Journal: Stem cell research & therapy

Article Title: VEGF-B-mediated myofiber types involved in high-fat diet-induced hyperglycemia through PKA-NFATs signaling pathway.

doi: 10.1186/s13287-025-04455-7

Figure Lengend Snippet: Fig. 8 Schematic diagram of this work. (A) VEGF-B acts as a bridge between skeletal muscle type and high-fat diet-induced hyperglycemia in vivo. (B) Matched with high-fat diet-induced hyperglycemia accompanied by increased content of slow-twitch type I fibers within the skeletal muscle of VEGF-B deficient high-fat diet-fed mice in vivo, VEGF-B186, which was continuously administered at a single high dosage in vitro, inhibited myoblast differentia tion/fusion and myofiber formation and glucose utilization via the PKA-NFATs signaling pathway

Article Snippet: The primary antibodies used were as follows: MyHC (1:3000, sc-376157, Santa Cruz, Dallas, Texas, USA), α-tubulin (1:10000, YM3035, Immunoway®, Newark, USA), PKA α/β/γ cat (1:1000, sc-365615, Santa Cruz, Dallas, Texas, USA), PKA α cat (1:3000, sc-28315, Santa Cruz, Dallas, Texas, USA), PKA γ cat (1:1000, sc-514087, Santa Cruz, Dallas, Texas, USA), PKA Iα reg (1:1000, sc-136231, Santa Cruz, Dallas, Texas, USA), PKA IIα reg (1:3000, sc-136262, Santa Cruz, Dallas, Texas, USA), PKA Iβ reg (1:2000, sc-100414, Santa Cruz, Dallas, Texas, USA), GLUT4 (1:2000, YT5523, Immunoway®, Newark, USA), NOQ (1:1000, ab11083, Abcam Corporation, Cambridge, England), My32 (1:1000, ab51263, Abcam Corporation, Cambridge, England), Nfatc1 (1:1000, ab25916, Abcam Corporation, Cambridge, England), Nfatc2 (1:1000, 5861T, Cell Signaling Technology Inc., Danvers, Massachusetts, USA), P-Nfatc1 (1:1000, ab183023, Abcam Corporation, Cambridge, England), P-Nfatc2 (1:1000, ab200819, Abcam Corporation, Cambridge, England), and Lamin B1 (1:5000, P60054, Abmart Shanghai Co., Ltd., Shanghai, China).

Techniques: In Vivo, In Vitro

Journal: Journal of Virology

Article Title: Small Hepatitis B Virus Surface Antigen Promotes Hepatic Gluconeogenesis via Enhancing Glucagon/cAMP/Protein Kinase A/CREB Signaling

doi: 10.1128/jvi.01020-22

Figure Lengend Snippet: SHBs elevates cAMP levels by regulating AC. (A) cAMP levels in the liver of LSL-SHBs and LSL-SHBs/Alb-Cre mice fasted for 16 h ( n = 6 to 7 mice/group). (B to E) Effect of AC inhibitor SQ22536 or PDE inhibitor IBMX on cAMP levels (B), glucose production (C), gluconeogenic gene expression (D), CREB phosphorylation, and PKA activity (E) in Ad-SHBs-infected mouse primary hepatocytes and in Huh7-SHBs cells. Cells were treated with SQ22536 (500 μM) or IBMX (500 μM) for 1 h and then with glucagon (100 nM) stimulation or FSK (10 μM) for 15 min (B), 6 h (C), 2 h (D) and 30 min (E). (F) Huh7 cells were transfected with pcDNA 3.1-SHBs-Flag for 48 h, and then co-IP assays were performed to determine the interaction between SHBs and PKA subunits. The immunoprecipitated complexes with anti-Flag antibody were subjected to immunoblotting with PKA Cα, PKA RIα/β, PKA RIIα, or PKA RIIβ antibody. The glycosylated (gp) and nonglycosylated (p) forms of SHBs were indicated. Arrowhead points to phospho-CREB. Data are presented as means ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ns, no significant difference.

Article Snippet: The primary antibodies used in this studies included anti-Flag (F1804; Sigma-Aldrich), anti-SHBs (DMABT-51328MH; Creative-Diagnostics, Shirley, NY), anti-CREB (9197S; Cell Signaling Technology [CST], Beverly, MA), anti-phospho-CREB (9198S; CST), anti-phospho-PKA substrate (9624S; CST), anti-PKA Cα (4782S; CST), anti-PKA RIα/β (3927; CST), anti-β-Actin (3700; CST), anti-PKA RIIα (MAB8000; R&D Systems, Minneapolis, MN), anti-PKA RIIβ (PAB18374; Abnova Inc., Walnut, CA), and anti-AC1 (LS-C314759; LifeSpan Biosciences, Seattle, WA).

Techniques: Gene Expression, Phospho-proteomics, Activity Assay, Infection, Transfection, Co-Immunoprecipitation Assay, Immunoprecipitation, Western Blot