Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera

Arthritis and Rheumatism
Theophany EystathioyEdward K L Chan

Abstract

To characterize the 15-kd human SmD-like autoantigen and its associated proteins previously shown to be recognized by IgM antibodies in patients with Epstein-Barr virus (EBV)-induced infectious mononucleosis. The full-length complementary DNA for the 15-kd protein was expressed as recombinant protein and analyzed for reactivity using biochemical analysis and immunoprecipitation (IP). The 15-kd protein was determined to be the human like-Sm protein LSm4 (hLSm4). Rabbit antibody raised against the C-terminal polypeptide immunoprecipitated a 68-kd complex composed of LSm4 together with a group of smaller proteins ranging in size from 6.5 to 14 kd, consistent with the reported heptameric LSm complexes involved in U4/U6 duplex formation and messenger RNA (mRNA) decapping/degradation. About 80% of all anti-Sm sera from patients with systemic lupus erythematosus (SLE) recognized the hLSm4 in vitro translated product, while 6.7% (29 of 434) immunoprecipitated from cell extracts hLSm4 together with the other members of the hLSm complex. Four sera (0.92%) showed apparently exclusive reactivity to the hLSm complex in the absence of reactivity to Sm core proteins in the IP assay. These findings document that while IgM, but not IgG, autoant...Continue Reading

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Citations

Feb 14, 2004·Clinical Immunology : the Official Journal of the Clinical Immunology Society·Laura M StintonMarvin J Fritzler
Nov 15, 2005·Nature Cell Biology·Andrew JakymiwEdward K L Chan
Jun 29, 2007·Molecular Biology of the Cell·Shangli LianEdward K L Chan
Mar 26, 2008·Biochemical and Biophysical Research Communications·Tadanori YamochiChikao Morimoto
Feb 16, 2005·The Journal of Biological Chemistry·Bozidarka ZaricChristian Kambach
Aug 1, 2007·Journal of Neuroscience Research·Joanna J MoserMarvin J Fritzler

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