Abstract

<p>A. PQ induced relocalization of SR proteins in the nucleus of treated cells. SH-SY5Y cells treated with vehicle or with 0.75 mM PQ for 18 h were immunostained with an anti-SC35 antibody (<i>upper row</i>), transiently transfected with GFP-ASF/SF2 (<i>middle row</i>), or with GFP-hnRNPA1 (<i>lower row</i>). Nuclei were stained with DAPI. B. Increased phosphorylation of SR proteins in PQ-treated cells. Total extract of control or PQ-treated cells was probed with mAb104 to determine the phosphorylation state of classical SR proteins. C. The same extracts used for the Western blot shown in panel B were probed with the 16H3 monoclonal antibody that detects SR proteins regardless of their phosphorylation status, with anti ASF/SF2 and anti-SRp20 monoclonal antibodies. Actin was used as loading control.</p

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