Journal: Cardiovascular research

Article Title: Growth hormone releasing peptide (ghrelin) is synthesized and secreted by cardiomyocytes.

doi: 10.1016/j.cardiores.2004.01.024

Figure Lengend Snippet: Fig. 1. RT-PCR results showing expression of preproghrelin gene in HL-1 cardiomyocytes (Panel A, lanes 3–6) and of ghrelin gene in human endocardium and myocardium (Panel B, lanes 3 and 4). Positive controls: expression of the target gene in mouse or human stomach (Panel A lane 1 and Panel B lane 2, respectively), and of GAPDH (Panel A lanes 7–11, and Panel B lanes 5–7). Negative controls: Panel A lanes 12 and 13, and Panel B lanes 8 and 9. Molecular weight markers: Panel A lane 2 and Panel B lane 1. (A) Bottom panel: autoradiographs of Southern blots of lanes 1–6 of the upper panel.

Article Snippet: Sections were successively incubated in (1) goat polyclonal anti-ghrelin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) at a dilution of 1:500 (1 h); (2) 3% hydrogen peroxide (Merck, Darmstadt, Germany) to block endogenous peroxidase (10 min); (3) biotinylated donkey anti-goat Ig (Santa Cruz) diluted to 1:100 (30 min); (4) streptavidin–biotin–peroxidase complex (Duet kit, Dakopatts, Glostrup, Denmark), prepared 30 min before use following the manufacturer’s protocol (30 min); and (5) 3,3V-diaminobenzidine tetrahydrochloride (DAB) solution, prepared by dissolving a DAB-buffer tablet (Merck) in 10 ml of distilled water (10 min).

Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Molecular Weight

Journal: Cardiovascular research

Article Title: Growth hormone releasing peptide (ghrelin) is synthesized and secreted by cardiomyocytes.

doi: 10.1016/j.cardiores.2004.01.024

Figure Lengend Snippet: Fig. 2. Ghrelin immunoreactivity in human (g) and HL-1 (e) cardiomyocytes, in human (l) and mouse (j) heart tissue, and, as positive controls, in human (c) and mouse (a) stomach (where immunoreactivity was found in neuroendocrine cells of gastric glands). For murine and human stomach, murine and human heart and HL-1 cells, negative controls were run with pre-saturated primary antibody (b, d, k, m and f, respectively), and for human cardiomyocyte primary cultures by replacing primary antibody with TBS (i). Human cardiomyocyte primary cultures were also stained by anti- MHC antibody (h). (b, d, i, k, m) Nomarsky differential interference contrast. Objective magnifications: c and k, 20; a, b, d, j, l and m, 40; e, f, g, h, i, 60.

Article Snippet: Sections were successively incubated in (1) goat polyclonal anti-ghrelin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) at a dilution of 1:500 (1 h); (2) 3% hydrogen peroxide (Merck, Darmstadt, Germany) to block endogenous peroxidase (10 min); (3) biotinylated donkey anti-goat Ig (Santa Cruz) diluted to 1:100 (30 min); (4) streptavidin–biotin–peroxidase complex (Duet kit, Dakopatts, Glostrup, Denmark), prepared 30 min before use following the manufacturer’s protocol (30 min); and (5) 3,3V-diaminobenzidine tetrahydrochloride (DAB) solution, prepared by dissolving a DAB-buffer tablet (Merck) in 10 ml of distilled water (10 min).

Techniques: Staining

Journal: American journal of physiology. Gastrointestinal and liver physiology

Article Title: Ghrelin receptors in rat and human nodose ganglia: putative role in regulating CB-1 and MCH receptor abundance.

doi: 10.1152/ajpgi.00543.2005

Figure Lengend Snippet: Fig. 6. RT-PCR indicates that ghrelin prevents food-induced downregulation of CB-1 (A), MCH-1 (B), and MCH (C) expression in rat nodose ganglia. Lanes 1–3, rats fed ad libitum: lane 1, control; lane 2, 5 h after administration of vehicle; and lane 3, 5 h after administration of ghrelin. Lanes 4–6, rats fasted for 48 h: lane 4, control; lane 5, refed for 5 h with vehicle at the time of refeeding; and lane 6, refed for 5 h with ghrelin (4 nmol/kg ip) at the time of refeeding. Lane 7 shows the calibration marker 50 DNA ladder. Samples were pooled from nodose ganglia of 6–7 rats; representative results are shown from 2–4 experiments. The predicted size of the CB-1 product was 330 bp, MCH-1 product 260 bp, and MCH product 333 bp.

