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Image Search Results
Journal: bioRxiv
Article Title: Fatty acid binding proteins shape the cellular response to activation of the glucocorticoid receptor
doi: 10.1101/2021.07.02.450968
Figure Lengend Snippet: GRE-transcriptional activity of GR in the absence or presence of FABP1, FABP2, FABP3, FABP4 or FABP5 in response to vehicle control or increasing concentrations of (A) hydrocortisone (B) dexamethasone or (C) prednisolone, was assessed using a reporter gene in COS-7 cells after 24 h treatment (n=3). (D) Expression of the GR in naïve COS-7 cells or following transfection with GR determined by immunoblotting. Transcriptional activity of the endogenous or transfected GR in the presence of FABP4 in response to (E) dexamethasone or (F) prednisolone (n=3). (G) FABP translocation to the nucleus in COS-7 cells transfected with GR and GFP-FABP1 or GFP-FABP4 following 24 h treatment with vehicle or an EC 80 concentration of hydrocortisone, dexamethasone or prednisolone (n=3). Data are mean ± SEM from n independent experiments, as stated. For concentration-response curves, symbols show means and error bars, S.E.M. *** p<0.001, two-way ANOVA with Sidak’s multiple comparison test. For bar graphs, bars show the mean, error bars the S.E.M. and symbols show the independent data points for each experiment. *** p<0.001, two-way ANOVA with Dunnett’s multiple comparisons test.
Article Snippet: Immunoblotting used primary antibodies recognising FABP1 (Abcam (AB76812; rabbit, 1:300), FABP2 (gift from Dr Satoshi Kaiura, Dainippon Sumi-tomo Pharma Co. Ltd., Osaka, Japan; mouse; 1:400),
Techniques: Activity Assay, Control, Expressing, Transfection, Western Blot, Translocation Assay, Concentration Assay, Comparison
Journal: Cell Discovery
Article Title: Luminal hormone-responsive cells tune the regenerative remodeling of mammary glands in large mammals
doi: 10.1038/s41421-025-00848-3
Figure Lengend Snippet: a UMAP plot displaying 14 identified cell types within the goat mammary glands. Cells are annotated and colored by type. Subsets of cell types including luminal, basal, fibroblast, immune, endothelial cell are labeled. b The percentages of −4W (red) and +1 W (blue) cells in each cell type are shown in a UMAP plot. c UMAP plots showing the expression of selected marker genes in four luminal subtypes. d Pseudotemporal trajectory analysis of scRNA-seq data of luminal secretory cells is shown in a UMAP plot. e Changes in the proportion of LumSecP and LumSec cells in luminal cell types were identified by scRNA-seq data at −4W and +1 W. n = 3 goats per group. f Representative images of tissue immunofluorescence staining for ALDH1A3 (red), KRT18 (green), and DAPI at −4W and +1 W. Scale bars, 50 μm. g Bar plots exhibiting the percentage of ALDH1A3-positive cells in luminal cells (labeled by KRT18) in f . n = 15 sections per group. h Representative images of tissue immunofluorescence staining for FABP3 (red), KRT18 (green), and DAPI at −4W and +1 W. Scale bars, 50 μm. i Bar plots exhibiting the percentage of FABP3-positive cells in luminal cells (labeled by KRT18) in h . n = 20 sections per group. The data are presented as the mean ± SEM. The P values of two-sided Student’s t -tests are shown in e , g , i .
