anti cd36  (Bioss)

Journal: PLOS Pathogens

Article Title: Retinol binding protein 4 enhances cellular cholesterol uptake to facilitate influenza A virus infection

doi: 10.1371/journal.ppat.1013623

Figure Lengend Snippet: (A, B) Quantification of total cholesterol levels in multiple WT and RBP4-deficient cell types (A) and in serum from WT and RBP4-deficient mice (B). (C) Heatmap representation of RNA sequencing analysis showing differentially expressed genes related to cholesterol metabolism in WT and RBP4-deficient BMDMs. (D, E) qPCR analysis of CD36 mRNA expression in WT and RBP4-deficient BMDMs (D, left) and HEK293T cells (D, right), or in lung tissues from WT and RBP4-deficient mice (E). (F, G) Immunoblotting analysis of CD36 protein levels in multiple WT and RBP4-decficent cells as indicated (F) or in lung tissues from WT and RBP4-deficient mice (G). (H to J) Immunoblotting analysis of protein levels of CD36, total JNK, phosphorylated (p)-JNK, STAT1, and p-STAT1 as indicated in PK-15 or 3D4/21 cells pretreated with SP600125 (SP, 10 μM) or Resatorvid (TAK, 1 μM) for 2 hours, followed by treatment with rpRBP4 for 24 hours. (K) Immunoblotting analysis of protein expression of CD36, NP and M1 in PK-15 cells treated as described in (H), followed by infection with IAV WSN strain (MOI = 0.1) for 24 hours. (L) Immunoblotting analysis of CD36, p-STAT1, total STAT1 and RBP4 protein levels in HEK293T cells transfected with RBP4 expression plasmid or control empty vector, followed by treatment with Ruxolitinib (Ruxo, 5 μM) for 2 hours. (M) Immunoblotting analysis of CD36, p-STAT1, STAT1, STRA6 and RBP4 protein levels in HEK293T cells co-transfected with RBP4 expression plasmid and siRNA for STRA6 or negative control for 36 hours. (N) Immunoblotting analysis of CD36, p-JAK2, JAK2, p-STAT1, STAT1 and RBP4 protein levels in HEK293T cells transfected with RBP4 expression plasmid or control empty vector, followed by treatment with Ruxo (5 μM) for 2 hours or transfected with siRNA for STRA6 or negative control for 36 hours. Data are pooled from three independent experiments (A, B, D, E, mean ± SD) or representative of two independent experiments (F-N). * p < 0.05, ** p < 0.01 (Student’s t -tes t ).

Article Snippet: The primary antibodies used in this study were sourced from commercial suppliers as follows: Rabbit polyclonal antibodies against RBP4 (1 : 2,000, 11774–1-AP), CD36 (1 : 2,000, 18836–1-AP), STRA6 (1 : 3,000, 22001–1-AP), p65 (1 : 1,000, 10745–1-AP) and β-actin (1 : 20,000, 66009–1-lg) were purchased from Proteintech Group Inc. Rabbit polyclonal antibodies against CD36 (1 : 1,000, CY5796) and FLAG (1 : 10,000, AB0030) were purchased from Abways.

Techniques: RNA Sequencing, Expressing, Western Blot, Infection, Transfection, Plasmid Preparation, Control, Negative Control

Journal: PLOS Pathogens

Article Title: Retinol binding protein 4 enhances cellular cholesterol uptake to facilitate influenza A virus infection

doi: 10.1371/journal.ppat.1013623

Figure Lengend Snippet: (A to D) Confocal microscopy (A and B) or flow cytometry (C and D) analysis of cholesterol uptake by Dil-OxLDL in WT and RBP4-deficient HEK293T cells or BMDMs. Scale bars, 100 μm. Statistics of mean fluorescence intensity was calculated by Image J software (A and B, right) or Flow Jo software (C and D, right). (E, F) Flow cytometry analysis of cholesterol uptake by Dil-OxLDL in WT, RBP4-deficient and CD36 overexpressing RBP4-deficient HEK293T cells (E) and BMDMs (F). Mean fluorescence intensities were quantified with Flow Jo software. (G, H) Flow cytometry analysis of SA expression in HEK293T cells (G, upper) transfected with hCD36 plasmid or in stable CD36-overexpressing iBMDMs (H, upper). Cells were left untreated or incubated with cholesterol for 1 hour at 37°C, followed by staining with SNA or MAL. Mean fluorescence intensities were quantified by Flow Jo software (lower panels). (I) Confocal microscopy analysis of SA expression and distribution in WT and CD36-overexpressing iBMDMs. Cells were left untreated or incubated with cholesterol for 1 hour at 37°C, followed by staining with SNA or MAL (green). Cell membranes were stained with Dil dye (red), and nuclei were counterstained with DAPI (blue). Data are representative (A-F, left, G, H, upper and I) or pooled from at least three independent experiments (A-F, right, G and H, lower, mean ± SD). * p < 0.05, ** p < 0.01, *** p < 0.001 (Student’s t -test).

