The C8-binding protein of human erythrocytes: interaction with the components of the complement-attack phase.

Immunology ·Vol. 63 ·No. 4 ·1988-04-00 ·Pages 585-90

Schönermark S, Filsinger S, Berger B, Hänsch GM

Abstract

C8-binding protein is an intrinsic membrane protein of the human erythrocyte. It inhibits the complement (C5b-9)-mediated lysis in a species-restricting manner. In the present study we incorporated C8bp, isolated from human erythrocytes, into sheep erythrocytes (SRBC). SRBC, normally sensitive to lysis by human C5b-9, became insensitive to lysis. Furthermore, we found that C8bp is incorporated into the membrane-attack complex C5b-9, most probably by interacting with C8, since C8bp has an affinity for C8, particularly for the C8 alpha-gamma-subunit. Antibodies to C8bp react with the C8 alpha-subunits and with C9, pointing to the possibility of a partial homology between these proteins.

MeSH Terms

Animals Blood Proteins/immunology,metabolism CD59 Antigens Carrier Proteins Cell Membrane/metabolism Complement C8/metabolism Complement Membrane Attack Complex Complement System Proteins/immunology,metabolism Cross Reactions Electrophoresis, Polyacrylamide Gel Erythrocytes/immunology Hemolysis Humans

Chemicals

Blood Proteins CD59 Antigens Carrier Proteins Complement C8 Complement Membrane Attack Complex CD59 protein, human Complement System Proteins

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Schönermark S

Institut für Immunologie, Universität Heidelberg, FRG.

Filsinger S

Berger B

Hänsch G M

References (22)

22 references, click to expand

Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
Paroxysmal nocturnal hemoglobinuria type III. Lack of an erythrocyte membrane protein restricting the lysis by C5b-9.
J Clin Invest. 1987 Jul;80(1):7-12 PMID: 3597779
Molecular analysis of the reaction of C9 with EAC1-8: reaction of C9 with EAC1-8.
J Immunol. 1974 Dec;113(6):1992-2003 PMID: 4214868
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. 1977 Oct;119(4):1482-5 PMID: 894048
Isolation of late complement components by affinity chromatography: I. Purification of the human complement component C9 and production of a C9-defective human serum.
Z Immunitatsforsch Immunobiol. 1979 Jun;155(5):365-77 PMID: 112795
Binding of the eighth component of human complement to the soluble cytolytic complex is mediated by its beta subunit.
J Biol Chem. 1980 Nov 25;255(22):10579-82 PMID: 7430137
The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure.
J Biol Chem. 1980 Dec 25;255(24):11997-2005 PMID: 7440581
Homologous species restriction in lysis of erythrocytes by terminal complement proteins.
Proc Natl Acad Sci U S A. 1981 Aug;78(8):5118-21 PMID: 6946459
Isolation of a human erythrocyte membrane glycoprotein with decay-accelerating activity for C3 convertases of the complement system.
J Immunol. 1982 Jul;129(1):184-9 PMID: 6211481
Circular polymerization of the ninth component of complement. Ring closure of the tubular complex confers resistance to detergent dissociation and to proteolytic degradation.
J Biol Chem. 1982 Dec 25;257(24):15204-12 PMID: 7174692
Evidence of direct insertion of terminal complement proteins into cell membrane bilayers during cytolysis. Labeling by a photosensitive membrane probe reveals a major role for the eighth and ninth components.
J Biol Chem. 1983 Apr 10;258(7):4318-24 PMID: 6833260
Paroxysmal nocturnal hemoglobinuria: deficiency in factor H-like functions of the abnormal erythrocytes.
J Exp Med. 1983 Jun 1;157(6):1971-80 PMID: 6222136
Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor.
Proc Natl Acad Sci U S A. 1983 Aug;80(16):5066-70 PMID: 6576376
Membrane attack by complement.
Mol Immunol. 1984 Jul;21(7):589-603 PMID: 6379417
Species-restricted target cell lysis by human complement: complement-lysed erythrocytes from heterologous and homologous species differ in their ratio of bound to inserted C9.
J Immunol. 1984 Oct;133(4):2133-7 PMID: 6470486
Inhibition of complement activation on the surface of cells after incorporation of decay-accelerating factor (DAF) into their membranes.
J Exp Med. 1984 Nov 1;160(5):1558-78 PMID: 6238120
The control of complement activation by the blood cells in paroxysmal nocturnal hemoglobinuria.
Blood. 1986 Feb;67(2):268-9 PMID: 2417643
Homologous species restriction in lysis of human erythrocytes: a membrane-derived protein with C8-binding capacity functions as an inhibitor.
J Immunol. 1986 Mar 1;136(5):1772-6 PMID: 2419413
Isolation of a human erythrocyte membrane protein capable of inhibiting expression of homologous complement transmembrane channels.
Proc Natl Acad Sci U S A. 1986 Sep;83(18):6975-9 PMID: 2428045
Deficiency of the homologous restriction factor in paroxysmal nocturnal hemoglobinuria.
J Exp Med. 1987 Feb 1;165(2):572-7 PMID: 2434597
[Recurrent meningitis in familial deficiency of the 8th component of the complement system].
Klin Wochenschr. 1987 Apr 15;65(8):387-90 PMID: 3586574
Studies on the terminal stages of complement lysis.
Immunology. 1973 Jan;24(1):135-45 PMID: 4346598

Article Info

Journal

Immunology

Abbr.

Immunology

ISSN

0019-2805

Published

1988-04-00

Pages

585-90

Language

English

Region

England

NLM ID

0374672

PMCID

PMC1454802

Subset

External Links

PubMed source PMC Full Text View journal details

Analysis Services

The C8-binding protein of human erythrocytes: interaction with the components of the complement-attack phase.

Contact

WeChat Official Account