concanavalin-a and Arthritis--Psoriatic

Changes of glycosylation of serum proteins of patients with psoriatic arthritis were detected by lectin blotting and a new enzyme-linked lectin assay (ELLA) using concanavalin A (Con A). A good linear correlation was found between the total Con A-reactivity of serum and the serum levels of C-reactive protein and interleukin-6, which is known to regulate the glycosylation pattern of proteins upon inflammation. A good linear correlation was also observed between the immunoreactivity of alpha 1-antitrypsin, measured by ELISA, using a monoclonal antibody sensitive to glycosylation changes, and the erythrocyte sedimentation rate and the serum concentrations of soluble interleukin-2 receptor, an index of lymphocyte activation which correlated with some inflammatory parameters of disease activity. These protein changes, which are described here for the first time, deserve to be studied in further detail in view of their possible clinical applications.

Topics: Acute-Phase Proteins; Adult; Aged; Arthritis, Psoriatic; Blood Proteins; Centrifugation; Concanavalin A; Enzyme-Linked Immunosorbent Assay; Female; Glycosylation; Humans; Interleukin-6; Male; Middle Aged; Receptors, Interleukin-2; Regression Analysis; Sensitivity and Specificity; Solubility