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<t>PRMT5</t> represses CAMP mRNA and transcription. A. PRMT5 and BRG1 are components of the same complex in lung epithelial cells. Beas-2B cell lysates were used for immunoprecipitation with BRG1antibody, PRMT5 antibody or control IgG antibody. Similar results were observed in 3 independent experiments. B. Beas-2B cells were transfected with the CAMP promoter luciferase construct (−693/+17; 250 ng) alone or with C/EBPα expression vector (100 ng) in the absence or presence of increasing concentrations of PRMT5. PRMT5 resulted in a significant decrease in the induction of CAMP transcription by 1,25(OH)2D3 or C/EBPα + 1,25(OH)2D3. Results represent the mean ± SE of 3-4 separate experiments. * p <0.05 compared to cells treated with 1,25(OH)2D3 or transfected with C/EBPα and treated with 1,25(OH)2D3 in the absence of PRMT5. Similar results were observed using A549 cells (not shown). C. qRT-PCR analysis of CAMP mRNA was performed using total RNA from Beas-2B cells. Upper panel: Cells were transfected with empty vector or PRMT expression vector. 24h post transfections cells were treated with vehicle (basal) or with 1,25(OH)2D3 (10 nM) for another 24h. Results represent the mean ± SE of 3 separate experiments. *p < 0.05 PRMT5 transfected 1,25(OH)2D3 treated compared to 1,25(OH)2D3 treated. Lower panel: Cells were transfected with vector or C/EBPα (100 ng) in the presence or absence of PRMT5. PRMT5 resulted in a significant decrease in induction of CAMP mRNA by C/EBPα (mean + SE of 3 separate experiments). * p < 0.05 PRMT5 transfected compared to cells transfected with C/EBPα in the absence of PRMT5. D. PRMT5 inhibitor CMP5 enhances 1,25(OH)2D3 induction of CAMP mRNA. qRT-PCR analysis of CAMP mRNA in NHBE cells treated with 1,25(OH)2D3 (10 nM) or 1,25(OH)2D3 + CMP5 (40 uM) for 24h. * p < 0.05 compared to 1,25(OH)2D3 (+D) treated NHBE cells. Data represent the mean ± SE of 3 independent experiments. E. ChIP analysis of dimethylation of H4R3 at the CAMP promoter in response to 1,25(OH)2D3. Beas-2B cells were treated with vehicle or 1,25(OH)2D3 for 2 or 6h and cross linked by 1% formaldehyde for 15 min. Cross linked cell lysates were subjected to immunoprecipitation with H4R3Me2 antibody. DNA was isolated and PCR using specific primers designed to amplify fragments of the CAMP promoter containing the C/EBP site (at −627/−619) was carried out in the linear range of DNA amplification. IgG was used as a control. F. Time dependent modulation of H4R3Me2 (H4R3 is a histone substrate of PRMT5) by 1,25(OH)2D3 in Beas-2B cells. Cells were treated with 1,25(OH)2D3 (10 nM) and protein lysates were collected at specific times. Representative Western blot. Lower panel: Graphic representation of Western blot analysis. 6-24h after 1,25(OH)2D3 treatment there was a significant increase in H4R3Me2s (p <0.05 compared to basal).

Prmt5 Antiserum, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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prmt5 antiserum - by Bioz Stars, 2026-07

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1) Product Images from "PU.1 and Epigenetic Signals Modulate 1,25-Dihydroxyvitamin D 3 and C/EBPα Regulation of the Human Cathelicidin Antimicrobial Peptide Gene in Lung Epithelial Cells"

Article Title: PU.1 and Epigenetic Signals Modulate 1,25-Dihydroxyvitamin D 3 and C/EBPα Regulation of the Human Cathelicidin Antimicrobial Peptide Gene in Lung Epithelial Cells

Journal: Journal of cellular physiology

doi: 10.1002/jcp.27702

PRMT5 represses CAMP mRNA and transcription. A. PRMT5 and BRG1 are components of the same complex in lung epithelial cells. Beas-2B cell lysates were used for immunoprecipitation with BRG1antibody, PRMT5 antibody or control IgG antibody. Similar results were observed in 3 independent experiments. B. Beas-2B cells were transfected with the CAMP promoter luciferase construct (−693/+17; 250 ng) alone or with C/EBPα expression vector (100 ng) in the absence or presence of increasing concentrations of PRMT5. PRMT5 resulted in a significant decrease in the induction of CAMP transcription by 1,25(OH)2D3 or C/EBPα + 1,25(OH)2D3. Results represent the mean ± SE of 3-4 separate experiments. * p <0.05 compared to cells treated with 1,25(OH)2D3 or transfected with C/EBPα and treated with 1,25(OH)2D3 in the absence of PRMT5. Similar results were observed using A549 cells (not shown). C. qRT-PCR analysis of CAMP mRNA was performed using total RNA from Beas-2B cells. Upper panel: Cells were transfected with empty vector or PRMT expression vector. 24h post transfections cells were treated with vehicle (basal) or with 1,25(OH)2D3 (10 nM) for another 24h. Results represent the mean ± SE of 3 separate experiments. *p < 0.05 PRMT5 transfected 1,25(OH)2D3 treated compared to 1,25(OH)2D3 treated. Lower panel: Cells were transfected with vector or C/EBPα (100 ng) in the presence or absence of PRMT5. PRMT5 resulted in a significant decrease in induction of CAMP mRNA by C/EBPα (mean + SE of 3 separate experiments). * p < 0.05 PRMT5 transfected compared to cells transfected with C/EBPα in the absence of PRMT5. D. PRMT5 inhibitor CMP5 enhances 1,25(OH)2D3 induction of CAMP mRNA. qRT-PCR analysis of CAMP mRNA in NHBE cells treated with 1,25(OH)2D3 (10 nM) or 1,25(OH)2D3 + CMP5 (40 uM) for 24h. * p < 0.05 compared to 1,25(OH)2D3 (+D) treated NHBE cells. Data represent the mean ± SE of 3 independent experiments. E. ChIP analysis of dimethylation of H4R3 at the CAMP promoter in response to 1,25(OH)2D3. Beas-2B cells were treated with vehicle or 1,25(OH)2D3 for 2 or 6h and cross linked by 1% formaldehyde for 15 min. Cross linked cell lysates were subjected to immunoprecipitation with H4R3Me2 antibody. DNA was isolated and PCR using specific primers designed to amplify fragments of the CAMP promoter containing the C/EBP site (at −627/−619) was carried out in the linear range of DNA amplification. IgG was used as a control. F. Time dependent modulation of H4R3Me2 (H4R3 is a histone substrate of PRMT5) by 1,25(OH)2D3 in Beas-2B cells. Cells were treated with 1,25(OH)2D3 (10 nM) and protein lysates were collected at specific times. Representative Western blot. Lower panel: Graphic representation of Western blot analysis. 6-24h after 1,25(OH)2D3 treatment there was a significant increase in H4R3Me2s (p <0.05 compared to basal).

Figure Legend Snippet: PRMT5 represses CAMP mRNA and transcription. A. PRMT5 and BRG1 are components of the same complex in lung epithelial cells. Beas-2B cell lysates were used for immunoprecipitation with BRG1antibody, PRMT5 antibody or control IgG antibody. Similar results were observed in 3 independent experiments. B. Beas-2B cells were transfected with the CAMP promoter luciferase construct (−693/+17; 250 ng) alone or with C/EBPα expression vector (100 ng) in the absence or presence of increasing concentrations of PRMT5. PRMT5 resulted in a significant decrease in the induction of CAMP transcription by 1,25(OH)2D3 or C/EBPα + 1,25(OH)2D3. Results represent the mean ± SE of 3-4 separate experiments. * p <0.05 compared to cells treated with 1,25(OH)2D3 or transfected with C/EBPα and treated with 1,25(OH)2D3 in the absence of PRMT5. Similar results were observed using A549 cells (not shown). C. qRT-PCR analysis of CAMP mRNA was performed using total RNA from Beas-2B cells. Upper panel: Cells were transfected with empty vector or PRMT expression vector. 24h post transfections cells were treated with vehicle (basal) or with 1,25(OH)2D3 (10 nM) for another 24h. Results represent the mean ± SE of 3 separate experiments. *p < 0.05 PRMT5 transfected 1,25(OH)2D3 treated compared to 1,25(OH)2D3 treated. Lower panel: Cells were transfected with vector or C/EBPα (100 ng) in the presence or absence of PRMT5. PRMT5 resulted in a significant decrease in induction of CAMP mRNA by C/EBPα (mean + SE of 3 separate experiments). * p < 0.05 PRMT5 transfected compared to cells transfected with C/EBPα in the absence of PRMT5. D. PRMT5 inhibitor CMP5 enhances 1,25(OH)2D3 induction of CAMP mRNA. qRT-PCR analysis of CAMP mRNA in NHBE cells treated with 1,25(OH)2D3 (10 nM) or 1,25(OH)2D3 + CMP5 (40 uM) for 24h. * p < 0.05 compared to 1,25(OH)2D3 (+D) treated NHBE cells. Data represent the mean ± SE of 3 independent experiments. E. ChIP analysis of dimethylation of H4R3 at the CAMP promoter in response to 1,25(OH)2D3. Beas-2B cells were treated with vehicle or 1,25(OH)2D3 for 2 or 6h and cross linked by 1% formaldehyde for 15 min. Cross linked cell lysates were subjected to immunoprecipitation with H4R3Me2 antibody. DNA was isolated and PCR using specific primers designed to amplify fragments of the CAMP promoter containing the C/EBP site (at −627/−619) was carried out in the linear range of DNA amplification. IgG was used as a control. F. Time dependent modulation of H4R3Me2 (H4R3 is a histone substrate of PRMT5) by 1,25(OH)2D3 in Beas-2B cells. Cells were treated with 1,25(OH)2D3 (10 nM) and protein lysates were collected at specific times. Representative Western blot. Lower panel: Graphic representation of Western blot analysis. 6-24h after 1,25(OH)2D3 treatment there was a significant increase in H4R3Me2s (p <0.05 compared to basal).

Techniques Used: Immunoprecipitation, Control, Transfection, Luciferase, Construct, Expressing, Plasmid Preparation, Quantitative RT-PCR, Isolation, DNA Amplification, Western Blot

Mechanistic model depicting the regulation of the induction of CAMP in lung epithelial cells. Induction of CAMP transcription involved cooperation among VDR, C/EBPα PU.1 and chromatin remodeling. 1,25(OH)2D3 induces C/EBPα in lung epithelial cells (Dhawan et al., 2015). 1,25(OH)2D3 or C/EBPα induce CAMP transcription. PU.1 alone does not enhance CAMP transcription. However, PU.1 together with C/EBPα results in an enhancement of CAMP transcription and together PU.1 and C/EBPα further enhance 1,25(OH)2D3/VDR regulation of CAMP. BRG1, which interacts with C/EBP and is recruited to the C/EBP site by 1,25(OH)2D3, acts cooperatively with histone acetylation to enhance CAMP transcription (cooperation between chromatin remodeling through BRG1 and histone acetylation in the enhancement of 1,25(OH)2D3 regulation of CAMP is shown in Fig. 4). PRMT5 negatively regulates 1,25(OH)2D3 induction of CAMP transcription at least in part via symmetrical dimethylation of H4R3 (see Fig. 5).

Figure Legend Snippet: Mechanistic model depicting the regulation of the induction of CAMP in lung epithelial cells. Induction of CAMP transcription involved cooperation among VDR, C/EBPα PU.1 and chromatin remodeling. 1,25(OH)2D3 induces C/EBPα in lung epithelial cells (Dhawan et al., 2015). 1,25(OH)2D3 or C/EBPα induce CAMP transcription. PU.1 alone does not enhance CAMP transcription. However, PU.1 together with C/EBPα results in an enhancement of CAMP transcription and together PU.1 and C/EBPα further enhance 1,25(OH)2D3/VDR regulation of CAMP. BRG1, which interacts with C/EBP and is recruited to the C/EBP site by 1,25(OH)2D3, acts cooperatively with histone acetylation to enhance CAMP transcription (cooperation between chromatin remodeling through BRG1 and histone acetylation in the enhancement of 1,25(OH)2D3 regulation of CAMP is shown in Fig. 4). PRMT5 negatively regulates 1,25(OH)2D3 induction of CAMP transcription at least in part via symmetrical dimethylation of H4R3 (see Fig. 5).

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Journal: Journal of cellular physiology

Article Title: PU.1 and Epigenetic Signals Modulate 1,25-Dihydroxyvitamin D 3 and C/EBPα Regulation of the Human Cathelicidin Antimicrobial Peptide Gene in Lung Epithelial Cells

doi: 10.1002/jcp.27702

Figure Lengend Snippet: PRMT5 represses CAMP mRNA and transcription. A. PRMT5 and BRG1 are components of the same complex in lung epithelial cells. Beas-2B cell lysates were used for immunoprecipitation with BRG1antibody, PRMT5 antibody or control IgG antibody. Similar results were observed in 3 independent experiments. B. Beas-2B cells were transfected with the CAMP promoter luciferase construct (−693/+17; 250 ng) alone or with C/EBPα expression vector (100 ng) in the absence or presence of increasing concentrations of PRMT5. PRMT5 resulted in a significant decrease in the induction of CAMP transcription by 1,25(OH)2D3 or C/EBPα + 1,25(OH)2D3. Results represent the mean ± SE of 3-4 separate experiments. * p <0.05 compared to cells treated with 1,25(OH)2D3 or transfected with C/EBPα and treated with 1,25(OH)2D3 in the absence of PRMT5. Similar results were observed using A549 cells (not shown). C. qRT-PCR analysis of CAMP mRNA was performed using total RNA from Beas-2B cells. Upper panel: Cells were transfected with empty vector or PRMT expression vector. 24h post transfections cells were treated with vehicle (basal) or with 1,25(OH)2D3 (10 nM) for another 24h. Results represent the mean ± SE of 3 separate experiments. *p < 0.05 PRMT5 transfected 1,25(OH)2D3 treated compared to 1,25(OH)2D3 treated. Lower panel: Cells were transfected with vector or C/EBPα (100 ng) in the presence or absence of PRMT5. PRMT5 resulted in a significant decrease in induction of CAMP mRNA by C/EBPα (mean + SE of 3 separate experiments). * p < 0.05 PRMT5 transfected compared to cells transfected with C/EBPα in the absence of PRMT5. D. PRMT5 inhibitor CMP5 enhances 1,25(OH)2D3 induction of CAMP mRNA. qRT-PCR analysis of CAMP mRNA in NHBE cells treated with 1,25(OH)2D3 (10 nM) or 1,25(OH)2D3 + CMP5 (40 uM) for 24h. * p < 0.05 compared to 1,25(OH)2D3 (+D) treated NHBE cells. Data represent the mean ± SE of 3 independent experiments. E. ChIP analysis of dimethylation of H4R3 at the CAMP promoter in response to 1,25(OH)2D3. Beas-2B cells were treated with vehicle or 1,25(OH)2D3 for 2 or 6h and cross linked by 1% formaldehyde for 15 min. Cross linked cell lysates were subjected to immunoprecipitation with H4R3Me2 antibody. DNA was isolated and PCR using specific primers designed to amplify fragments of the CAMP promoter containing the C/EBP site (at −627/−619) was carried out in the linear range of DNA amplification. IgG was used as a control. F. Time dependent modulation of H4R3Me2 (H4R3 is a histone substrate of PRMT5) by 1,25(OH)2D3 in Beas-2B cells. Cells were treated with 1,25(OH)2D3 (10 nM) and protein lysates were collected at specific times. Representative Western blot. Lower panel: Graphic representation of Western blot analysis. 6-24h after 1,25(OH)2D3 treatment there was a significant increase in H4R3Me2s (p <0.05 compared to basal).

Article Snippet: Materials Polyvinylidene difluoride (PVDF) membranes were purchased from Bio-Rad Laboratories, Inc. PRMT5 antiserum (C-20, sc-22132), BRG-1 antiserum (H88, sc-10768), PU.1 antiserum (T-21, sc-352) were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Immunoprecipitation, Control, Transfection, Luciferase, Construct, Expressing, Plasmid Preparation, Quantitative RT-PCR, Isolation, DNA Amplification, Western Blot

Journal: Journal of cellular physiology

Article Title: PU.1 and Epigenetic Signals Modulate 1,25-Dihydroxyvitamin D 3 and C/EBPα Regulation of the Human Cathelicidin Antimicrobial Peptide Gene in Lung Epithelial Cells

doi: 10.1002/jcp.27702

Figure Lengend Snippet: Mechanistic model depicting the regulation of the induction of CAMP in lung epithelial cells. Induction of CAMP transcription involved cooperation among VDR, C/EBPα PU.1 and chromatin remodeling. 1,25(OH)2D3 induces C/EBPα in lung epithelial cells (Dhawan et al., 2015). 1,25(OH)2D3 or C/EBPα induce CAMP transcription. PU.1 alone does not enhance CAMP transcription. However, PU.1 together with C/EBPα results in an enhancement of CAMP transcription and together PU.1 and C/EBPα further enhance 1,25(OH)2D3/VDR regulation of CAMP. BRG1, which interacts with C/EBP and is recruited to the C/EBP site by 1,25(OH)2D3, acts cooperatively with histone acetylation to enhance CAMP transcription (cooperation between chromatin remodeling through BRG1 and histone acetylation in the enhancement of 1,25(OH)2D3 regulation of CAMP is shown in Fig. 4). PRMT5 negatively regulates 1,25(OH)2D3 induction of CAMP transcription at least in part via symmetrical dimethylation of H4R3 (see Fig. 5).

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