Article Snippet: For immunofluorescence staining, goat mammary tissues were stained with primary antibodies against ALDH1A3 (#25167-1-AP, Proteintech),
Techniques: Labeling, Expressing, Marker, Immunofluorescence, Staining
Journal: Cell Discovery
Article Title: Luminal hormone-responsive cells tune the regenerative remodeling of mammary glands in large mammals
doi: 10.1038/s41421-025-00848-3
Figure Lengend Snippet: a Relative proportions of LumHR cells in total luminal cells identified by scRNA-seq data at −4W and +1 W. n = 3 goats per group. b , c Bar plots exhibiting the percentage of PGR - and ESR1 -positive cells within luminal cells in scRNA-seq data. n = 3 goats per group. d Representative images of immunofluorescence staining for PR (red), KRT18 (green), and DAPI (blue). Scale bars, 50 μm. e Bar plots exhibiting the percentage of PR-positive cells in luminal cells (labeled by KRT18) in ( d ). n = 5 goats per group. f Representative images of immunofluorescence staining for ER (red), KRT18 (green), and DAPI (blue). Scale bars, 50 μm. g Bar plots exhibiting the percentage of ER-positive cells in luminal cells (labeled by KRT18) in ( f ). n = 5 goats. h Violin plot showing the specific expression of PRLR in LumHR cells by scRNA-seq. i Heatmap displaying the transcriptional level of indicated genes related to milk protein and luminal differentiation in the goat mammary organoids ( n = 3 biological replicates) treated with or without prolactin and in the mammary tissue at −4W (non-lactation) and +1 W (lactation). n = 3 goats for tissues. j Proportions of luminal cell types in goat mammary organoids incubated with or without prolactin predicted by CIBERSORTx deconvolution. n = 3 biological replicates. k Representative images of immunofluorescence staining for ALDH1A3 (red), KRT18 (green), and DAPI in mammary organoids incubated with or without prolactin. Scale bars, 10 μm. l Bar plots exhibiting the percentage of ALDH1A3-positive cells in luminal cells (labeled by KRT18) in ( k ). n = 14 domes in the control group and n = 10 domes in the prolactin treated group. m Representative images of immunofluorescence staining for FABP3 (red), KRT18 (green) and DAPI in mammary organoids incubated with or without prolactin. Scale bars, 10 μm. n Bar plots exhibiting the percentage of FABP3-positive cells in luminal cells (labeled by KRT18) in ( m ). n = 6 domes in the control group and n = 7 domes in the prolactin-treated group. The data are presented as the mean ± SEM. The P values of two-sided Student’s t -tests are shown in ( a – c , e , g , j , l , n ).
Article Snippet: For immunofluorescence staining, goat mammary tissues were stained with primary antibodies against ALDH1A3 (#25167-1-AP, Proteintech),
Techniques: Immunofluorescence, Staining, Labeling, Expressing, Incubation, Control
Journal: Cell Discovery
Article Title: Luminal hormone-responsive cells tune the regenerative remodeling of mammary glands in large mammals
doi: 10.1038/s41421-025-00848-3
Figure Lengend Snippet: a Schematic illustration of targeted ablation of LumHR cells using the prlr -promoter to drive expression of DTA. b Experimental setup used in AAV intraductally injected mammary gland of ROSA-DTA +/ − mice under RR. c Whole-mount staining with carmine alum of mammary glands from ROSA-DTA +/ − mice (lactation day 2) intraductally injected with AAV-pPrlr-Cre or AAV-Control . Scale bars, 4 mm (top) and 500 μm (bottom). d , e Immunohistochemical staining and quantification of ER-positive luminal cells in mammary glands intraductally injected with AAV-pPrlr-Cre or AAV-Control. n = 3 mice per group. Scale bars, 50 μm. f , g Immunohistochemical staining and quantification of PR-positive luminal cells in mammary glands intraductally injected with AAV-pPrlr-Cre or AAV-Control . n = 3 mice per group. Scale bars, 50 μm. h , i Immunohistochemical staining and quantification of β-casein-positive alveoli number per mm 2 in mammary glands intraductally injected with AAV-pPrlr-Cre or AAV-Control . n = 3 mice per group. Scale bars, 50 μm. j Representative images of immunofluorescence staining for FABP3 (red), KRT18 (green), and DAPI in mammary glands intraductally injected with AAV-pPrlr-Cre or AAV-Control . Scale bars, 50 μm. k Bar plots exhibiting the percentage of FABP3-positive cells in luminal cells (labeled by KRT18) in j . n = 3 mice per group. l Representative images of immunofluorescence staining for ALDH1A3 (red), KRT18 (green), and DAPI in mammary glands intraductally injected with AAV-pPrlr-Cre or AAV-Contro l. Scale bars, 50 μm. m Bar plots exhibiting the percentage of FABP3-positive cells in luminal cells (labeled by KRT18) in ( l ). n = 3 mice per group. The data are presented as the mean ± SEM. The P values of two-sided Student’s t -tests are shown in d , g , i , l , m .
Article Snippet: For immunofluorescence staining, goat mammary tissues were stained with primary antibodies against ALDH1A3 (#25167-1-AP, Proteintech),
Techniques: Expressing, Injection, Staining, Control, Immunohistochemical staining, Immunofluorescence, Labeling
Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research
Article Title: Protective Effects of Dexmedetomidine and Oxycodone in Patients Undergoing Limb Ischemia-Reperfusion
doi: 10.12659/MSM.918261
Figure Lengend Snippet: Perioperative variables of I/R and immune parameters.