Article Snippet: The primary antibodies used in this study were sourced from commercial suppliers as follows: Rabbit polyclonal antibodies against RBP4 (1 : 2,000, 11774–1-AP), CD36 (1 : 2,000, 18836–1-AP), STRA6 (1 : 3,000, 22001–1-AP), p65 (1 : 1,000, 10745–1-AP) and β-actin (1 : 20,000, 66009–1-lg) were purchased from Proteintech Group Inc. Rabbit polyclonal antibodies against CD36 (1 : 1,000, CY5796) and FLAG (1 : 10,000, AB0030) were purchased from Abways.

Techniques: Confocal Microscopy, Flow Cytometry, Fluorescence, Software, Expressing, Transfection, Plasmid Preparation, Incubation, Staining

Journal: PLOS Pathogens

Article Title: Retinol binding protein 4 enhances cellular cholesterol uptake to facilitate influenza A virus infection

doi: 10.1371/journal.ppat.1013623

Figure Lengend Snippet: (A, B) Flow cytometry analysis of α-2,3-linked SA or α-2,6-linked SA in WT, RBP4-deficient and CD36 overexpressing RBP4-deficient HEK293T cells, as wells as murine BMDMs transduced with CD36 retrovirus. Mean fluorescence intensities were quantified with FlowJo software. (C, D) qPCR analysis of vRNA levels of the NP gene or NP and M1 mRNA expression in HEK293T cells (C) or BMDMs (D) infected with IAV WSN strain (MOI = 5) during the viral attachment stage. (E) Flow cytometry analysis of α-2,3-linked SA or α-2,6-linked SA in WT and stable CD36-overexpressing iBMDMs cultured in serum-free medium. Cells were cultured with serum-free medium for 6 hours and subsequently stained with Lectins. Mean fluorescence intensities were quantified with FlowJo software. Data are pooled from three independent experiments (A-E, mean ± SD). * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 (Student’s t -test).

Article Snippet: The primary antibodies used in this study were sourced from commercial suppliers as follows: Rabbit polyclonal antibodies against RBP4 (1 : 2,000, 11774–1-AP), CD36 (1 : 2,000, 18836–1-AP), STRA6 (1 : 3,000, 22001–1-AP), p65 (1 : 1,000, 10745–1-AP) and β-actin (1 : 20,000, 66009–1-lg) were purchased from Proteintech Group Inc. Rabbit polyclonal antibodies against CD36 (1 : 1,000, CY5796) and FLAG (1 : 10,000, AB0030) were purchased from Abways.

Techniques: Flow Cytometry, Transduction, Fluorescence, Software, Expressing, Infection, Cell Culture, Staining

Journal: PLOS Pathogens

Article Title: Retinol binding protein 4 enhances cellular cholesterol uptake to facilitate influenza A virus infection

doi: 10.1371/journal.ppat.1013623

Figure Lengend Snippet: (A) Experimental scheme for lentiviral transduction and influenza virus infection in mice. WT and RBP4-deficient mice were intravenously injected with lentivirus (10 9 PFU in 200 μL per mouse) followed by infection with 10 4 PFU of IAV (WSN strain) 5 days later. Lungs were collected 3 days post-IAV infection. (B) qPCR analysis of CD36 mRNA levels in lung tissues from WT, RBP4-deficient, and CD36-overexpressing RBP4-deficient mice as treated in (A). (C) Body weight changes of indicated mouse genotypes at day 3 post-IAV infection. (D) Plaque assay analysis of virus titer in lung tissues from mice described in (A). (E, F) Immunofluorescence images (E, left) and quantitative analysis of NP protein intensity (E, right) or immunoblotting analysis of M1, NP and CD36 protein expression (F) in lung tissues from the mice described in (A). Mean fluorescence intensity was determined by Image J software (E, right). Scale bars, 100 μm. (G, H) Representative H&E-stained lung sections (G) and corresponding histopathological scores (H) from indicated groups. Each dot in (B-D, H) represents an individual mouse. (I) Proposed model of RBP4-mediated promotion of influenza virus infection. Created in BioRender. Huang, L. (2025) https://BioRender.com/rll2ll1 . Data are representative of two independent experiments (E-G). * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 (Student’s t -test).

