Surprisingly high levels of anaphylatoxin C5a des Arg are extractable from psoriatic scales.
Water-soluble extracts from psoriatic scales and normal human skin were prepared using either phosphate-buffered saline, pH 7.2, or 0.1 M carbonate buffer, pH 10.8. Anaphylatoxin C5a des Arg was quantified using a novel sandwich enzyme-linked immunosorbent assay (ELISA) using neoepitope-specific monoclonal antibodies. Alkali was about five to eight times more efficient than PBS in extracting C5a des Arg from scales, probably via dissociation of bound C5a des Arg. C5a des Arg concentration in scales from three patients suffering from psoriasis vulgaris varied between 2.5 and 4.6 ng/mg scale. No C5a des Arg was detectable in normal skin extracts. The biological activity of alkali-extractable C5a des Arg, i.e. chemotaxis, was preserved. The concentration of C5a des Arg relative to the concentration of albumin was taken as a parameter of the degree of complement activation in the psoriatic lesions, and was found to be more than six times higher than values attained in serum after maximum complement activation by zymosan. We conclude that complement activation may play a quantitatively important role in the inflammatory process in psoriasis.
Department of Microbiology, University Hospital, Norway.
K
K
Bergh
O J
OJ
Iversen
H
H
Lysvand
D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D003167:Complement Activation; D015937:Complement C5a, des-Arginine / Q000276:immunology / Q000302:isolation & purification*; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D011565:Psoriasis / Q000276:immunology / Q000378:metabolism*; D012680:Sensitivity and Specificity
D000911:Antibodies, Monoclonal; D015937:Complement C5a, des-Arginine