Multiple phosphorylation of human SS-B/La autoantigen and its effect on poly(U) 
and autoantibody binding

Pfeifle, J; Anderer, FA; Franke, M

doi:10.1016/0167-4889(87)90124-8

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Multiple phosphorylation of human SS-B/La autoantigen and its effect on poly(U) and autoantibody binding

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Pfeifle, J
Anderer Group, Friedrich Miescher Laboratory, Max Planck Society;

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Anderer, FA
Anderer Group, Friedrich Miescher Laboratory, Max Planck Society;

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Citation

Pfeifle, J., Anderer, F., & Franke, M. (1987). Multiple phosphorylation of human SS-B/La autoantigen and its effect on poly(U) and autoantibody binding. Biochimica et Biophysica Acta: Molecular Cell Research, 928(2), 217-226. doi:10.1016/0167-4889(87)90124-8.

Cite as: https://hdl.handle.net/21.11116/0000-000F-4324-D

Abstract

The metabolic turnover rates and the effect of in vitro phosphorylation on poly(U) and autoantibody binding of human SS-B/La ribonucleoprotein, an autoantigen expressed in various autoimmune disorders, were studied. The determination of the metabolic turnover rates of SS-B/La protein, SS-B/La protein phosphorylation and RNA binding yielded values of 12.1 h, 3.6 h and 3.7 h, respectively, indicating a possible functional correlation of RNA-binding and phosphorylation. This assumption was confirmed by studies of in vitro phosphorylation using purified SS-B/La protein and purified casein kinase type II as a model system. A high degree of phosphorylation of the SS-B/La protein (molecular mass 49 kDa) substantially diminished its binding capacity for poly[3H]U. However, binding of human autoantibodies against SS-B/La antigen increases 2-fold with increased SS-B/La phosphorylation. Complete phosphorylation in vitro led to partial molecular transformation, yielding an antigenically cross-reacting component with an apparent molecular mass of 51 kDa which could not be detected during in vivo phosphorylation.