Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP modulates the STING–NFκB2–IL10 signaling pathway in CRC cells. Immunofluorescence staining showing the effects of MIIP knockdown and MIIP overexpression on dsDNA levels (A) and the distribution and expression of STING (B) in SW480 and SW620 cells. (C) Western blots showing the effects of MIIP knockdown and overexpression on STING, TRAF3, p-p100, and p52 levels. (D) ELISA results showing the effects of MIIP knockdown and overexpression on IL10 levels in the cell culture medium. (E and F) Effects of MIIP knockdown and/or STING knockdown on p52 expression (E) and IL10 levels in the cell culture medium (F). All data are presented as the means ± SDs ( n = 3). * P < 0.05, ** P < 0.01, and *** P < 0.001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included mouse anti-dsDNA (1:1000, ab270732; Abcam, Cambridge, MA, USA), rabbit anti-NFKB2/p52 (1:200, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-TMEM173/STING (1:200, 19851-1-AP; Proteintech, Wuhan, Hubei, China), and rabbit anti-IL-10 antibodies (1:100, 20850-1-AP; Proteintech, Wuhan, Hubei, China).

Techniques: Immunofluorescence, Staining, Knockdown, Over Expression, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP inhibits tumor growth and metastasis and M2 macrophage infiltration in a syngeneic CRC mouse model through the STING–NFκB2–IL10 axis. (A) Tumors in situ (indicated by green arrows) and liver metastatic nodules (indicated by black arrows) were observed in a syngeneic CRC mouse model. Statistics for the size of tumors in situ (B) and the number of metastatic foci (C). (D) Statistical analysis of IL10 levels in mouse blood. (E) Representative images of HE and IHC staining for SATB2, MIIP, STING, IL10, p52, and CD163 (green arrows) in tumor tissues from the different groups. The bar graphs show the percentages of high/low STING (F), IL-10 (G), and p52 (H) expression in the different groups. (I) Comparison of the number of CD163-positive cells among the different groups. All data are presented as the means ± SDs ( n = 3). ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included mouse anti-dsDNA (1:1000, ab270732; Abcam, Cambridge, MA, USA), rabbit anti-NFKB2/p52 (1:200, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-TMEM173/STING (1:200, 19851-1-AP; Proteintech, Wuhan, Hubei, China), and rabbit anti-IL-10 antibodies (1:100, 20850-1-AP; Proteintech, Wuhan, Hubei, China).

Techniques: In Situ, Immunohistochemistry, Expressing, Comparison

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP modulates the STING–NFκB2–IL10 signaling pathway in CRC cells. Immunofluorescence staining showing the effects of MIIP knockdown and MIIP overexpression on dsDNA levels (A) and the distribution and expression of STING (B) in SW480 and SW620 cells. (C) Western blots showing the effects of MIIP knockdown and overexpression on STING, TRAF3, p-p100, and p52 levels. (D) ELISA results showing the effects of MIIP knockdown and overexpression on IL10 levels in the cell culture medium. (E and F) Effects of MIIP knockdown and/or STING knockdown on p52 expression (E) and IL10 levels in the cell culture medium (F). All data are presented as the means ± SDs ( n = 3). * P < 0.05, ** P < 0.01, and *** P < 0.001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included rabbit anti-MIIP (1:1000, HPA044948; Sigma-Aldrich, St. Louis, MO, USA), rabbit anti-MIIP (1:1000, orb537083; Biorbyt, Cambridge, UK), rabbit anti-STING (1:2000, 19851-1-AP; Proteintech, Wuhan, Hubei, China), mouse anti-TRAF3 (1:1000, 66310-1-Ig; Proteintech, Wuhan, Hubei, China), rabbit anti-p52 (1:1000, 4882S; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-p52 (1:500, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-p-p100 (1:1000, 4810T; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-CD163 (1:1000, 68922; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-β-actin antibodies (1:1000, 3700S; Cell Signaling Technology, Danvers, MA, USA).

