Journal: Cancers

Article Title: Murlentamab, a Low Fucosylated Anti-Müllerian Hormone Type II Receptor (AMHRII) Antibody, Exhibits Anti-Tumor Activity through Tumor-Associated Macrophage Reprogrammation and T Cell Activation

doi: 10.3390/cancers13081845

Figure Lengend Snippet: Flow cytometry antibodies used.

Article Snippet: CD36-PEVio770 , Miltenyi , 130-110-742 , REA770 , .

Techniques: Flow Cytometry, In Vivo, In Vitro

Journal: Cancers

Article Title: Murlentamab, a Low Fucosylated Anti-Müllerian Hormone Type II Receptor (AMHRII) Antibody, Exhibits Anti-Tumor Activity through Tumor-Associated Macrophage Reprogrammation and T Cell Activation

doi: 10.3390/cancers13081845

Figure Lengend Snippet: Murlentamab opsonization of SKOV3-R2 + orients naïve macrophages and reprograms TAMs towards an M1-like profile. SKOV3-R2 + ovarian tumor cells were labeled with different 3C23K antibodies (3C23K-FcKO control, 3C23K-CHO normally fucosylated or murlentamab the low fucosylated form) and cultured in the presence of human monocyte-derived macrophages from healthy donors unstimulated (M0) or stimulated with M-CSF and IL-10 (TAMs). ( A ) The proportion of macrophages expressing M1/M2 membrane markers (CD32, CD64, CD80, TLR2, CD163, CD36 and CD206) was determined by flow cytometry after three days of co-culture with SKOV3-R2 + cells. ( B ) The release of cytokines (IL1β, IL12, TNFα, IL6, IFNγ, IL10) and chemokines (CCL2, CCL4, CCL5, CXCL9 and CXCL10) in the culture medium was determined by AlphaLISA after three days of co-culture with SKOV3-R2 + cells. Data shown (boxplots) are the results from three different experiments (performed with three different healthy donors). * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001. p values were determined using one-way ANOVA analysis followed by Tukey’s multiple comparisons test.

Article Snippet: CD36-PEVio770 , Miltenyi , 130-110-742 , REA770 , .

Techniques: Labeling, Cell Culture, Derivative Assay, Expressing, Membrane, Flow Cytometry, Co-Culture Assay

Journal: Nature communications

Article Title: CD36 mediates SARS-CoV-2-envelope-protein-induced platelet activation and thrombosis.

doi: 10.1038/s41467-023-40824-7

Figure Lengend Snippet: Fig. 6 | CD36 deficiency or CD36 blockade in vivo attenuates E protein- enhanced thrombosis. a Levels of CD36 in wild-type (WT) and CD36−/−mouse platelets. Results were confirmed in three independent experiments using platelets from different mice. b and c WT and CD36−/−mice were intravenously injected with the E protein (4 μg per mouse) or PBS 4 h before the pulmonary embolism (PE) model. b Quantification of the numbers of lung embolisms per visual field on lung sections. Data are mean ± SD of 25 counts from 5 mice in each group. c Representative field on lung sections by hematoxylin-eosin (HE) staining from WT and CD36−/−mice injected with the E protein or PBS. Scale bar = 100 μm. d and e Inferior vena cava (IVC) stenosis model was performed in WT and CD36−/−mice. WT and CD36−/−mice were pretreated with the E protein (4 μg per mouse) or PBS. d Representative image of the IVC thrombi. e The quantification analysis of the thrombi weight (n = 5). f and g WT mice were intraperitoneally injected with 10 mg/ kg SB203580 or DMSO. After 2 h, mice were intravenously infused with the E

