Complement activation by female protein, the hamster homologue of human C-reactive protein.

Abstract

The capacity of Syrian hamster female protein (FP), a phosphorylcholine (PC)-binding pentraxin, to activate complement was tested in an in vitro system consisting of PC-coupled sheep red blood cells and guinea pig serum as the complement (C) source. FP was demonstrated to fix complement as reflected by hemolysis. Such hemolysis was eliminated by heat treatment (56 degrees C, 30 min) of guinea pig serum and inhibited by PC chloride but not dinitrophenyl lysine. The inability of C4-deficient guinea pig serum to provide lytic activity indicated that lysis proceeded through the classical hemolytic pathway.

• Authors: H M Etlinger, J E Coe
• Journal: International archives of allergy and applied immunology (Int Arch Allergy Appl Immunol) Vol. 81 Issue 2 Pg. 189-91 ( 1986) ISSN: 0020-5915 [Print] Switzerland
• PMID: 2428756 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Acute-Phase Proteins
• Alpha-Globulins
• female protein, hamster
• Phosphorylcholine
• C-Reactive Protein

Topics

• Acute-Phase Proteins (immunology)
• Alpha-Globulins (immunology)
• Animals
• C-Reactive Protein (immunology)
• Complement Activation
• Complement Pathway, Classical
• Cricetinae
• Phosphorylcholine (metabolism)
• Protein Binding
• Structure-Activity Relationship