Article Snippet: The primary antibodies used in this study were sourced from commercial suppliers as follows: Rabbit polyclonal antibodies against RBP4 (1 : 2,000, 11774–1-AP), CD36 (1 : 2,000, 18836–1-AP), STRA6 (1 : 3,000, 22001–1-AP), p65 (1 : 1,000, 10745–1-AP) and β-actin (1 : 20,000, 66009–1-lg) were purchased from Proteintech Group Inc. Rabbit polyclonal antibodies against CD36 (1 : 1,000, CY5796) and FLAG (1 : 10,000, AB0030) were purchased from Abways.

Techniques: Transduction, Virus, Infection, Injection, Plaque Assay, Immunofluorescence, Western Blot, Expressing, Fluorescence, Software, Staining

Journal: Advanced Science

Article Title: A Myelin Debris Cleaner for Spinal Cord Injury Recovery: Polycaprolactone / Cell Membrane Assembled Scaffolds

doi: 10.1002/advs.202503269

Figure Lengend Snippet: Preparation of pMM and validation of its adsorption to myelin debris. A) Optical microscope comparison of macrophages and macrophages pretreated with myelin debris. Scale bar: 200 µm (× 10). B) Transmission Electron Microscope (TEM) comparison of macrophages and macrophages pretreated with myelin debris. Scale bar: 2 µm (× 200). The yellow in the picture referred to mitochondria and the red referred to lipid droplets. Scale bar: 500 nm (× 800). C) Statistical analysis of the number of mitochondria (n = 3), assessed via t‐test. D) Comparison of the number of CD36 receptors on the surface of macrophages and macrophages pretreated with myelin debris. Scale bar: 100 µm (× 5). E) Statistical analysis of CD36 IF intensity (n = 3), assessed via t‐test. F) Optical microscope and TEM of pretreated macrophage cell membrane. Scale bar: 200 µm (× 5). G) Comparison of the adsorption efficiency to myelin debris between macrophage membrane and pretreatment macrophage membrane. Scale bar: 100 µm (×5). H) Statistical analysis of adsorbed MBP IF intensity (n = 3), assessed via t‐test. ****p < 0.05.

Article Snippet: CD36 Polyclonal antibody, Myelin basic protein (MBP) polyclonal antibodies, CD206 polyclonal antibodies, INOS polyclonal antibodies, CD86 polyclonal antibodies, Arg1 polyclonal antibodies, MAP2 polyclonal antibodies, GFAP polyclonal antibodies, TUBB3 polyclonal antibodies, and NF200 polyclonal antibodies were purchased from Proteintech, USA.

Techniques: Biomarker Discovery, Adsorption, Microscopy, Comparison, Transmission Assay, Membrane

Journal: Frontiers in Pharmacology

Article Title: α-Mangostin prevents diabetic cardiomyopathy by inhibiting oxidative damage and lipotoxicity through the AKT–FOXO1–CD36 pathway

doi: 10.3389/fphar.2025.1566311

Figure Lengend Snippet: Primers for RT-qPCR.

Article Snippet: These included BCL-2 (68103-1), ACTB (81115-1-RR), Nrf2 (16396-1-AP), CPT1β (22170-1), ACADM (55210-1), and PPARα (66826-1), all purchased from Proteintech (Wuhan, China); BAX (#2772), SOD2 (#13141), p-FOXO1 (#9461), FOXO1 (#2880), and caspase9 (#9508), purchased from Cell Signaling Technology (Inc., MA, United States); cleaved-caspase 3 (WL01992), cleaved-caspase 9 (WL01838), and HO-1 (WL02400), purchased from Wanleibio (Shenyang, China); CD36 (bs-8873R) and p-AKT (bs-0876R), purchased from Bioss (Beijing, China); and AKT (179463, Abcam).

Techniques: Sequencing

Journal: Frontiers in Pharmacology

Article Title: α-Mangostin prevents diabetic cardiomyopathy by inhibiting oxidative damage and lipotoxicity through the AKT–FOXO1–CD36 pathway

doi: 10.3389/fphar.2025.1566311

Figure Lengend Snippet: A-MG reduces lipid accumulation in HG/F-induced H9C2 cells. (A) Heatmap depicting A-MG-induced changes in gene expression influencing fat digestion and absorption. (B) GSEA gene enrichment map. (C) RT-qPCR analysis of CD36, PPARα, and CPT1β mRNA levels in H9C2 cells. (D) Representative images of intracellular lipid droplets in H9C2 cells stained with BODIPY 493/503. (E) Quantification of the mean fluorescence intensity of BODIPY 493/503; IntDen/Area (A.U.), integrated density/area (arbitrary unit). (F–H) Western blot analysis of p-FOXO1, FOXO1, and CD36 protein expressions in H9C2 cells. (I) Representative images of immunofluorescent staining of FOXO1 in H9C2 cells. (J) Quantification of the FOXO1 immunofluorescence signal in H9C2 cells. (K–M) Analysis of docking between A-MG and CD36 proteins. (K) 3D structure of CD36 bound with A-MG; the structure of CD36 is shown in cyan and A-MG is rendered in green. (L) Depiction of the electrostatic surface of the A-MG binding site on CD36. (M) Detail of the binding mode of A-MG on CD36. The results represent at least three independent experiments; data are expressed as the mean ± SD (n ≥ 3). * p < 0.05, ** p < 0.01, and *** p < 0.001.

