Journal: Breast cancer research : BCR

Article Title: PTHrP intracrine actions divergently influence breast cancer growth through p27 and LIFR.

doi: 10.1186/s13058-024-01791-z

Figure Lengend Snippet: Fig. 4 PTHrP differentially regulates p27 through LIFR in breast cancer cells. (A) Immunofluorescence staining and quantification of LIFR in primary tumors from mice inoculated with MSCV, FLSEC, DNLS, or DNLS + CTERM cells. All panels = 40X and scale bars = 50 μm. (B) Western blot analysis of p27, pERK, ERK, p-p38, p38 and tubulin (loading control) protein levels in MSCV, FLSEC, DNLS, or DNLS + CTERM cells treated with vehicle (DMSO) or LIFR inhibitor (EC359, 50nM or 100nM) for 24 h. Densitometry for western blot analysis of (C) p27, (D) pERK/ERK and (E) p-p38/p38 described in (B). (A) **p < 0.01 vs. DNLS by unpaired t-test. (C) *p < 0.05 vs. DNLS by unpaired t-test or *p < 0.05 vs. MSCV by one-way ANOVA with multiple comparisons. (D & E) *p < 0.05 vs. MSCV by one-way ANOVA with multiple comparisons or *p < 0.05, **p < 0.01, ***p < 0.001 versus vehicle by two-way ANOVA. Graphs represent mean ± SEM

Article Snippet: The following day, cells were treated with EC359, a leukemia inhibitory factor receptor (LIFR) inhibitor (50nM or 100nM; MedChemExpress; Catalog No. HY-1,201,420) or vehicle (0.1% dimethyl sulfoxide, DMSO) for 1, 6, or 24 h in full-serum media.

Techniques: Immunofluorescence, Staining, Western Blot, Control

Journal: Breast cancer research : BCR

Article Title: PTHrP intracrine actions divergently influence breast cancer growth through p27 and LIFR.

doi: 10.1186/s13058-024-01791-z

Figure Lengend Snippet: Fig. 6 Model of PTHrP domain-specific actions in breast cancer progression and bone colonization. In the primary breast site (top left panel, left of ar rows), PTHrP lacking the NLS and C-terminal domain decreases tumor cell proliferation through p27 induction driven by the tumor suppressor leukemia inhibitory factor receptor (LIFR). PTHrP lacking the NLS and C-terminal domain also preferentially induces p38 phosphorylation and signaling to inhibit cell cycling downstream of LIFR activation. In the breast, truncated PTHrP lacking the NLS alone (top left panel, right of arrows) downregulates LIFR expression (denoted by transparent coloring) and prevents induction of p27 expression and activation of p38 signaling (denoted by dashed arrows, dot ted outlines and transparent coloring) to drive cell proliferation and tumor growth. In bone disseminated tumor cells (bottom panel), LIFR expression is downregulated and the induction of p27 by PTHrP lacking the NLS and C-terminal domain persists, but is not sufficient to repress metastatic outgrowth (denoted by dashed inhibitor line), in contrast to the primary tumor. In the bone, tumor cells expressing PTHrP peptides lacking the NLS or NLS and C- terminal domain readily proliferate into metastatic tumors. Image created with Biorender.com

Article Snippet: The following day, cells were treated with EC359, a leukemia inhibitory factor receptor (LIFR) inhibitor (50nM or 100nM; MedChemExpress; Catalog No. HY-1,201,420) or vehicle (0.1% dimethyl sulfoxide, DMSO) for 1, 6, or 24 h in full-serum media.

Techniques: Phospho-proteomics, Activation Assay, Expressing

Journal: iScience

Article Title: MCM7 supports the stemness of bladder cancer stem-like cells by enhancing autophagic flux

doi: 10.1016/j.isci.2022.105029

Figure Lengend Snippet:

Article Snippet: LIF , MedChemExpress , Cat. # HY-P73276.

Techniques: Recombinant, MTS Assay, Protein Concentration, Software

Journal: Journal of biomolecular screening

Article Title: Discovery of Enhancers of the Secretion of Leukemia Inhibitory Factor for the Treatment of Multiple Sclerosis.

doi: 10.1177/1087057116638821

Figure Lengend Snippet: Figure 4. Correlation across assays of 200 selected compounds from HTS. (A) LIF production activation fold in U87-MG cells, AlphaScreen vs. ELISA (r2 = 0.753). (B) LIF production activation fold in AlphaScreen assay format, U87-MG vs. WM-115 cells (r2 = 0.347). Shape by chemical clustering: circles, cluster 3; squares, cluster 5; triangle, other cluster.

Article Snippet: Rat LIF ELISA kit was from Cusabio (Wuhan, China).

Techniques: Activation Assay, Amplified Luminescent Proximity Homogenous Assay, Enzyme-linked Immunosorbent Assay

Journal: Veterinary Research

Article Title: Cytokine response to the RSV antigen delivered by dendritic cell-directed vaccination in congenic chicken lines

doi: 10.1186/s13567-017-0423-8

Figure Lengend Snippet: Specific binding of anti-chCD205 and internalization of antigen delivery complex. A The recombinant parts of chicken CD205 receptor used for monoclonal antibody preparation and the monoclonal antibody characterization. The CD205B and CD205F proteins were purified from inclusion bodies on DEAE Sepharose and separated on Tris-Tricine polyacrylamide gel stained by Coomassie blue (left). Monoclonal mouse anti-CD205 antibodies were analyzed using Western blots. Results of two representative detections of monoclonal anti-CD205 specific for CD205B or CD205F are shown. B CD205 expression on leukocytes. Splenocytes and peripheral leukocytes were stained with anti-chicken CD205 antibody and antibodies recognizing each of the indicated antigens. Histograms represent the CD205 fluorescence for cells gated for positive expression of the markers indicated at the left. The results of one representative of three experiments are shown. C Median fluorescence intensity (MFI) of CD205 stained cells and standard deviation. D Internalization of streptavidin-CD205-FITC complex by chicken primary splenocytes one (left) and two (right) hours of incubation in different temperatures. Dotted line plot non-labelled cells (biot—control IgG); Black line plot—FITC labelled cells incubated in 4 °C; Gray line plot—FITC labelled cells incubated in 40 °C.

Article Snippet: For each cytokine, the recombinant protein, capture antibody and detection antibody were obtained as complete kit (Kingfisher Biotech, USA; cat.nos.

Techniques: Binding Assay, Recombinant, Purification, Staining, Western Blot, Expressing, Fluorescence, Standard Deviation, Incubation, Control