hdac2  (BPS Bioscience)

Journal: medRxiv

Article Title: The Effect of Vitamin-D Supplementation on HDAC2 Levels in Stable COPD Patients

doi: 10.64898/2026.04.05.26348641

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Article Snippet: HDAC2 levels were measured using a commercially available enzyme-linked immunosorbent assay (ELISA) kit (BT LAB, Bioassay Technology Laboratory, Cat. No. E0988 Hu), according to the manufacturer’s instructions.

Techniques:

Journal: Journal of Advanced Research

Article Title: HDAC2 enhances the antimicrobial activity of neutrophils by promoting the formation of neutrophil extracellular traps (NETs) in sepsis

doi: 10.1016/j.jare.2025.08.041

Figure Lengend Snippet: HDAC2 is highly expressed in sepsis. (A) Analysis of HDAC2 expression in GEO. HDAC2 expression was analyzed using the GSE95233 dataset, including 22 healthy controls and a total of 102 patients with sepsis. (B)The level of HDAC2 in serum was detected in the CLP-induced septic mice. Blood was collected from mouse orbits, and the level of HDAC2 was measured by Elisa. (C) The level of HDAC2 in serum was detected in the LPS (10 mg/kg)-induced septic mice. Blood was collected from mouse orbits, and the level of HDAC2 was measured by Elisa. (D) The HDAC2 mRNA expression in the peripheral blood leukocytes of (i) CLP-induced septic mice and (ii) 10 mg/kg LPS-induced septic mice. Data are presented as the means ± SEM. of independent experiments. *P < 0.05, **P < 0.01 (two-tailed Student’s t -test). n = 5 mice per group.

Article Snippet: HDAC2 KO mice (6–8 weeks old, male) were supplied by Jackson Laboratory.

Techniques: Expressing, Enzyme-linked Immunosorbent Assay, Two Tailed Test

Journal: Journal of Advanced Research

Article Title: HDAC2 enhances the antimicrobial activity of neutrophils by promoting the formation of neutrophil extracellular traps (NETs) in sepsis

doi: 10.1016/j.jare.2025.08.041

Figure Lengend Snippet: HDAC2 deficiency or inhibition compromises the antimicrobial efficacy, but improves anti-inflammatory responses in the mice with sepsis. (A-D) Effects of the HDAC2-knockout or inhibition on the survival of mice with CLP-induced or LPS-induced sepsis. Kaplan-Meier curves for the HDAC2-knockout or inhibition by SAHA-treated mice with or CLP-induced or LPS-induced sepsis (n = 20 mice). (E-H) Serum IL-6 and IL-1β levels were determined in the sham or CLP-induced or LPS-induced septic mice treated with or without SAHA (25 mg/kg). These inflammatory parameters were measured by ELISA. Data are shown as mean ± SEM. *p < 0.05; n = 5 mice per group. (I and J) Serum AST, ALT, Urea and Crea levels were measured in sham or CLP-induced or LPS-induced septic mice treated with or without SAHA. Blood was collected by orbital sampling, and these biochemical parameters were measured by the Automatic Biochemistry Analyzer. Data are shown as mean ± SEM. **p < 0.01; n = 5 mice per group.

Article Snippet: HDAC2 KO mice (6–8 weeks old, male) were supplied by Jackson Laboratory.

Techniques: Inhibition, Knock-Out, Enzyme-linked Immunosorbent Assay, Sampling

Journal: Journal of Advanced Research

Article Title: HDAC2 enhances the antimicrobial activity of neutrophils by promoting the formation of neutrophil extracellular traps (NETs) in sepsis

doi: 10.1016/j.jare.2025.08.041

Figure Lengend Snippet: HDAC2 enhances antimicrobial activities against E.coli in mice. (A) Bacterial loads in the blood were calculated in HDAC2-knockout and wild type mice. (A)The picture of the bacterial clones was taken by BIO-RAD ChemiDoc“MP Imaging System. (B)The number of colony-forming units (CFU) in the blood of mice was calculated. HDAC2 WT and HDAC2 KO mice were administrated with E. coli- GFP (5 × 10 7 ) by intravenous Injection. Blood (20 μl) was taken from the tail vein of the mice, applied to the pretreated solid MHA medium, and incubated at 37 °C for 20 h. Count the colonies on the culture medium and take pictures. The experiments were performed in quintuplicate, data are presented as the means ± SEM. of independent experiments. *P < 0.05, **P < 0.01 (two-tailed Student’s t -test). (B) Bacterial loads in the kidneys were calculated in HDAC2-knockout and wild type mice. The picture of kidneys from HDAC2 WT and HDAC2 KO mice were taken. The number of colony-forming units (CFU) in the kidneys of mice was calculated. The kidneys from HDAC2 KO and HDAC2 WT mice were weighed, ground, spread on the MHA plates, incubated for 16–24 h at 37 °C, and then bacterial clones were counted. The experiments were performed in quintuplicate, data are presented as the means ± SEM. of independent experiments. *P < 0.05, **P < 0.01 (two-tailed Student’s t -test). n = 5 mice per group. (C) H&E staining of livers and kidneys. The arrows indicate damage section of tissue. (D) Serum CRP and PCT levels of mice with E. coli- GFP bacteremia at 24 h. The CRP and PCT were measured by ELISA. Data are shown as mean ± SEM. *p < 0.05; n = 5 mice per group. ns, not significant.