Article Snippet: For quantification the serum concentration by enzyme-linked immunosorbent assay (ELISA), commercially available ELISA kits for measuring human tumor necrosis factor-α (TNF-α, Proteintech), interleukin-6 (IL-6, Proteintech), brain-derived neurotrophic factor (BDNF, Proteintech), fatty acid binding
Techniques:
Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research
Article Title: Protective Effects of Dexmedetomidine and Oxycodone in Patients Undergoing Limb Ischemia-Reperfusion
doi: 10.12659/MSM.918261
Figure Lengend Snippet: Plasma FABP3 ( A ), ET-1 ( B ), and BDNF ( C ) levels. The serum concentration of fatty acid binding protein 3 (FABP3), endothelin-1 (ET-1), and brain-derived neurotrophic factor (BDNF) were measured before anesthesia (T0) and at 30 min (T8) and 6 h after tourniquet release (T9). Sham – control (ischemia-reperfusion, I/R) group; Dex – dexmedetomidine group; Oxy – oxycodone group. Data are expressed as mean±SD. + P<0.05 vs. T0; * P<0.05 vs. sham; # P<0.05 vs. Dex.
Article Snippet: For quantification the serum concentration by enzyme-linked immunosorbent assay (ELISA), commercially available ELISA kits for measuring human tumor necrosis factor-α (TNF-α, Proteintech), interleukin-6 (IL-6, Proteintech), brain-derived neurotrophic factor (BDNF, Proteintech), fatty acid binding
Techniques: Concentration Assay, Binding Assay, Derivative Assay, Control
Journal: Genes & Nutrition
Article Title: Mechanism of continuous high temperature affecting growth performance, meat quality, and muscle biochemical properties of finishing pigs
doi: 10.1186/s12263-019-0643-9
Figure Lengend Snippet: Primer sequences
Article Snippet: All primary antibodies were raised in rabbits and were suitable for detecting specific porcine proteins: DECR1(sc-393473, Santa Cruz Biotechnology, Dallas, TX),
Techniques: Sequencing
Journal: Genes & Nutrition
Article Title: Mechanism of continuous high temperature affecting growth performance, meat quality, and muscle biochemical properties of finishing pigs
doi: 10.1186/s12263-019-0643-9
Figure Lengend Snippet: Differentially expressed genes related to energy metabolism, muscle structure, and stress response
Article Snippet: All primary antibodies were raised in rabbits and were suitable for detecting specific porcine proteins: DECR1(sc-393473, Santa Cruz Biotechnology, Dallas, TX),
Techniques: Binding Assay
Journal: Genes & Nutrition
Article Title: Mechanism of continuous high temperature affecting growth performance, meat quality, and muscle biochemical properties of finishing pigs
doi: 10.1186/s12263-019-0643-9
Figure Lengend Snippet: Significant KEGG pathway analysis
Article Snippet: All primary antibodies were raised in rabbits and were suitable for detecting specific porcine proteins: DECR1(sc-393473, Santa Cruz Biotechnology, Dallas, TX),
Techniques: Migration, Infection, Starch
Journal: Genes & Nutrition
Article Title: Mechanism of continuous high temperature affecting growth performance, meat quality, and muscle biochemical properties of finishing pigs
doi: 10.1186/s12263-019-0643-9
Figure Lengend Snippet: Western blots for a selection of differentially expressed proteins. Targeted protein DECR1, FABP3, HSPA1L, LPIN1, PFKM, TNNT3, TNNI1, PPARGC-1, MSTN, FASN, and PCK1, with GAPDH as a reference protein. a Representative sample from each treatment fractionated by SDS-PAGE, blotted and then detected with specific antibodies. b Semi-quantification of protein content from scans of band, ( n = 4 pools of two pigs per treatment)
Article Snippet: All primary antibodies were raised in rabbits and were suitable for detecting specific porcine proteins: DECR1(sc-393473, Santa Cruz Biotechnology, Dallas, TX),
Techniques: Western Blot, Selection, SDS Page
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: ( A ) Structure of heart-type fatty acid-binding protein (FABP3, PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay, Sequencing, Residue
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Toxicity of C16:0-carnitine in PANC-1 cells after 4 h of incubation in the presence or in the absence of 60 μM heart-type fatty acid-binding protein (FABP3) in the cell media. Data are shown as the mean ± SEM of 3 independent experiments in at least 6 technical replicates. * indicates a significant difference compared to the cells not subjected to FABP3 treatment at the respective C16:0-carnitine concentration.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Incubation, Binding Assay, Concentration Assay
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Toxicity of C16:0-carnitine in native and heart-type fatty acid-binding protein (FABP3)-overexpressing PANC-1 cells after 4 h of incubation. Data are shown as the mean ± SEM of 3 independent experiments in at least 6 technical replicates. * indicates a significant difference compared to the native cells at the respective concentration of C16:0-carnitine.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay, Incubation, Concentration Assay
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Superposition of the 2D 1 H- 15 N HSQC spectra for ( A ) heart-type fatty acid-binding protein (FABP3)-C18:1(n-9) t and ( B ) FABP3-C18:1(n-9) t -carnitine complex in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). The spectrum of apo-FABP3—in blue, spectrum of the FABP3-ligand complex—in red. Residues with chemical shift perturbations (CSPs) larger than the mean plus one standard deviation are assigned and black arrows show the shift of the corresponding crosspeak. * marks the crosspeaks that have disappeared upon binding of the acylcarnitines (ACs).