Article Snippet: Some fasted rats were then refed for up to 5 or 16 h; others received rat ghrelin (Tocris Bioscience; Avonmouth, UK) by intraperitoneal injection (4 nmol/kg) or PBS and were killed up to 5 or 16 h later.

Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Control, Marker

Journal: American journal of physiology. Gastrointestinal and liver physiology

Article Title: Ghrelin receptors in rat and human nodose ganglia: putative role in regulating CB-1 and MCH receptor abundance.

doi: 10.1152/ajpgi.00543.2005

Figure Lengend Snippet: Fig. 7. Ghrelin attenuates the effect of food in decreasing expression of the CB-1 receptor, MCH-1R, and MCH in vagal afferent neurons. A: CB-1 immunoreactivity in neurons of nodose ganglia of rats fasted for 48 h; B: decreased CB-1 abundance 5 h after refeeding of rats fasted for 48 h, which was inhibited by the administration of ghrelin (4 nmol/kg ip) at the time of refeeding (C). D –I: similar data for MCH-1R (D–F) and MCH (G–I) expression. The expression of CB-1 is barely detectable in nodose neurons of rats ad libitum and those receiving ghrelin 5 (J) or 16 h (K) earlier or vehicle (L). M–R: similar data for MCH-1R expression (M–O) and MCH expression (P–R). Representative results from 4–5 rats in each group are shown. Scale bars 25 m.

Article Snippet: Some fasted rats were then refed for up to 5 or 16 h; others received rat ghrelin (Tocris Bioscience; Avonmouth, UK) by intraperitoneal injection (4 nmol/kg) or PBS and were killed up to 5 or 16 h later.

Techniques: Expressing

Journal: Food & Nutrition Research

Article Title: A thermogenic botanical composition containing Citrus aurantifolia fruit rind and Theobroma cacao seed extracts improves body composition in overweight adults: a clinical investigation

doi: 10.29219/fnr.v69.12159

Figure Lengend Snippet: CL19183 modulates serum adiponectin, ghrelin, and total glucagon-like peptide-1 (GLP-1) levels. Each bar presents as mean ± SD of serum adiponectin (A), ghrelin (B), and total GLP-1 (C) levels in the placebo ( n = 60) and CL19183 ( n = 60) supplemented participants at baseline, 8th, and 16th weeks of the study. * and # indicate significance ( p < 0.05) in the ANCOVA model (vs. baseline) and the ANOVA model (vs. placebo), respectively.

Article Snippet: Adiponectin assay kit (Cat#DRP300) was procured from R&D Systems, Minneapolis, MN, and ghrelin (Cat# E-EL-H1919) and GLP-1 (Cat# E-EL-H6025) assay kits were procured from Elabscience, Houston, TX.

Techniques:

Journal: International journal of molecular sciences

Article Title: Maternal Exposure to Low-Dose BDE-47 Induced Weight Gain and Impaired Insulin Sensitivity in the Offspring.

doi: 10.3390/ijms25168620

Figure Lengend Snippet: Figure 2. Maternal BDE-47 exposure and expression of key genes in adipose tissue and liver and serum adipokines in the female offspring. (A) The mRNA expression levels of selected target genes investigated in adipose tissue and (B) liver of 12-week-old female offspring. (C) Levels of leptin, adiponectin, resistin, and ghrelin measured in serum of female offspring. Data are expressed as mean ± SEM, n ≥5. Significant differences were derived by Mann–Whitney test with * p < 0.05.

Article Snippet: Adiponectin, leptin, resistin, and acetylated ghrelin serum concentrations were determined by ELISA using mouse standards according to the manufacturer’s guidelines (mouse adiponectin, leptin, resistin ELISA; R&D Systems, Minneapolis, MN, USA), (mouse/rat acylated ghrelin ELISA; BioVendor, Karasek, Czech Republic).

Techniques: Expressing, Derivative Assay, MANN-WHITNEY