title: [Biochemical data on C1 intrinsic activation (author's transl)].
abstract: C1 activation can be triggered by immune complexes and various effectors such as extrinsic proteases, bacterial or viral membranes, polyanions and polysaccharides. The basic mechanism of activation involves a limited proteolytic cleavage of C1r, with the generation of a proteolytic activity. Highly purified proenzymic C1r was obtained in high yield from human plasma by an indirect affinity chromatography step. Activation of isolated C1r in a fluid phase proceeded according to two distinct coexisting mechanisms: 1) an autocatalytic intradimer activation mediated by the pro-site of non-activated C1r; 2) an autocatalytic interdimer proteolysis triggered by nascent activated C1r formed in the course of the first reaction. DFP and C1-inhibitor did not have any effect on the first mechanism but were able to block the second mechanism. C1 activation is discussed in the light of recent results obtained by others from electron microscopy, and a tentative model is proposed.
mesh_terms: D000936:Antigen-Antibody Complex; D001667:Binding, Competitive; D003166:Complement Activating Enzymes / Q000378:metabolism; D003167:Complement Activation; D003172:Complement C1 / Q000276:immunology*; D003174:Complement C1 Inactivator Proteins / Q000378:metabolism; D015923:Complement C1r; D006801:Humans; D007531:Isoflurophate / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology
chemical_list: D000936:Antigen-Antibody Complex; D003172:Complement C1; D003174:Complement C1 Inactivator Proteins; D007531:Isoflurophate; D003166:Complement Activating Enzymes; D010447:Peptide Hydrolases; D015923:Complement C1r
vernacular_title: Aspects biochimiques de l'activation intrinsèque de C1.