Journal: Journal of cellular physiology

Article Title: Adhesion G-protein coupled receptor 56 is required for 3T3-L1 adipogenesis.

doi: 10.1002/jcp.29079

Figure Lengend Snippet: FIGURE 7 (a) Confocal images of Phalloidin staining of actin cytoskeleton in 3T3‐L1 and RM4.2.5.5 cells. Actin is stained with iFlour 488 conjugated Phalloidin (green). Merged images show both Phalloidin and DAPI (blue) stain. White arrows indicate regions selected for magnification shown in adjacent panels. The white size lines indicate scale bar of 20 μm or 10 μm. (b) Histogram showing quantitative analysis of Phalloidin stained confocal images of the indicated cell lines using the ImageJ software. Statistical analysis shows unpaired the Student's t test, **p ≤.01. DAPI, 4',6‐diamidino‐2‐ phenylindole [Color figure can be viewed atwileyonlinelibrary.com]

Article Snippet: Subsequently, membranes were washed in REVERTTM reversal solution and western blot analysis performed with antibodies to α‐GPR56 (Merck, H11), α‐PPARγ (C26H12), α‐C/EBP‐α (2295), α‐βACTIN (8H10D10), total β‐catenin (D10A8), active β‐catenin (D13A1; Cell Signaling Technologies®, Leiden, The Netherlands), or α‐AP‐2 (Santa Cruz Biotechnology Inc, C‐15) at 1:1,000 dilution.

Techniques: Staining, Software

Journal: Journal of cellular physiology

Article Title: Adhesion G-protein coupled receptor 56 is required for 3T3-L1 adipogenesis.

doi: 10.1002/jcp.29079

Figure Lengend Snippet: FIGURE 8 Model illustrating adipogenesis in Gpr56 + ve and −ve cells. Model shows the cell membrane lipid bilayer and Gpr56 transmembrane protein ( + ve Gpr56) indicated by a black line passing through membrane that is absent in Gpr56 −ve cells (−ve Gpr56). Chemical treatment of preadipocytes allows differentiation in the presence of Gpr56. The link between Gpr56 and + ve stimulation of adipogenesis is unknown (?) but involves induction of Pparγ2 and C/ebpα (1) and other cryptic processes (2). Differentiation is indicated by morphological change from spindle like preadipocyte fibroblast cells to round adipocytes (3). In the absence of Gpr56 the change from fibroblast to adipocyte cells is blocked (4) and cells remain fibroblast like. Sustained levels of the known Pparγ2 and adipogenesis inhibitor, active β‐Catenin, occur (5). Reduced cell proliferation, adhesion and actin cytoskeleton and changes in extracellular matrix (ECM) gene expression are all proposed to contribute to inhibition of adipogenesis via β‐Catenin dependent (6) and independent (7) mechanisms [Color figure can be viewed atwileyonlinelibrary.com]

Article Snippet: Subsequently, membranes were washed in REVERTTM reversal solution and western blot analysis performed with antibodies to α‐GPR56 (Merck, H11), α‐PPARγ (C26H12), α‐C/EBP‐α (2295), α‐βACTIN (8H10D10), total β‐catenin (D10A8), active β‐catenin (D13A1; Cell Signaling Technologies®, Leiden, The Netherlands), or α‐AP‐2 (Santa Cruz Biotechnology Inc, C‐15) at 1:1,000 dilution.

Techniques: Membrane, Gene Expression, Inhibition

Journal: Frontiers in Endocrinology

Article Title: Exploring the multifaceted antitumor activity of axitinib in lung carcinoids

doi: 10.3389/fendo.2024.1433707

Figure Lengend Snippet: Examination of cell cycle arrest by Western blot analysis. (A, C) Representative Western blot images for each target in LC cell lines. Histograms (B, D) summarize the change in expression of one target after 6 days of treatment with AXI in each LC cell line. The analyzed targets are phospho-Chk1(Ser345) (P-ChK1), total Chk1 (Chk1) (A, B) , phospho-p53 (Ser15) (pp53) and p21 Waf1/Cip1 (C, D) . βActin is used as a loading control. Values represent the mean ± S.E.M. of a minimum of three independent experiments. The significance is calculated by performing an unpaired t-test between the control and the treated group: *p<0.05; ** p<0.01; ***p<0.001.

Article Snippet: Antibodies, all diluted 1:1000 and provided by Cell Signaling Technology (Danvers, MA, USA), were as follow: Caspase-3 (D3R6Y) Rabbit Ab; Poly(ADP-ribose)polymerase (PARP) (46D11) Rabbit Ab; Phospho-Chk1(Ser345) (133D3) Rabbit mAb; Chk1 (2G1D5) Mouse mAb; p21 WAF1/Cip1 (12D1) Rabbit mAb; Phospho-p53 (Ser15) (16G8) Mouse mAb; Cyclin-B1 Rabbit Ab; Phospho-Histone H2A.X (Ser139) (D7T2V) Mouse mAb (γ-H2AX); Nuclear factor erythroid 2-related factor 2 (Nrf2) (D1Z9C) XP Rabbit mAb; Kelch-like ECH-associated protein 1 (Keap1) (D6B12) Rabbit mAb; and βActin (8H10D10) mouse mAb.

Techniques: Western Blot, Expressing, Control