Complement pp 49-72 | Cite as

The β-Cys-γ-Glu Thiolester Bond in Human C3, C4, and α2-Macroglobulin

  • Brian F. Tack

Abstract

The third and fourth components of complement, C3 and C4, are integral components of the complement system and play a significant role in host resistance to infection. Two primary pathways of activation are known, the classical and alternative, which are each subject to a variety of intrinsic and extrinsic controls. Both pathways proceed initially by the sequential self-assembly of multimacromolecular enzyme complexes. C4 consists of three polypeptide chains, α, β, and γ, with respective molecular weights of 94 000, 70 000, and 32 000. Cleavage of C4 by the classical pathway enzyme, \(Cl\bar s\), results in the formation of two fragments, a vasoactive peptide (C4a) and a macromolecular fragment (C4b), having an α′βγ chain structure. A bimolecular complex \((C\overline {4b2a} )\) constitutes the C3 cleaving enzyme. In contrast to C4, C3 is an active participant in both pathways of activation. C3 consists of two polypeptide chains, α and β, with respective molecular weights of 115 000 and 75 000. Cleavage of C3 by the classical pathway convertase \((C\overline {4b2a} )\) also results in the formation of two fragments. Again, a vasoactive peptide (C3a) is removed from the amino end of the α-chain leaving a disulfide-bridged protein (C3b), having an α′β chain structure. A bimolecular complex of activated forms of C3 and Factor B \((C\overline {3bBb} )\) further functions in the alternative pathway as a C3 convertase, thereby providing a positive feedback amplification mechanism for further C3 consumption [for reviews see 46, 52, 54, 64, 68].

Keywords

Glycerol Cysteine Histidine Plasminogen Transesterification 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1985

Authors and Affiliations

  • Brian F. Tack
    • 1
  1. 1.Department of ImmunologyResearch Institute of Scripps ClinicLa JollaUSA

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