Regulation of GM-CSF expression by the transcription factor c-Maf

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Regulation of GM-CSF expression by the transcription factor c-Maf Jane Gilmour, PhD, David J. Cousins, PhD, David F. Richards, MSc, Zahid Sattar, PhD, Tak H. Lee, MD, DSc, Paul Lavender, PhD Journal of Allergy and Clinical Immunology Volume 120, Issue 1, Pages 56-63 (July 2007) DOI: 10.1016/j.jaci.2007.03.033 Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 1 c-Maf activates GM-CSF expression. A, Schematic diagram of the human chromosome 5q cytokine locus. Conventional RT-PCR (B) and quantitative real-time RT-PCR (C) of the chromosome 5q cytokine locus. D, qRT-PCR of Amaxa transfected CD4+ cells; average data from 5 experiments. qRT-PCR was performed for each gene as described in Methods. Journal of Allergy and Clinical Immunology 2007 120, 56-63DOI: (10.1016/j.jaci.2007.03.033) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 2 Increased GM-CSF and IL-4 production by c-Maf transfected Jurkat cells. Supernatants were taken from activated Jurkat cells transiently transfected with a plasmid containing c-Maf, the control plasmid pcDNA3, or no DNA. A, GM-CSF levels assayed by ELISA at 72 hours. B, IL-4 levels assayed by CBA at 24 hours. C, IL-2 levels assayed by CBA at 24 hours. Graphs represent mean data from 4, 6, and 6 separate experiments, respectively. Journal of Allergy and Clinical Immunology 2007 120, 56-63DOI: (10.1016/j.jaci.2007.03.033) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 3 Transactivation of the GM-CSF promoter by c-Maf. CAT activity was measured in extracts from activated Jurkat cells cotransfected with cytokine promoter constructs and either c-Maf or a control plasmid. Data are from 3 separate experiments and normalized to the sample cotransfected with c-Maf and pIL-4. ∗P < .05 and ∗∗P < .01 compared with the sample cotransfected with c-Maf and pBLCAT3. B, CAT activity was measured in extracts from activated Jurkat cells cotransfected with the GM-CSF promoter constructs and either a plasmid containing c-Maf or a control plasmid. Data are from 6 separate experiments and normalized to the sample cotransfected with c-Maf and pGM-100. ∗∗P < .01 compared with the sample cotransfected with c-Maf and pBLCAT3. Journal of Allergy and Clinical Immunology 2007 120, 56-63DOI: (10.1016/j.jaci.2007.03.033) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 4 c-Maf interacts with the GM-CSF proximal promoter. A, Sequence of the GM-CSF promoter region thought to be bound by c-Maf. Known binding sites are represented by black boxes. Oligos used as competitors in the affinity pulldown shown in Fig E1, A, and to construct the plasmids transfected in Fig E1 are represented by gray boxes. B, Biotinylated oligo affinity pulldown of the GM-CSF promoter in HEK-293 cells. Journal of Allergy and Clinical Immunology 2007 120, 56-63DOI: (10.1016/j.jaci.2007.03.033) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 5 Analysis of 28-day in vitro differentiated human TH1 and TH2 cells. A, Western blot of nuclear (N) and cytoplasmic (C) extracts from TH1 and TH2 cells using the indicated primary antibodies and the relevant secondary antibodies. B, Densitometry of c-Maf protein expression. The graph represents mean data from 3 independent experiments normalized to the TH2 unstimulated sample. Data were analyzed by using a 2-way ANOVA test. NE, Nuclear extract. Journal of Allergy and Clinical Immunology 2007 120, 56-63DOI: (10.1016/j.jaci.2007.03.033) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions