hdac 1 Search Results


human recombinant c ter gst hdac 1  (Sino Biological)
93
Sino Biological human recombinant c ter gst hdac 1
Human Recombinant C Ter Gst Hdac 1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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short hairpin sh ‑hdac1  (OriGene)
91
OriGene short hairpin sh ‑hdac1
Short Hairpin Sh ‑Hdac1, supplied by OriGene, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hdac1  (Cell Signaling Technology Inc)
97
Cell Signaling Technology Inc hdac1
Figure 8. ARID1A interacts with <t>HDAC1</t> through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.
Hdac1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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complex with hsp70  (BPS Bioscience)
95
BPS Bioscience complex with hsp70
Figure 8. ARID1A interacts with <t>HDAC1</t> through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.
Complex With Hsp70, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hdac1  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Hdac1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti hdac1  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc anti hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Anti Hdac1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pcdna3 1 hdac1  (Addgene inc)
93
Addgene inc pcdna3 1 hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Pcdna3 1 Hdac1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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lactate dehydrogenase a  (Biorbyt)
93
Biorbyt lactate dehydrogenase a
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Lactate Dehydrogenase A, supplied by Biorbyt, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hdac1 sirna knockdown  (OriGene)
90
OriGene hdac1 sirna knockdown
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Hdac1 Sirna Knockdown, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti hdac1  (Bethyl)
93
Bethyl anti hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Anti Hdac1, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hdac1  (Proteintech)
96
Proteintech hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Hdac1, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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kinetic hdac1 assay kit  (BPS Bioscience)
93
BPS Bioscience kinetic hdac1 assay kit
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Kinetic Hdac1 Assay Kit, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Figure 8. ARID1A interacts with HDAC1 through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

Journal: Cellular and molecular gastroenterology and hepatology

Article Title: Targeting USP9X-AMPK Axis in ARID1A-Deficient Hepatocellular Carcinoma.

doi: 10.1016/j.jcmgh.2022.03.009

Figure Lengend Snippet: Figure 8. ARID1A interacts with HDAC1 through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

Article Snippet: Antibodies against acetyl–histone H3 (Lys9) (9649), acetyl–histone H3 (Lys9) (8173), ULK1 (8054), phospho-ULK1 (Ser317) (12753), phospho-ULK1 (Ser555) (5869), phospho-ULK1 (Ser757) (6888), acetyl-CoA carboxylase (3676), phospho-acetyl-CoA carboxylase (Ser79) (11818), AMPKa (2532), phosphoAMPKa (Thr172) (2535), LC3B (3868), and HDAC1 (34589) were purchased from Cell Signaling Technology (Danvers, MA); antibodies against PRKAA1 (10929), PRKAA2 (18167), USP9X (55054), glyceraldehyde-3-phosphate dehydrogenase (10494), and liver kinase B1 (10746) were purchased from Proteintech (Rosemont, IL); antibodies against ARID1A (sc-32761), a-tubulin (sc-32293), b-actin (sc-47778), ubiquitin (sc-8017), and c-myc (sc-764) were purchased from Santa Cruz Biotechnology (Dallas, Texas); and antibodies against Flag and HA were purchased from Sigma-Aldrich (St. Louis, MO).

Techniques: Staining, Control, Transfection, Co-Immunoprecipitation Assay, FLAG-tag

Figure 9. ARID1A regulates the promoter activity of USP9X via HDAC1. (A) Data from the Catalogue of Somatic Mutations in Cancer shows that 1989* is the most frequent mutation of ARID1A. (B) Interaction between ARID1A-WT or ARID1A-1989* mutation with HDAC1. (C) Influence of ARID1A-WT or ARID1A-1989* mutation on the ubiquitination of PRKAA2. (D) Influence of ARID1A-WT or ARID1A-1989* mutation on the promoter activity of USP9X. The promoter activity of USP9X in (E) HEK293T cells overexpressing ARID1A or HDAC1 (OE) or in (F) ARID1A knockout Huh7 and YY-8103 cells is examined by luciferase reporter assay. (G) Influence of ARID1A-WT or ARID1A-1989* mutation on the expression of USP9X and PRKAA2. CTRL, control; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. **P<0.01, ***P<0.001, ns, not significant.

Journal: Cellular and molecular gastroenterology and hepatology

Article Title: Targeting USP9X-AMPK Axis in ARID1A-Deficient Hepatocellular Carcinoma.

doi: 10.1016/j.jcmgh.2022.03.009

Figure Lengend Snippet: Figure 9. ARID1A regulates the promoter activity of USP9X via HDAC1. (A) Data from the Catalogue of Somatic Mutations in Cancer shows that 1989* is the most frequent mutation of ARID1A. (B) Interaction between ARID1A-WT or ARID1A-1989* mutation with HDAC1. (C) Influence of ARID1A-WT or ARID1A-1989* mutation on the ubiquitination of PRKAA2. (D) Influence of ARID1A-WT or ARID1A-1989* mutation on the promoter activity of USP9X. The promoter activity of USP9X in (E) HEK293T cells overexpressing ARID1A or HDAC1 (OE) or in (F) ARID1A knockout Huh7 and YY-8103 cells is examined by luciferase reporter assay. (G) Influence of ARID1A-WT or ARID1A-1989* mutation on the expression of USP9X and PRKAA2. CTRL, control; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. **P<0.01, ***P<0.001, ns, not significant.

Article Snippet: Antibodies against acetyl–histone H3 (Lys9) (9649), acetyl–histone H3 (Lys9) (8173), ULK1 (8054), phospho-ULK1 (Ser317) (12753), phospho-ULK1 (Ser555) (5869), phospho-ULK1 (Ser757) (6888), acetyl-CoA carboxylase (3676), phospho-acetyl-CoA carboxylase (Ser79) (11818), AMPKa (2532), phosphoAMPKa (Thr172) (2535), LC3B (3868), and HDAC1 (34589) were purchased from Cell Signaling Technology (Danvers, MA); antibodies against PRKAA1 (10929), PRKAA2 (18167), USP9X (55054), glyceraldehyde-3-phosphate dehydrogenase (10494), and liver kinase B1 (10746) were purchased from Proteintech (Rosemont, IL); antibodies against ARID1A (sc-32761), a-tubulin (sc-32293), b-actin (sc-47778), ubiquitin (sc-8017), and c-myc (sc-764) were purchased from Santa Cruz Biotechnology (Dallas, Texas); and antibodies against Flag and HA were purchased from Sigma-Aldrich (St. Louis, MO).

Techniques: Activity Assay, Mutagenesis, Ubiquitin Proteomics, Knock-Out, Luciferase, Reporter Assay, Expressing, Control

Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, HDAC1, HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005

Journal: PloS one

Article Title: Histone deacetylases and NF-kB signaling coordinate expression of CX3CL1 in epithelial cells in response to microbial challenge by suppressing miR-424 and miR-503.

doi: 10.1371/journal.pone.0065153

Figure Lengend Snippet: Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, HDAC1, HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005

Article Snippet: In brief, 106 H69 cells were exposed to C. parvum infection for 8 h. The chromatin fraction was immunoprecipitated overnight at 4uC using antibodies to p65 (Upstate Biotechnologies), p50 (Santa Cruz), HDAC1 (Santa Cruz), HDAC2 (Santa Cruz), Sirt1 (Santa Cruz), C/EBPb (Abcam).

Techniques: Infection, Binding Assay, Real-time Polymerase Chain Reaction, Control