Journal: Frontiers in pharmacology

Article Title: Brg1 and RUNX1 synergy in regulating TRPM4 channel in mouse cardiomyocytes.

doi: 10.3389/fphar.2024.1494205

Figure Lengend Snippet: FIGURE 8 Brg1 modulated TRPM4 promoter activity by interaction with RUNX1. (A) Predicting the residue label and hydrogen bond length of interaction between Brg1 and RUNX1, and the combination state and surface structure of Brg1 and RUNX1 by Protein Data Bank. (B) Co-immunoprecipitation assays of Brg1 and RUNX1 on the nucleoprotein extracted from neonatal mouse cardiomyocytes. (C) RUNX1 significantly boosted TRPM4 promoter activity. Statistical analysis was performed with two-tailed Student’s t-test. *p < 0.05, **p < 0.01 vs. NC group. n = 8 in each group. (D) Brg1 knockdown significantly decreased the TRPM4 promoter activity. **p < 0.01 vs. Scramble-siRNA group by two-tailed Student’s t-test. n = 6 in each group. (E) Inhibited Brg1 by PFI-3 (10 μM) significantly reduced the TRPM4 promoter activity. **p < 0.01 vs. DMSO group by two-tailed Student’s t-test. n = 6 in each group. (F) RUNX1 knockdown declined the increases in TRPM4 promoter activity caused by Brg1-OE. *p < 0.05, vs. NC group; ##p < 0.01 vs. +Scramble-siRNA by (Continued)

Article Snippet: After incubation in 5% non-fat milk for 1.5 h at room temperature, the membranes were incubated at 4°C overnight with TRPM4 antibody (1:500; ABclonal Technology Co.,Ltd.), β-actin antibody (1:1000; Santa, United States), Brg1 antibody (Sigma-Aldrich, 07–478, 1:500) and RUNX1 antibody (Proteintech 25315-1-AP, 1:1000).

Techniques: Activity Assay, Residue, Immunoprecipitation, Two Tailed Test, Knockdown

Journal: Frontiers in pharmacology

Article Title: Brg1 and RUNX1 synergy in regulating TRPM4 channel in mouse cardiomyocytes.

doi: 10.3389/fphar.2024.1494205

Figure Lengend Snippet: FIGURE 9 A schematic diagram summarizing the potential mechanisms that Brg1 interacted with RUNX1 transcriptional regulated TRPM4, that eventually leads to TRPM4 overactivation in cardiomyocytes induced by hypoxia.

Article Snippet: After incubation in 5% non-fat milk for 1.5 h at room temperature, the membranes were incubated at 4°C overnight with TRPM4 antibody (1:500; ABclonal Technology Co.,Ltd.), β-actin antibody (1:1000; Santa, United States), Brg1 antibody (Sigma-Aldrich, 07–478, 1:500) and RUNX1 antibody (Proteintech 25315-1-AP, 1:1000).

Techniques:

Journal: PLoS ONE

Article Title: Demineralized bone matrix used for direct pulp capping in rats

doi: 10.1371/journal.pone.0172693

Figure Lengend Snippet: (A): Representative immunohistochemical images of the blank control group, the Ca(OH) 2 group and the DBM group. a: The blank control group. Pulp morphology was normal. b- f: Ca(OH) 2 group (1, 3, 7, 14, 28 days). g- k: DBM group (1, 3, 7, 14, 28 days). (B): Mean IOD value of Runx2. *means significant difference.

Article Snippet: The sections were deparaffinized with xylene, hydrated in a series of descending grades of ethanol, and then rinsed briefly with PBS for the primary antibodies; the sections were incubated overnight at 4°C with polyclonal anti- Runx2, COL I, OCN and DSP (Wuhan Boster Biological Technology, Wuhan, China).

Techniques: Immunohistochemical staining, Control

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Knockdown of eukaryotic translation initiation factor 3 subunit B inhibits cell proliferation and migration and promotes apoptosis by downregulating WNT signaling pathway in acute myeloid leukemia

doi:

Figure Lengend Snippet: EIF3B relative expression in human AML cell lines. EIF3B mRNA relative expression (A) and protein expression (B) were increased in AML-193, OCI-AML2, and KG-1 cell lines compared to human primary BMMC. The comparison of EIF3B mRNA relative expression between human AML cell lines and human primary BMMC was conducted using one-way ANOVA followed by Dunnett’s multiple comparisons test. P < 0.05 was considered significant. NS, non-significant; *P < 0.05, **P < 0.01, ***P < 0.001. EIF3B, eukaryotic translation initiation factor 3 subunit B; AML, acute myeloid leukemia; BMMC, bone marrow mononuclear cells.

Article Snippet: Cell culture Human AML cell lines AML-193, HL-60, OCI-AML2 and KG-1 were purchased from Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures (Braunschweig, Germany), AML-193 cells were cultured in 90% Iscove’s Modified Dulbecco’s Medium (Gibco, USA) and 10% fetal bovine serum (FBS) (Gibco, USA), and HL-60, OCI-AML2 and KG-1 cells were cultured in 90% Roswell Park Memorial Institute 1640 Medium (Gibco, USA) and 10% FBS (Gibco, USA) under 95% air and 5% CO 2 at 37°C.

