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Introduction

  • Franco Celada
  • Verne N. Schumaker
  • Eli E. Sercarz

Abstract

In order to understand at the molecular level how the immunological signal, generated upon interaction of antibody with antigen, can result in the cleavage of a peptide chain in C1r and, thereby, initiate the proteolytic cascade among the early complement components of the classical pathway, it is essential to know how C1 is assembled from its subunits, that is, how the quaternary structure of the complex is formed, and what is the value of the association constant for the interaction between C1q and C1r2C1s2. Moreover, as part of understanding how different immune complexes activate the classical pathway, it is important to know how tightly the binding sites located on the C1q heads interact with immunoglobulins of different classes and subclasses, and with immunoglobulin aggregates of different sizes. Finally, it appears that a number of fibrous macromolecules, notably fibronectin and heparin, can compete for the site on C1q to which the C1r2C1s2 tetramer binds, and it seems probable that similar interactions between C1q and fibrous macromolecules play a role in the immune defense.

Keywords

Immune Defense Classical Pathway Relay System Cyanogen Bromide Proteolytic Cascade 
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.

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • Franco Celada
    • 1
  • Verne N. Schumaker
    • 2
  • Eli E. Sercarz
    • 2
  1. 1.University of GenoaGenoaItaly
  2. 2.University of CaliforniaLos AngelesUSA

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