roelcke D, Hänsch GM (1986) Homologous species restriction in lysis of human erythrocytes: a membrane-derived protein with C8-binding capacity functions as an inhibitor. J Immunol 136: 1772–1776
Schönermark S, Felsinger S, Berger B, Hänsch GM (1988) The C8-binding protein of human erythrocytes: interaction with the components of the complement-attack phase. Immunology 63: 585–590
Shin ML, Hänsch G, Hu VW, Nicholson-Weller A (1986) Membrane factors responsible for homologous species restriction of complement-mediated lysis: evidence for a factor other than DAF operating at the stage of C8 and C9. J Immunol 136: 1777–1782
Sugita Y, Nakano Y, Tomita M (1988) Isolation from human erythrocytes of a new transmembrane protein which inhibits the formation of complement transmembrane channels. J Biochem 104: 633–637
Watts MJ, Dankert JR, Morgan BP (1990) Isolation and characterization of a membrane-attack- complex-inhibiting protein present in human serum and other biological fluids. Biochem J 265: 471–477
Weiss A, Imboden J, Hardy K, Manger B, Terhorst C, Stobo J (1986) The role of the T3/antigen receptor complex in T-cell activation. Annu Rev Immunol 4: 593
Yamamoto K-I (1977) Lytic activity of C5–9 complexes for erythrocytes from the species other than sheep: C9 rather than C8-dependent variation in lytic activity. J Immunol 119: 1482–1485
Zalman LS, Wood LM, Müller-Eberhard HJ (1986a) Isolation of a human erythrocyte membrane protein capable of inhibiting expression of homologous complement transmembrane channels. Proc Natl Acad Sci USA 83: 6975–6979
Zalman LS, Brothers MA, Chui FJ, Müller-Eberhard HJ (1986b) Mechanism of cytotoxicity of human large granular lymphocytes: relationship of the cytotoxic lymphocyte protein to C8 and C9 of human complement. Proc Natl Acad Sci USA 83: 5262–5266
Zalman LS, Wood LM, Frank MM, Müller-Eberhard HJ (1987a) Deficiency of the homologous restriction factor in paroxysmal nocturnal hemoglobinuria. J Exp Med 165: 572–577
Zalman LS, Wood LM, Müller-Eberhard HJ (1987b) Inhibition of antibody-dependent lymphocyte cytotoxicity by homologous restriction factor incorporated into target cell membranes. J Exp Med 166: 947–955
Zalman LS, Brothers MA, Müller-Eberhard HJ (1988) Self-protection of cytotoxic lymphocytes: a soluble form of homologous restriction factor in cytoplasmic granules. Proc Natl Acad Sci USA 85: 4827–4831
Zalman LS, Brothers MA, Müller-Eberhard HJ (1989) Isolation of homologous restriction factor from human urine—immunochemical properties and biologic activities. J Immunol 154: 1943–1947
Zalman LS, Brothers MA, Strauss KL (1991) Inhibition of cytolytic lymphocytes by homologous restriction factor—lack of species restriction. J Immunol 146: 4278–4281
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© 1992 Springer-Verlag Berlin Heidelberg
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Zalman, L.S. (1992). Homologous Restriction Factor. In: Parker, C.J. (eds) Membrane Defenses Against Attack by Complement and Perforins. Current Topics in Microbiology and Immunology, vol 178. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77014-2_6
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DOI: https://doi.org/10.1007/978-3-642-77014-2_6
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