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay, Standard Deviation
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Mapping of the chemical shift perturbations (CSPs) caused by binding of ( A ) C8:0, ( B ) C12:0, ( C ) C14:0, ( D ) C16:0, ( E ) C18:1(n-9) c , ( F ) C20:5(n-3) c , ( G ) C8:0-carnitine, ( H ) C12:0-carnitine, ( I ) C14:0-carnitine, ( J ) C16:0-carnitine, ( K ) C18:1(n-9) c -carnitine, or ( L ) C20:5(n-3) c -carnitine onto the heart-type fatty acid-binding protein (FABP3) structure. The CSPs are color-coded, in which red indicates larger shifts, while blue indicates no changes in the averaged δ H and δ N NMR chemical shifts. Unassigned or disappeared residues are colored in gray. FABP3 structure is taken from PDB ID 3WVM.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: ITC results of the heart-type fatty acid-binding protein (FABP3) interaction with fatty acids (FAs) and acylcarnitines (ACs) in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi) at 25 °C.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques:
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: ( A ) Superposition of the ITC titration curves of the heart-type fatty acid-binding protein (FABP3) interaction with C18:1(n-9) c in black and C18:1(n-9) c -carnitine in cyan. Both experiments were performed in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi) at 25 °C. Graphical representation of the thermodynamic binding parameters of the FABP3 interaction with ( B ) C18:1(n-9) c and ( C ) C18:1(n-9) c -carnitine.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Titration, Binding Assay
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Superposition of the ITC thermograms for heart-type fatty acid-binding protein (FABP3) titrated with ( A ) C18:1(n-9) c and ( B ) C18:1(n-9) c -carnitine at three different temperatures: 16 (cyan), 25 (black), and 37 °C (red).
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Heat capacity change, Δ C p , and temperature dependence of the binding free energy, Δ G . ( A ) Δ C p values for four fatty acids (FAs) and corresponding acylcarnitines (ACs) binding to heart-type fatty acid-binding protein (FABP3). ( B ) Δ G of FA or AC binding to FABP3 within the temperature range from 0 to 100 °C.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Comparison of the changes in the heat capacity, Δ C p , for the heart-type fatty acid-binding protein (FABP3)—ligand complexes.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Comparison
Journal: International Journal of Molecular Sciences
Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
doi: 10.3390/ijms24065528
Figure Lengend Snippet: Top. Competitive binding studies of heart-type fatty acid-binding protein (FABP3)-C18:1(n-9) t -carnitine and three fatty acids (FAs) of different chain lengths. ( A ) Reference titration of C18:1(n-9) t -carnitine to apo-FABP3. ( B ) FABP3-C8:0 complex titrated with C18:1(n-9) t -carnitine. ( C ) FABP3-C10:0 complex titrated with C18:1(n-9) t -carnitine. ( D ) FABP3-C18:1(n-9) t -carnitine complex titrated with C10:0. ( E ) FABP3-C18:1(n-9) t -carnitine complex titrated with C12:0. All experiments were performed in 20 mM K 2 HPO 4 /KH 2 PO 4 and 50 mM KCl buffer pH 7.6 (KPi) at 25 °C. Bottom. Schematic representation of ligand binding and competition. Protein is represented as the dark blue sector, acylcarnitines (ACs) as orange, and FAs as cyan circles. Green arrows indicate that the competition event between ligands was successful.
Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the
Techniques: Binding Assay, Titration, Ligand Binding Assay