Fig. 4.
Fig. 4. Effects in an HuT-102 cell line. / Effects of a 48-hour treatment of IFN and As in an HuT-102 cell line on the activation of the transcription factors NF-κB (A) and RXR (B) assessed by electrophoretic mobility shift assay using consensus oligonucleotide probes for NF-κB and RXR, respectively. Note that As-IFN significantly diminishes 1 of the 2 NF-κB complexes (arrow in A). (C) NF-κB subunit specificity was determined by using antibodies to the NF-κB components p50 and p65/RelA, resulting in “supershift” (arrow). A longer exposure (*) of the RelA supershift is shown. (D) Effects of IFN, As, and their combination on the expression of p65/RelA protein. Combined As-IFN treatment dramatically decrease Rel-A–containing complexes without inducing Rel-A degradation. Effects of a 48-hour As-IFN treatment on NF-κB binding in C91-PL cell line (E) and fresh ATL leukemic cells (F). As above, subunit specificity was determined by “supershift” (arrow) and * indicates longer exposure.

Effects in an HuT-102 cell line.

Effects of a 48-hour treatment of IFN and As in an HuT-102 cell line on the activation of the transcription factors NF-κB (A) and RXR (B) assessed by electrophoretic mobility shift assay using consensus oligonucleotide probes for NF-κB and RXR, respectively. Note that As-IFN significantly diminishes 1 of the 2 NF-κB complexes (arrow in A). (C) NF-κB subunit specificity was determined by using antibodies to the NF-κB components p50 and p65/RelA, resulting in “supershift” (arrow). A longer exposure (*) of the RelA supershift is shown. (D) Effects of IFN, As, and their combination on the expression of p65/RelA protein. Combined As-IFN treatment dramatically decrease Rel-A–containing complexes without inducing Rel-A degradation. Effects of a 48-hour As-IFN treatment on NF-κB binding in C91-PL cell line (E) and fresh ATL leukemic cells (F). As above, subunit specificity was determined by “supershift” (arrow) and * indicates longer exposure.

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