Article Snippet: Anti-phospho-p38 (1:1000, clone D3F9, #4511, CST), anti-p38 (1:1000, clone D13E1, #8690, CST), antiphospho-NF-κB p65 (1:1000, clone 93H1, #3033, CST), anti-NF-κB p65 (1:1000, clone D14E12, #8242, CST), anti-phospho-ERK (1:1000, clone D13.14.4E, #4370, CST), anti-ERK (1:1000, clone 137F5, #4695, CST), anti-phospho-JNK (1:1000, clone 81E11, #4668, CST), anti-JNK (1:1000, clone 56G8, #9258, CST), anti-ICAM-1 (1:1000, #4915, CST), anti-VCAM-1(1:1000, clone E1E8X, #13662, CST), anti-human CD36 (1 μg/mL, #MAB1955, R&D Systems), anti-mouse CD36 (1 μg/mL, SMφ, #sc-7309, Santa Cruz), anti-His-Tag (1:2000, clone AMC0149, #AE003, ABclonal Technology), anti-Human IgG Fc (HRP)(1:3000, #ab97225, Abcam), and biotin-conjugated anti-SARS-CoV-2 envelope (1 μg/mL, #ab284658, Abcam) antibodies were used as primary antibodies.

Techniques: In Vivo, Injection, Staining

Journal: Molecular Nutrition & Food Research

Article Title: Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

doi: 10.1002/mnfr.202000834

Figure Lengend Snippet: Inhibition of sRAGE, Gal‐3, CD36 and SR‐AI by BLG and whey proteins measured in competition ELISA. BLG (A) and WP (B), non‐treated or heated in the absence of sugar (BLG‐H) or in the presence of lactose or glucose (BLG‐Glu, BLG‐Lac) were pre‐incubated with the recombinant forms of sRAGE, Gal‐3, CD36 and SR‐AI prior adding to the ELISA plate coated with glycated soy protein extract. The data are expressed as percentage of inhibition by the use of non‐inhibited signal as the maximum value. Positive control: highly glycated soy protein extract; Negative control: ovalbumin. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments on three different batches of processed BLG. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Article Snippet: Inhibition ELISA was conducted as a screening tool to determine the binding strength of the processed BLG to the following receptors: soluble RAGE (# RD172116100, BioVendor, Brno, Czech Republic), galectin‐3 (# 1154‐DC, R&D Systems, Minneapolis, United States) and two receptors from the scavenger receptor family: SR‐AI (# 1154‐DC, R&D Systems, Minneapolis, United States) and CD36 (# 1955‐CD, R&D Systems, Minneapolis, United States) according to the protocol described by Zenker et al. [ ] The detailed information about antibodies used in the assay are displayed in Table , Supporting Information.

Techniques: Inhibition, Enzyme-linked Immunosorbent Assay, Incubation, Recombinant, Positive Control, Negative Control, Comparison

Journal: Molecular Nutrition & Food Research

Article Title: Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

doi: 10.1002/mnfr.202000834

Figure Lengend Snippet: Inhibition of binding and internalization of processed BLG by human THP‐1 macrophages. PMA differentiated THP‐1 macrophages were pre‐incubated with endocytosis inhibitors: dynasore and cytochalasin D (Cyt D) or inhibitors of specific receptors: amyloid‐β and FPS‐ZM1 for RAGE; Oxidized low‐density lipoprotein (Ox‐LDL) for CD36; fucoidan for SR‐AI, short peptides 33‐DFTG and G3‐C12 for Gal‐3. Followed by pre‐incubation with inhibitor the cells were incubated in a presence or absence of BLG: non‐treated (BLG‐NT), heated (BLG‐H), heated with lactose (BLG‐Lac) or heated with glucose (BLG‐Glu) and stained extracellularly (A) or intracellularly (B) with Alexa Fluor 647 conjugated anti‐BLG antibodies. The level of fluorescence was measured by flow cytometry and expressed as a relative to non‐inhibited THP‐1 cells. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Article Snippet: Inhibition ELISA was conducted as a screening tool to determine the binding strength of the processed BLG to the following receptors: soluble RAGE (# RD172116100, BioVendor, Brno, Czech Republic), galectin‐3 (# 1154‐DC, R&D Systems, Minneapolis, United States) and two receptors from the scavenger receptor family: SR‐AI (# 1154‐DC, R&D Systems, Minneapolis, United States) and CD36 (# 1955‐CD, R&D Systems, Minneapolis, United States) according to the protocol described by Zenker et al. [ ] The detailed information about antibodies used in the assay are displayed in Table , Supporting Information.

