anti hresistin  (R&D Systems)

Journal: The FASEB Journal

Article Title: Periodontitis in Patients With Severe Obesity: From the Oral and Gut Microbiota Dysregulation to the Visceral Adipose Tissue Inflammatory and Metabolic Disorders

doi: 10.1096/fj.202600054R

Figure Lengend Snippet: Link between the periodontal status and the levels of plasma inflammatory and metabolic markers. Blood samples were obtained from patients with (Presence, n = 23) or without (Absence, n = 13) periodontitis, noting that samples were unavailable for 3 patients without periodontal infection. Plasma levels of IL‐6 (a), MCP‐1 (b), TNFα (c), IL‐8 (d), leptin (e), resistin (f), adiponectin (g), IL‐10 (h), MPO (i), LBP (j), and anti‐ P. gingivalis (Pg) IgG (k) were evaluated by ELISA. Data are expressed as mean ± standard deviation. Wilcoxon rank‐sum test was performed, * p < 0.05 as compared to Absence of periodontitis.

Article Snippet: Saliva, plasma and adipose tissue protein lysates were analyzed by ELISA kits targeting human interleukins (IL‐6, IL‐8, IL‐10), tumor necrosis factor‐alpha (TNF‐α), monocyte chemoattractant protein‐1 (MCP‐1, eBioscience, ThermoFisher Scientific, Dardilly, France), adiponectin, resistin (Ray Biotech, USA), leptin, myeloperoxidase (MPO), LPS‐binding protein (LBP), lipoprotein(a) (Lp(a), Abcam, France) and proprotein convertase subtilisin/kexin type 9 (PCSK9, R&D Sytems, Abingdon, UK).

Techniques: Clinical Proteomics, Infection, Enzyme-linked Immunosorbent Assay, Standard Deviation

Journal: PLOS One

Article Title: Human resistin is critical to activation of the NLRP3 inflammasome in macrophages

doi: 10.1371/journal.pone.0337682

Figure Lengend Snippet: ( A ) Schematic presentation of proposed pathway. ( B ) Human macrophages were cultured in 6-well plates under the conditions shown for 15 minutes before being washed and lysed for western blot analysis with antibodies to phospho-tyrosine (p-Y) and NLRP3 (image is representative of 6 repeats). ( C ) Human macrophages were cultured under the conditions shown for 12 hours. PBS was used as a control. Cells were washed, lysed, and assayed for their ability to cleave a fluorescent caspase-1 substrate, YVAD-AFC. Values were normalized to PBS controls. All conditions were run in duplicate wells, and two independent experiments were performed. Error bars represent the mean ± SD (n = 4). **** p < 0.001 versus PBS. ( D ) Hypoxia upregulates BTK and NLRP3 colocalization in C57BL/6 WT mice but not in RELMα KO mice. Immunofluorescence images of NLRP3 and BTK in lung tissues of mice kept under normoxic or hypoxic conditions for 4 days. Lung sections were stained with anti-NLRP3 (red) and BTK (green). The arrowheads point to cells positively stained for BTK and NLRP3 (yellow). The upper images are shown at higher magnification (400×); the lower panels display separate channels. Representative photograph of n = 6 mice per group. ( E ) Human resistin colocalized with BTK and NLRP3 in patients with PH. Immunofluorescence images of lung tissue slices from PH patients. Sections were stained with anti-hResistin (red) and co-stained with anti-BTK (green) and anti-NLRP3 (cyan) antibodies. The arrowheads point to cells positively stained for hResistin, BTK, and NLRP3. Separate channels are displayed in the lower panels. Original magnification: 100 × , 200 × , and 400 × . 4DHx, 4-day hypoxic; ab, antibody; BTK, Bruton’s tyrosine kinase; Con, control; Hres, human resistin; Ib, ibrutinib; KO, knockout; NLRP3, nucleotide-binding domain–like receptor protein 3; Nx, normoxic; PBS, phosphate-buffered saline; PH, pulmonary hypertension; RELMα, resistin-like molecule alpha; WT, wild-type. Created in BioRender. Lam, W. (2026) https://BioRender.com/1zhhut0 .