Techniques: Immunofluorescence, Staining, Knockdown, Over Expression, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP inhibits tumor growth and metastasis and M2 macrophage infiltration in a syngeneic CRC mouse model through the STING–NFκB2–IL10 axis. (A) Tumors in situ (indicated by green arrows) and liver metastatic nodules (indicated by black arrows) were observed in a syngeneic CRC mouse model. Statistics for the size of tumors in situ (B) and the number of metastatic foci (C). (D) Statistical analysis of IL10 levels in mouse blood. (E) Representative images of HE and IHC staining for SATB2, MIIP, STING, IL10, p52, and CD163 (green arrows) in tumor tissues from the different groups. The bar graphs show the percentages of high/low STING (F), IL-10 (G), and p52 (H) expression in the different groups. (I) Comparison of the number of CD163-positive cells among the different groups. All data are presented as the means ± SDs ( n = 3). ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included rabbit anti-MIIP (1:1000, HPA044948; Sigma-Aldrich, St. Louis, MO, USA), rabbit anti-MIIP (1:1000, orb537083; Biorbyt, Cambridge, UK), rabbit anti-STING (1:2000, 19851-1-AP; Proteintech, Wuhan, Hubei, China), mouse anti-TRAF3 (1:1000, 66310-1-Ig; Proteintech, Wuhan, Hubei, China), rabbit anti-p52 (1:1000, 4882S; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-p52 (1:500, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-p-p100 (1:1000, 4810T; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-CD163 (1:1000, 68922; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-β-actin antibodies (1:1000, 3700S; Cell Signaling Technology, Danvers, MA, USA).

Techniques: In Situ, Immunohistochemistry, Expressing, Comparison

Journal: bioRxiv

Article Title: The MUC1 extracellular domain and cytoplasmic tail play distinct roles during Salmonella invasion of enterocytes

doi: 10.1101/2025.10.15.682509

Figure Lengend Snippet: A) Number of DEGs in each cell line comparing Salmonella -infected cultures to their respective uninfected controls. B) Venn diagram of DEGs found in MUC1-WT, MUC1-ΔCT, and ΔMUC1 when comparing Salmonella -infected cultures to uninfected cultures. C) Heatmap displaying the 24 shared DEGs induced during Salmonella infection in the three genotypes. D) Heatmap displaying the 132 DEGs uniquely induced in MUC1-WT cultures but not MUC1-ΔCT and ΔMUC1 cultures during Salmonella infection. E) GSEA for the biological process using the profileR database of 132 DEGs uniquely found in MUC1-WT during Salmonella infection. F) Heatmap displaying DEGs related to the NFKB2 and RELB signaling pathway uniquely found in Salmonella -infected MUC1-WT cultures.

Article Snippet: Incubation with primary antibodies was performed overnight at 4°C or 1-2 hours at RT with either the α-MUC1-ED antibody 214D4 or 139H2 (1:1000), α-MUC1-CT antibody CT2 (1:1000, Thermo, MA5-11202), or the α-Actin antibody (1:5000; bs-0061R, Bioss), NFκB antibodies (RELA (D14E12, #8242), RELB (D7D7W, #10544), NFKB1 (D4P4D, #13586), NFKB2 (D7A9K, #37359), IκBα (L35A5, #4814), Cell Signaling, 1:1000) diluted in TSMT 1% BSA.

Techniques: Infection

Journal: Frontiers in Veterinary Science

Article Title: Se-methylselenocysteine inhibits inflammatory response in an LPS-stimulated chicken HD11 macrophage-like cell model through the NFKB2 pathway

doi: 10.3389/fvets.2024.1503436

Figure Lengend Snippet: Visualization of the Flaver’s result, take the NFKB2 gene set in SeMC+LPS/LPS gene list as an example. The results of the Flaver’s analysis were plotted by first sorting the genes by RDE (top-left panel) or weighted RANKs (lower panel) and then using a sliding window with a size of 0.02n to traverse from the highest value to the lowest value. The distribution of Jindex (light blue) and RDE (light yellow) in the window was then calculated. The term “Saverage” is used to denote the weighted value of gene set values, whereas “Laverage” represents the weighted values of gene list.

Article Snippet: The anti-NFKB2/p52 rabbit antibody (113157) was obtained from NovoPro (Shanghai, China).

Techniques:

Journal: Frontiers in Veterinary Science

Article Title: Se-methylselenocysteine inhibits inflammatory response in an LPS-stimulated chicken HD11 macrophage-like cell model through the NFKB2 pathway

doi: 10.3389/fvets.2024.1503436

Figure Lengend Snippet: Pathway for Se-methylselenocysteine inhibits intermediated inflation in a LPS-stimulated chicken HD11 macrophage-like cell model. The p52 is a analog of the amino-terminal half of p100, which is encoded by NFKB2. The p52 protein is devoid of the transcription activation domains and can function as a repressor of NF-κB-specific transcription. The p65 protein is encoded by the RELA gene, containing both DNA-binding domains and the transcription activation domains. These domains can server as transcription activation domain of the NF-κB complex.

Article Snippet: The anti-NFKB2/p52 rabbit antibody (113157) was obtained from NovoPro (Shanghai, China).

Techniques: Activation Assay, Binding Assay