Techniques: Inhibition, Binding Assay, Incubation, Staining, Fluorescence, Flow Cytometry, Comparison

Journal: Molecular Nutrition & Food Research

Article Title: Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

doi: 10.1002/mnfr.202000834

Figure Lengend Snippet: Immunoreactivity of heated and glycated BLG after enzymatic digestion in infant gastrointestinal static in vitro model. BLG: Non‐treated, heated (BLG‐H), heated with lactose (BLG‐Lac) or heated with glucose (BLG‐Glu) were subjected to gastric and intestinal phase of enzymatic digestion and immunogenicity of digested samples was measured as (A) binding to sRAGE, Gal‐3, CD36 and SR‐AI in inhibition ELISAs; following positive controls were used: amyloid‐β for sRAGE and CD36, fucoidan for SRAI and soy protein extract glycated with glucose for Gal‐3. B) binding assay to THP‐1 macrophages using Alexa Fluor 647 conjugated anti‐BLG antibodies for flow cytometry detection. Digestion blank (dBlank) – sample containing all digestive enzymes but no BLG. Data shown as mean ± SD of triplicate wells and are representative of at three (A) or two (B) independent experiments. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Article Snippet: Inhibition ELISA was conducted as a screening tool to determine the binding strength of the processed BLG to the following receptors: soluble RAGE (# RD172116100, BioVendor, Brno, Czech Republic), galectin‐3 (# 1154‐DC, R&D Systems, Minneapolis, United States) and two receptors from the scavenger receptor family: SR‐AI (# 1154‐DC, R&D Systems, Minneapolis, United States) and CD36 (# 1955‐CD, R&D Systems, Minneapolis, United States) according to the protocol described by Zenker et al. [ ] The detailed information about antibodies used in the assay are displayed in Table , Supporting Information.

Techniques: In Vitro, Immunopeptidomics, Binding Assay, Inhibition, Flow Cytometry, Comparison

Journal: bioRxiv

Article Title: Direct interactions of CEACAM1 and CD36 with LPS and each other

doi: 10.64898/2026.02.01.703119

Figure Lengend Snippet: A-C. Flow analysis of CEACAM1-4L and CD36-BioID2 expression in transfected HEK cells. ( A ) HEK cells untransfected controls. ( B ) HEK cells transfected with CD36-BioID2 only. ( C HEK cells transfected with both CD36-BioID2 and CEACAM1-4L. D-E . Immunoblots of HEK cells expressing only CD36-BioID2 (lane 1) or both CD36-BioID2 and CEACAM1-4L (lane 2), immunostained with antibodies to CD36 ( D ) or CEACAM1-4L ( E ). Transfected cells were grown for 4 days, incubated with 50 µM biotin overnight, washed twice with PBS, lysed with 1% NP40, incubated with streptavidin beads for 4 hrs, eluted with SDS running buffer, run on SDS gels and immunoblotted with either anti-CD36 or anti-CEACAM1 antibodies.

Article Snippet: On day 4 following transfection, the cells were collected and stained with either anti-CD36 (FAB19551G) or anti-CEACAM-1 (R&D systems, FAB2244P) antibody to assess the level of expression using flow cytometry.

Techniques: Expressing, Transfection, Western Blot, Incubation

Journal: Cell reports

Article Title: CD36-Mediated Metabolic Rewiring of Breast Cancer Cells Promotes Resistance to HER2-Targeted Therapies

doi: 10.1016/j.celrep.2019.11.008

Figure Lengend Snippet:

Article Snippet: CD36 Human siRNA Oligo Duplex , Origene , Cat# SR319610.

Techniques: Blocking Assay, Control, Recombinant, Isolation, cDNA Synthesis, SYBR Green Assay, Transfection, Proliferation Assay, Microarray, Negative Control, Software

Journal: iScience

Article Title: Targeting CD36 determines nicotine derivative NNK-induced lung adenocarcinoma carcinogenesis

doi: 10.1016/j.isci.2023.107477

Figure Lengend Snippet:

Article Snippet: CD36 shRNA: 5'-GGACCATTGGTGATGAGAAGG CAAACATG-3' , Origene , Cat# TL314090.

Techniques: Recombinant, Virus, Subcloning, Plasmid Preparation, shRNA, Software