Article Snippet: HDAC2 KO mice (6–8 weeks old, male) were supplied by Jackson Laboratory.

Techniques: Knock-Out, Clone Assay, Imaging, Injection, Incubation, Two Tailed Test, Staining, Enzyme-linked Immunosorbent Assay

Journal: Journal of Advanced Research

Article Title: HDAC2 enhances the antimicrobial activity of neutrophils by promoting the formation of neutrophil extracellular traps (NETs) in sepsis

doi: 10.1016/j.jare.2025.08.041

Figure Lengend Snippet: HDAC2 is required for NET formation. (A and B) Phagocytic uptake and intracellular killing in neutrophils were detected by flow-based assay and colon-formation assay. (A) Phagocytic uptake in neutrophils was detected by flow-based assay. Neutrophils were isolated from peripheral blood of HDAC2 KO or HDAC2 WT mice, and they were co-incubated with E. coli -GFP for two hours. (B) Intracellular killing in neutrophils was detected by colon-formation assay. Blood was taken from the tail vein of the mice, then applied to the pretreated solid MHA medium and incubated at 37 °C for 24 h. The number of bacterial clones was calculated. n = 5 mice per group. (C-D) NETs were detected in the neutrophils from peripheral blood of HDAC2 KO or HDAC2 WT mice by immunofluorescence. Representative data showing MPO-positive cells defined as positive NETs. Data are presented as the means ± SEM. of independent experiments. *P < 0.05, **P < 0.01 (two-tailed Student’s t -test). (E) NETs were detected in the neutrophils from peripheral blood of HDAC2 KO or HDAC2 WT mice by a flow cytometry-based assay. Representative flow data showing positive cells in global Histone H3 citrullination of H3R2, H3R8 or H3R17 sites, defined as positive NETs. (F) NETs markers were detected by western blotting in the neutrophils from HDAC2 WT mice after stimulation with LPS (50 μg/ml) and SAHA (5 μM). Representative data showing H3-Cit expression defined as NETs. The H3 protein was used for western blot loading controls.

Article Snippet: HDAC2 KO mice (6–8 weeks old, male) were supplied by Jackson Laboratory.

Techniques: Tube Formation Assay, Isolation, Incubation, Clone Assay, Immunofluorescence, Two Tailed Test, Flow Cytometry, Western Blot, Expressing

Journal: Journal of Advanced Research

Article Title: HDAC2 enhances the antimicrobial activity of neutrophils by promoting the formation of neutrophil extracellular traps (NETs) in sepsis

doi: 10.1016/j.jare.2025.08.041

Figure Lengend Snippet: HDAC2 promotes NETs formation through the acetylation-citrullination pathway. (A–C) Representative images for LPS (50 μg/ml)-stimulated primary neutrophils from HDAC2 WT and HDAC2 KO mice. (A) Immunostaining for histone H3K18 acetylation (green) was performed with DNA counterstained with Hoechst 33342 (blue) and corresponding MFI of quantitative data (E). Scale bars, 20 μm. (B) Immunostaining for histone H3R17 methylation (green) was performed with DNA counterstained with Hoechst 33342 (blue) and corresponding MFI of quantitative data (F). Scale bars, 20 μm. (C) Immunostaining for histone H3R17 citrullination (green) was performed with DNA counterstained with Hoechst 33342 (blue) and corresponding MFI of quantitative data (G). Scale bars, 20 μm. (D) Histone H3R17 citrullination was regulated by H3R17 methylation inhibitor (EZM2302) and HDAC2 inhibitor (SAHA), and immunostaining for histone H3R17 citrullination (green) was performed with DNA counterstained with Hoechst 33342 (blue), the corresponding MFI of quantitative data (H). Scale bars, 20 μm. (I) H3K18 acetylation, H3R17 methylation and H3R17 citrullination were detected by western blotting in the neutrophils from HDAC2 WT and HDAC2 KO mice after stimulation with LPS (50 μg/ml). The H3 protein was used for western blot loading controls. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: HDAC2 KO mice (6–8 weeks old, male) were supplied by Jackson Laboratory.

