PubMed · 10635767
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S Takemura. 1999. [Hemolytic complement activity via classical pathway].. https://pubmed.ncbi.nlm.nih.gov/10635767/
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Apart from their antigen-recognising function, immunoglobulins have other physicochemical properties. The best described is cryoprecipitation of monoclonal and/or polyclonal immunoglobulins. The cryoprecipitation phenomenon is unique for each cryoglobulin, and depends on the intrinsic properties of the monoclonal immunoglobulin, the protein environment, temperature and the surrounding ionic concentrations. The complement activating properties of monoclonal immunoglobulins are also unique. We have described a series of monoclonal immunoglobulins which are able to activate the classical pathway of complement without the formation of antigen/antibody complexes. Analysis of the properties of these monoclonal immunoglobulins suggests new therapeutic strategies in oncology. Monoclonal chimeric antibodies, combining antibody specific against tumour antigens and strong complement activation, may be more damaging to tumor cells than currently used antibodies.
This paper describes the creation of a three-dimensional animation showing the classical pathway of the complement cascade, made in Studio Strata Pro Blitz (v1.75+) on the Macintosh computer. An analysis of two dimensional depictions of the process from the chapters of current textbooks of immunology revealed inconsistencies; animation was used to demonstrate how these difficulties can be overcome.
Pseudomonas aeruginosa lipopolysaccharide (LPS) plays a key role in pathogenesis. In acute infections, a smooth LPS protects the organism from complement-mediated killing and, during chronic lung infections, an altered rough LPS helps the organism evade host defense mechanisms.