Extended reports
Serum samples of patients with rheumatoid arthritis contain a
specific autoantibody to "denatured" aldolase A in the
osteoblast-like cell line, MG-63
a Department of
Laboratory and Molecular Medicine, Kagoshima University, School of
Medicine, Kagoshima, Japan, b Tsukuba Research Laboratories, Tokuyama
Corporation, Tsukuba, Japan, c Department of Orthopaedic Surgery, Kyoto
Prefectural University of Medicine, Kyoto, Japan, d Institute
of Applied Biochemistry, University of Tsukuba, Tsukuba, Japan
Correspondence to: Dr I Kitajima, Department of Laboratory and Molecular Medicine, Faculty of Medicine, Kagoshima University, 8-35-1 Sakuragaoka, Kagoshima City, Kagoshima 890-8520, Japan.
Accepted for publication 23 December 1998
OBJECTIVE
To identify
rheumatoid arthritis (RA) specific autoantibody and its antigen in the
human osteoblast-like cell line, MG-63.
METHODS
MG-63 cell
extract was subjected to western blotting by using RA and normal serum
samples as probes. The autoantigen was purified and its N-terminal
sequence was determined by automated Edman degradation. The reactivity
of denatured aldolase A was evaluated by immunoblotting. Screening by
enzyme linked immunosorbent assay (ELISA) using the autoantibody was performed.
RESULTS
40 kDa protein
was found only in the RA serum samples and it was identified as
aldolase A. A polyclonal antibody for rabbit muscle aldolase A bound to
the 40 kDa protein and reacted in preference with the denatured enzyme.
Using ELISA for denatured rabbit aldolase A, the autoantibody was found
in approximately 10% of RA patients, whereas it was not found in the
other arthropathy and healthy adults.
CONCLUSION
This 40 kDa
anti-aldolase A autoantibody, which was identified only in serum
samples of RA patients with severe bone erosion, could be related to a
certain event that induces RA specific joint destructions.
© 1999 by Annals of the Rheumatic Diseases
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