Techniques: Immunostaining, Methylation, Western Blot

Journal: Journal of Advanced Research

Article Title: HDAC2 enhances the antimicrobial activity of neutrophils by promoting the formation of neutrophil extracellular traps (NETs) in sepsis

doi: 10.1016/j.jare.2025.08.041

Figure Lengend Snippet: Protective effects of HDAC2 inhibition and histone methylation inhibition in CLP-induced septic mice (A) Kaplan-Meier curves of CLP-induced septic mice treated with or without SAHA and EZM2302 (n = 20 mice). (B and C) Serum MPO, IL-6 and IL-1β levels were measured with mouse ELISA kit in the CLP-induced septic mice treated with or without SAHA and EZM2302. (D) Serum AST, ALT, Urea and Crea levels were measured in the CLP-induced septic mice treated with or without SAHA and EZM2302. Blood was collected by orbital sampling, and serum biochemical parameters were measured by the Automatic Biochemistry Analyzer. The experiments were performed in quintuplicate, data are presented as the means ± SEM. of independent experiments. *P < 0.05, **P < 0.01 (two-tailed Student’s t -test). (n = 5 mice). (E and F) Histology of lungs, kidneys and livers from mice treated with or without SAHA and EZM2302. (E) The Histology with H&E staining for lungs, kidneys and livers. (F) Cell apoptosis in lungs, kidneys and livers was stained with cleaved-caspase 3. The mice were treated with EZM2302 (25 mg/kg) two hours prior to cecal ligation and puncture (CLP), and SAHA was administered after CLP surgery. SAHA, a HDAC2 inhibitor; EZM2302, a methylation inhibitor.

Article Snippet: HDAC2 KO mice (6–8 weeks old, male) were supplied by Jackson Laboratory.

Techniques: Inhibition, Methylation, Enzyme-linked Immunosorbent Assay, Sampling, Two Tailed Test, Staining, Ligation

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: HDAC1, HDAC2 and HDAC8 are DUSP26-interacting proteins in chondrocytes. (A) IP/MS analysis in DUSP26-overexpressing chondrocytes under IL-1β stimulation. (B) Flow chart of target protein screening. (C) Immunohistochemical staining of HDAC1, HDAC2 and HDAC8 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (D) Protein expression levels of HDAC1, p-HDAC1, HDAC2, p-HDAC2, HDAC8 and p-HDAC8 in the chondrocytes by western blotting. (E) Co-IP experiments with DUSP26 protein from extracts of IL-1β-treated chondrocytes followed by western blotting with indicated antibodies. DEG, differentially expressed gene; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IB, immunoblot; IL, interleukin; IP, immunoprecipitation; LC-MS/MS, liquid chromatography-tandem MS; mRNA-seq, mRNA sequencing; MS, mass spectrometry; p-, phosphorylated.

Article Snippet: These antibodies included those specific for DUSP26 (cat. no. bs-7910R; BIOSS), COL2A1 (cat. no. AF0135; Affinity Biosciences), histone deacetylase (HDAC)1 (cat. no. AF6433; Affinity Biosciences), phosphorylated (p)-HDAC1 (Ser421) (cat. no. PA5-36810; Thermo Fisher Scientific, Inc.), HDAC2 (cat. no. AF6470; Affinity Biosciences), p-HDAC2 (Ser394) (cat. no. bs-5389R; BIOSS), HDAC8 (cat. no. AF6481; Affinity Biosciences) and p-HDAC8 (Ser39) (cat. no. AF3481; Affinity Biosciences).

Techniques: Protein-Protein interactions, Immunohistochemical staining, Staining, Control, Expressing, Western Blot, Co-Immunoprecipitation Assay, Histone Deacetylase Assay, Immunoprecipitation, Liquid Chromatography with Mass Spectroscopy, Liquid Chromatography, Sequencing, Mass Spectrometry

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: Inactivation of HDAC1/2/8 inhibits DUSP26 silencing-triggered cartilage degeneration. (A) Total protein and phosphorylation levels of HDAC1, HDAC2 and HDAC8 in IL-1β-treated chondrocytes determined by western blotting. (B) Relative mRNA expression levels of HDAC1, HDAC2 and HDAC8 in chondrocytes, as determined by reverse transcription-quantitative PCR. (C) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (D) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. (E) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (F) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. (B-D) Representative results of three independent experiments are shown. COL1A1, type I collagen; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IL, interleukin; NC, negative control; ns, no significance; sh, short hairpin; TSA, trichostatin A.

Article Snippet: These antibodies included those specific for DUSP26 (cat. no. bs-7910R; BIOSS), COL2A1 (cat. no. AF0135; Affinity Biosciences), histone deacetylase (HDAC)1 (cat. no. AF6433; Affinity Biosciences), phosphorylated (p)-HDAC1 (Ser421) (cat. no. PA5-36810; Thermo Fisher Scientific, Inc.), HDAC2 (cat. no. AF6470; Affinity Biosciences), p-HDAC2 (Ser394) (cat. no. bs-5389R; BIOSS), HDAC8 (cat. no. AF6481; Affinity Biosciences) and p-HDAC8 (Ser39) (cat. no. AF3481; Affinity Biosciences).

Techniques: Phospho-proteomics, Western Blot, Expressing, Reverse Transcription, Real-time Polymerase Chain Reaction, Histone Deacetylase Assay, Negative Control