Literature DB >> 2472922

Activation-dependent antigenic changes of human C3.

P Garred1, T E Mollnes, M D Kazatchkine.   

Abstract

The C3 molecule is crucial in the function of the complement system. It is the only substrate for both the classical and the alternative pathways. Native C3 exhibits no biological activity. Upon activation, biologically active C3 fragments are formed, on which new antigenic determinants appear. Activated C3 express distinct binding sites for other complement proteins and cell surface receptors. Recently, it has been possible to study these neoepitopes with monoclonal antibodies. These antibodies are also found valuable in the detection and quantitation of C3 activation products and C3-containing circulating immune complexes.

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Year:  1989        PMID: 2472922     DOI: 10.1159/000463094

Source DB:  PubMed          Journal:  Complement Inflamm        ISSN: 1012-8204


  2 in total

1.  Herpes simplex virus glycoprotein C: molecular mimicry of complement regulatory proteins by a viral protein.

Authors:  H P Huemer; Y Wang; P Garred; V Koistinen; S Oppermann
Journal:  Immunology       Date:  1993-08       Impact factor: 7.397

2.  Comparative study of in vitro inhibition of activation of the classical and alternative pathways of human complement by the magnesium and sodium salts of the anti-inflammatory peptide N-acetyl-aspartyl-glutamic acid (NAAGA).

Authors:  J Feuillard; F Maillet; P Goldschmidt; L Weiss; M D Kazatchkine
Journal:  Agents Actions       Date:  1991-03
  2 in total

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