Immunochemical aberrations of alpha2-macroglobulin purified from a patient with multiple sclerosis.
We report on a patient with primary progressive multiple sclerosis who was found to present alpha2-macroglobulin with aberrant immunochemical properties. alpha2-macroglobulin was purified from plasma and investigated in ELISA using highly conformation specific monoclonal antibodies. The purified alpha2-macroglobulin displayed reactivity with antibodies specific for binding to native alpha2-macroglobulin as well as with antibodies specific for binding to transformed alpha2-macroglobulin. Furthermore, following methylamine treatment, alpha2-macroglobulin from the multiple sclerosis patient presented a reduced shift in antibody reactivity from the native-specific to the transformed-specific antibodies, as compared to normal alpha2-macroglobulin. In conclusion, the results suggest that alpha2-macroglobulin from this multiple sclerosis patient presents conformational aberrations, which may have implications on the capacity to eliminate proteinases from the systemic circulation.
Gunnarsson
M
M
Department of Immunology, Umeå University, Sweden.
Stigbrand
T
T
Jensen
P E
PE
D000328:Adult; D000911:Antibodies, Monoclonal; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007120:Immunochemistry; D008297:Male; D008744:Methylamines / Q000627:therapeutic use; D009103:Multiple Sclerosis / Q000276:immunology* / Q000503:physiopathology; D011487:Protein Conformation; D000511:alpha-Macroglobulins / Q000737:chemistry* / Q000276:immunology
D000911:Antibodies, Monoclonal; D008744:Methylamines; D000511:alpha-Macroglobulins; C027451:methylamine