Techniques: Expressing, Comparison

Journal: Development (Cambridge, England)

Article Title: Termination of cell-type specification gene programs by the miR-183 cluster determines the population sizes of low-threshold mechanosensitive neurons.

doi: 10.1242/dev.165613

Figure Lengend Snippet: Fig. 1. The population sizes of TRKB+ and TRKC+ neurons are altered in the P0 miRCKO mice. (A-C) The percentage of TRKB+ neurons was increased in the miRCKO mice. Immunostaining for TRKB on DRG sections of control Wnt1-Cre mice (A) and the miRCKO mice (B) as well as quantification of the percentage of TRKB+ neurons in L3-L5 ganglions (C, n=3, 4). (D) The number of total neurons (ISL1+) in L5 DRG was not altered in the miRCKO mice compared with controls (n=3, 4; not significant). (E-G) The percent of total TRKC neurons were decreased in the miRCKO mice. Double immunostaining for TRKC and RUNX3 on DRG sections of Wnt1-Cre mice (E) and miR CKO mice (F), arrow heads in E and F point to NF3 (TRKC+RUNX3-) neurons, inset are higher magnifications of areas outlined in E and F. (G) Quantification of the percentage of total TRKC, TRKC+RUNX3+ (not significant) and TRKC+RUNX3- neurons in L3-L5 ganglions (n=4, 4). Data shown in mean±s.e.m. and analyzed by t-test and P<0.05 is statistically significant. *P<0.05, **P<0.01. Scale bar =µ.

Article Snippet: The following primary antibodies were used: mouse antibodies against ISL1 (DSHB, USA, 1:100), SHOX2 (Santa Cruz, USA, 1:400), NFH (neurofilament, heavy polypeptide) (CloneN52; Sigma-aldrich, St. Louis, MO, USA, 1:500); rabbit antibodies against RUNX3 (gifts from Thomas Jessell, Columbia University Medical Center, 1:300), ISL1 (gifts from Thomas Jessell, Columbia University Medical Center, 1:250), NFH (Millipore, USA, 1:200), TRKA (Millipore, USA, 1:500), TRKC (Cell signaling, USA, 1:500), NECAB2 (Proteintech Europe, 1:1000), CALB1 (Millipore, USA, 1:500) and chicken-TRKB (kind gift from Louis F. Reichardt, 1:2000); goat antibodies against TRKA (R&D systems, Minneapolis, MN, USA, 1:500), TRKB (R&D systems, Minneapolis, MN, USA, 1:500), TRKC (R&D, 1:500), Ret (R&D, 1:100) and GFP (Abcam, USA, 1:500); Guinea pig antibodies against TLX3 (kind gift from Carmen Birchmeier).

Techniques: Immunostaining, Control, Double Immunostaining

Journal: International journal of molecular medicine

Article Title: Brain death induces the alteration of liver protein expression profiles in rabbits.

doi: 10.3892/ijmm.2014.1806

Figure Lengend Snippet: Figure 5. Re‑identification of altenation of runt‑related transcription factor 1 (RUNX1) proteins by immunohistochemistry and western blot analysis. (A) Representative images (x100) of immunohistochemical analysis of (a‑d) control samples and (e‑h) paired brain death groups. The protein expression of RUNX1 stained in the nucleus in each brain death group is clearly decreased as compared to the control group at 2, 4, 6 and 8 h after brain death. (B) Representative results of western blot analysis of paired brain death groups and control samples with β‑actin as an internal control. A significant decrease in a time‑dependent manner and compared with the control groups was observed for the brain death groups. *P<0.05 indicates statistical significance compared with the previous groups. △P<0.05 indicates statistical significance compared with the control groups.

Article Snippet: The membrane was then blocked with 5% non-fat dry milk overnight and probed with primary rabbit polyclonal antibody against RUNX1 (1:500, Boster Biological Engineering, Co., Ltd.).

Techniques: Immunohistochemistry, Western Blot, Immunohistochemical staining, Control, Expressing, Staining

Journal: International journal of molecular medicine

Article Title: Brain death induces the alteration of liver protein expression profiles in rabbits.

doi: 10.3892/ijmm.2014.1806

Figure Lengend Snippet: Figure 4. Identification of alteration of runt‑related transcription factor 1 (RUNX1) protein expression by MALDI‑TOF/TOF tandem mass spectrometry. Acquired spectra were searched against a Mascot search engine based on the Swiss‑Prot protein database. MS/MS spectrum of the precursor ion with m/z 2425.2 for peptide 335ILPPCTNASTGAALLNPSLPSQSDVVETEGSHSNSPTNMPPARLEEAVWRPY386 with corresponding peak values was identi fied as RUNX1. Inset is the Swiss‑Prot protein score from the Swiss‑Prot database.

Article Snippet: The membrane was then blocked with 5% non-fat dry milk overnight and probed with primary rabbit polyclonal antibody against RUNX1 (1:500, Boster Biological Engineering, Co., Ltd.).

Techniques: Expressing, Mass Spectrometry, Tandem Mass Spectroscopy