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Role of the human C8 subunits in complement-mediated bacterial killing: evidence that C8γ is not essential

Molecular Immunology, 2002
Human C8 is one of five complement components (C5b, C6, C7, C8 and C9) that interact to form the cytolytic membrane attack complex (MAC) on bacterial cell membranes. It is an oligomeric protein composed of a disulfide-linked C8 alpha-gamma heterodimer and a non-covalently associated C8 beta chain.
Chasta L, Parker, James M, Sodetz
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Sequence homology of complement C8γ chain with α1-microglobulin and its implications for C8 structure and function

Molecular Immunology, 1988
Complement C8 gamma is a disulphide bonded subunit of C8 with no known homology or function. We show here that it strongly resembles alpha 1-microglobulin and protein HC in both length and sequence suggesting a common genetic origin. By extrapolation from the alpha 1-microglobulin family we are able to suggest that the cysteine residue of C8 gamma is ...
J P, Luzio, K K, Stanley
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Expression and characterization of recombinant subunits of human complement component C8: further analysis of the function of C8 alpha and C8 gamma.

Journal of immunology (Baltimore, Md. : 1950), 1998
Human C8 is composed of three nonidentical subunits (C8 alpha, C8 beta, and C8 gamma) that are encoded in separate genes. In C8 isolated from serum, these are arranged as a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta.
S F, Schreck   +6 more
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Biotinylation: a simple method for labelling complement component C8 with preservation of functional activity

Journal of Immunological Methods, 1989
Biotinylation of human C8 with the water-soluble biotin derivative biotinylamidohexanoic acid, N-hydroxysulfosuccinimide ester is an excellent method for labelling this terminal complement component with preservation of its functional activity. The biotinylated product can be detected both in native form and also following its incorporation into the ...
S, Bhakdi, M, Roth, F, Hugo
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[Further study on heterogeneic basis of complement C8 beta deficiency].

Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics, 2004
In Caucasian population, the most common molecular basis for C8 beta deficiency s a single C to T transition in exon 9 of C8 beta gene resulting in a stop codon. In previous family studies, two individuals were identified with C8 beta complete deficiency and were found to be only heterozygous for this mutation.
Li, Rao   +5 more
openaire   +1 more source

Genomic organization of human complement protein C8 alpha and further examination of its linkage to C8 beta.

Human genetics, 1995
Human C8 is one of five complement components (C5b, C6, C7, C8, C9) that interact to form the cytolytic C5b-9 complex on target membranes. It is composed of three nonidentical subunits (C8 alpha, C8 beta, C8 gamma) encoded by separate genes. C8 alpha and C8 beta are linked on chromosome 1p32, whereas C8 gamma is located on 9q22.3-q32.
G A, Michelotti   +2 more
openaire   +1 more source

4.2. Genetic polymorphism of complement component C8

Forensic Science International, 1983
B. Mevåg   +4 more
openaire   +1 more source

Structure and Function of C8 in the Membrane Attack Sequence of Complement

1988
Complement-mediated cell lysis occurs as a result of interactions between complement proteins C5b, C6, C7, C8, and C9 to produce the membrane attack complex C5b-9 (Muller-Eberhard 1986): $$ C5b\;\xrightarrow{{C6}}\;C5b - 6\;\xrightarrow{{C7}}\;C5b - 7\xrightarrow{{C8}}\;C5b - 8\;\xrightarrow{{nC9}}\;C5b - 9 $$ Assembly of C5b-9 begins with ...
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The state of complement in COVID-19

Nature Reviews Immunology, 2021
Behdad Afzali   +2 more
exaly  

Complement Protein C8

2005
Lukasz Lebioda, James M. Sodetz
openaire   +1 more source

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