Monoclonal Antibody Against the Lupus Antigen Sm Cross-Reacts with RNA Polymerase I
作者:
AndPhillip Morris,
StetlerDean A.,
期刊:
Autoimmunity
(Taylor Available online 1989)
卷期:
Volume 2,
issue 3
页码: 241-251
ISSN:0891-6934
年代: 1989
DOI:10.3109/08916938909014688
出版商: Taylor&Francis
关键词: anti-Sm antibody;rheumatic disease antigens;systemic lupus erythematosus
数据来源: Taylor
摘要:
Monoclonal anti-Sm antibody, a specificity directed against a constituent of nuclear ribonucleoprotein and considered to be a marker for systemic lupus erythematosus (SLE), was tested for its ability to react with four other rheumatic disease antigens of known enzymatic activity. No binding of the antibody was observed in radioimmunoassays with immobilized protein kinase Nil, po!y(A) polymerase, or topoiso-merase I. In contrast, anti-Sm antibody did react with RNA polymerase I. Under conditions of antibody excess, anti-Sm was determined to bind RNA polymerase I on an equimolar basis, indicating that the polymerase posesses a single epitope recognized by the anti-Sm antibody. Addition of the anti-Sm antibody toin vitrotranscription reactions resulted in inhibition of RNA polymerase I activity but had no effect on the reaction catalyzed by RNA polymerase II. When the subunits of RNA polymerase I were separated by polyacrylamide gel electrophoresis under denaturing conditions and incorporated individually into the radioimmunoassay. anti-Sm antibody bound only to the sixth polymerase polypeptide (Mr, 21,000). These data establish an immunological relationship between two important rheumatic disease antigens and help explain the apparent diversity of the autoimmune response in murine and human SLE.
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