Article Snippet: These included BCL-2 (68103-1), ACTB (81115-1-RR), Nrf2 (16396-1-AP), CPT1β (22170-1), ACADM (55210-1), and PPARα (66826-1), all purchased from Proteintech (Wuhan, China); BAX (#2772), SOD2 (#13141), p-FOXO1 (#9461), FOXO1 (#2880), and caspase9 (#9508), purchased from Cell Signaling Technology (Inc., MA, United States); cleaved-caspase 3 (WL01992), cleaved-caspase 9 (WL01838), and HO-1 (WL02400), purchased from Wanleibio (Shenyang, China); CD36 (bs-8873R) and p-AKT (bs-0876R), purchased from Bioss (Beijing, China); and AKT (179463, Abcam).

Techniques: Gene Expression, Quantitative RT-PCR, Staining, Fluorescence, Western Blot, Immunofluorescence, Binding Assay

Journal: Frontiers in Pharmacology

Article Title: α-Mangostin prevents diabetic cardiomyopathy by inhibiting oxidative damage and lipotoxicity through the AKT–FOXO1–CD36 pathway

doi: 10.3389/fphar.2025.1566311

Figure Lengend Snippet: A-MG activates the AKT pathway. (A–E) Western blot analysis examining the effect of LY294002 on AKT, p-AKT, Nrf2, SOD2, and HO-1 protein expression in HG/F-induced H9C2 cells. (F–I) Western blot analysis examining the effect of LY294002 on FOXO1, p-FOXO1, CD36, and CPT1β expression in HG/F-induced H9C2 cells. The results represent at least three independent experiments; data are expressed as the mean ± SD (n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Article Snippet: These included BCL-2 (68103-1), ACTB (81115-1-RR), Nrf2 (16396-1-AP), CPT1β (22170-1), ACADM (55210-1), and PPARα (66826-1), all purchased from Proteintech (Wuhan, China); BAX (#2772), SOD2 (#13141), p-FOXO1 (#9461), FOXO1 (#2880), and caspase9 (#9508), purchased from Cell Signaling Technology (Inc., MA, United States); cleaved-caspase 3 (WL01992), cleaved-caspase 9 (WL01838), and HO-1 (WL02400), purchased from Wanleibio (Shenyang, China); CD36 (bs-8873R) and p-AKT (bs-0876R), purchased from Bioss (Beijing, China); and AKT (179463, Abcam).

Techniques: Western Blot, Expressing

Journal: Frontiers in Pharmacology

Article Title: α-Mangostin prevents diabetic cardiomyopathy by inhibiting oxidative damage and lipotoxicity through the AKT–FOXO1–CD36 pathway

doi: 10.3389/fphar.2025.1566311

Figure Lengend Snippet: A-MG attenuates lipid accumulation and oxidative stress in the cardiac tissue of DCM mice. (A) Representative images of myocardial BODIPY 493/503 staining. (B–D) Analysis of serum TG, TC, and LDL-C levels. (E–M) Western blot analysis of p-AKT, AKT, p-FOXO1, FOXO1, CD36, PPARα, CPT1β, Nrf2, HO-1, and SOD2 in heart tissues. Data are presented as the mean ± SD. In (B–D) , n = 5; in (F, H–M) , n = 4; in (G) , n = 3. * p < 0.05, ** p < 0.01, and *** p < 0.001.

Article Snippet: These included BCL-2 (68103-1), ACTB (81115-1-RR), Nrf2 (16396-1-AP), CPT1β (22170-1), ACADM (55210-1), and PPARα (66826-1), all purchased from Proteintech (Wuhan, China); BAX (#2772), SOD2 (#13141), p-FOXO1 (#9461), FOXO1 (#2880), and caspase9 (#9508), purchased from Cell Signaling Technology (Inc., MA, United States); cleaved-caspase 3 (WL01992), cleaved-caspase 9 (WL01838), and HO-1 (WL02400), purchased from Wanleibio (Shenyang, China); CD36 (bs-8873R) and p-AKT (bs-0876R), purchased from Bioss (Beijing, China); and AKT (179463, Abcam).

Techniques: Staining, Western Blot