Results 211 to 220 of about 11,877 (255)
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Genetic Aspects of Complement Component C8 in Norwegian Meningococcal Disease Patients
Scandinavian Journal of Infectious Diseases, 1990Sera from 85 consecutive systemic meningococcal disease patients and 203 matched control individuals were C8 typed. In the patient group, one C8B deficient individual was discovered; none in the control group. No case of C8A deficiency was encountered. The material was collected during a period of epidemic meningococcal disease in Norway, mainly due to
S, Rogde +3 more
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Human complement protein C8 gamma.
Biochimica et biophysica acta, 2000Human C8 gamma is a 22 kDa subunit of complement component C8, which is one of five components (C5b, C6, C7, C8, C9) that interact to form the cytolytic membrane attack complex (MAC) of complement. C8 contains three nonidentical subunits (alpha, beta, gamma) that are products of different genes.
S F, Schreck +3 more
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Blocking Complement-Mediated Hemolysis Using RNA Aptamers That Bind Complement Component C8.
Blood, 2005Abstract A recent pilot study in patients with paroxysmal nocturnal hemoglobinuria (PNH), using a humanized monoclonal antibody that binds human complement C5 and inhibits terminal complement protein activation, suggests that blocking complement is a potentially effective therapeutic option for PNH.
Jun-ichi Nishimura +10 more
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Structure and Function of C8 in the Membrane Attack Sequence of Complement
1988Complement-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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Human complement C81 (C8 A) polymorphism: detection and segregation of new variants
Human Genetics, 1993In addition to the earlier detected C81(A) rare variants A1, A2 (now A3) and B1 (now B2), six new rare variants (C81 A2 new, A4, A5, A6, M1 and B1new) are described within the polymorphism of the eighth component of human complement (alpha-gamma chain subunit). Except for A3, all rare C81 A variants are only detected by isoelectric focusing, and not by
C, Rittner, B, Stradmann-Bellinghausen
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Homologous restriction factor: Effect on complement C8 and C9 uptake and lysis
Molecular Immunology, 1994Homologous restriction factor (HRF) is a complementary regulatory protein found on the surface of human erythrocytes and other cell types. It has the function of blocking the lytic action of the membrane attack complex (MAC) of complement when incorporated into a membrane.
L S, Zalman, H, Müller-Eberhard
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Genetic Polymorphisms and Linkage Relations of Complement Factor C8
1985Abstract Genetically determined variation in both the C8α-chain (C81) and β-chain (C82) is detected by isoelectric focusing and imnunoblotting, supplemented by two dimensional electrophoresis. The C81 and C82 loci are closely linked. Both C8 loci are linked to the chromosome 1 marker loci PGM1 and Rh .
S. ROGDE +4 more
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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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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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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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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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Complementary DNA cloning of complement C8.beta. and its sequence homology to C9
Biochemistry, 1987The complete amino acid sequence of mature C8 beta has been derived from the DNA sequence of a cDNA clone identified by expression screening of a human liver cDNA library. Comparison with the amino acid sequence of C9 shows an overall homology with few deletions and insertions.
Haefliger JA +6 more
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