Article Snippet: After deparaffinization of tissue, rehydration, and antigen retrieval, sections were treated with anti-NLRP3 (Abcam, ab214185) and anti-Mac2 (Cedarlane, CL8942LE), anti-MPO (R&D Systems, AF3667), anti-CD79b (Abcam, ab134147), anti-BTK (Sigma-Aldrich, SAB4502936), anti-hResistin (R&D Systems, AF1359), or anti-RELMα (R&D Systems, MAB1523) antibodies overnight at 4°C and then with Alexa Fluor 488-donkey anti-mouse IgG (Jackson ImmunoResearch, 715-545-150) and Cy3-donkey anti-rabbit IgG (Jackson ImmunoResearch, 711-166-152) for double fluorescence staining.

Techniques: Cell Culture, Western Blot, Control, Immunofluorescence, Staining, Knock-Out, Binding Assay, Saline

Journal: Nature Communications

Article Title: The REDD1–NF-κB–miRNAs–eNOS/SIRT1 axis mediates obesity-induced endothelial cell senescence and hypertension

doi: 10.1038/s41467-026-70601-1

Figure Lengend Snippet: a – c Aortic vessels were isolated from male mice fed either a chow diet (lean) or an HFD (DIO) for 16 weeks. Vessels were either intact (E+) or de-endothelialized (E−). REDD1 expression was assessed by Western blotting ( a , b ) and confocal microscopy ( c ). Representative images from four mice per group with similar results. Scale bar = 50 µm. d , e REDD1 mRNA ( d , n = 4 independent experiments) and REDD1 protein levels ( e , n = 3 independent experiments) were measured after treatment with BSA-conjugated palmitic acid (PA, 300 µM), cholesterol (Chol, 100 µM, dissolved in DMSO), leptin (10 µg/ml), resistin (Retn, 100 ng/ml), oxLDL (50 µg/ml), or high glucose (HG, 25 mM) using qRT-PCR and Western blotting. f – h HAECs were transfected with 80 nM control siRNA (siC) or REDD1 siRNA (siREDD1) and then treated with PA ( f ), oxLDL ( g ), or high glucose (HG, h ) for 48 h. SA-β-gal + cells were detected using a SA-β-gal staining kit. Scale bar = 100 µm. The percentage of SA-β-gal + cells was calculated as the ratio of blue-stained to total cells ( n = 4 independent experiments). Western blotting for REDD1, p53, and p21 was performed in three independent experiments with similar results. Data are presented as mean ± s.e.m. Statistical significance was determined using one-way ANOVA with Holm–Sidak’s multiple comparisons test ( d , f – h ).

Article Snippet: Cells were then treated with or without oxLDL (50 μg/ml), prepared by incubating native LDL (1.019 mg protein) with 10 μM CuSO4 for 4 h , cholesterol (100 μM, #C8667; Sigma-Aldrich, St. Louis, MO, USA), glucose (25 mM, 25 mM L -glucose used for osmotic control), recombinant human resistin (100 ng/ml, #1359-RN; R&D systems, Minneapolis, MN, USA), recombinant human leptin (10 μg/ml, #398-LP; R&D Systems), recombinant human TNF-α (10 ng/ml, #10291-TA; R&D Systems), recombinant human IL-6 (40 ng/ml, #206-IL; R&D Systems), palmitate-BSA (300 μM), or H 2 O 2 (50–150 μM) for 48 h. Palmitic acid-BSA solution (5 mM) was prepared by mixing 10 μL of palmitate solution (500 mM in ethanol, #P9767; Sigma-Aldrich) with 1 mL of BSA solution (10%, w/v in serum-free M199, #A8806; Sigma-Aldrich).

Techniques: Isolation, Expressing, Western Blot, Confocal Microscopy, Quantitative RT-PCR, Transfection, Control, Staining

Journal: Nature Communications

Article Title: The REDD1–NF-κB–miRNAs–eNOS/SIRT1 axis mediates obesity-induced endothelial cell senescence and hypertension

doi: 10.1038/s41467-026-70601-1

Figure Lengend Snippet: a – c Representative H&E-stained images of renal tissues from lean and DIO mice: WT and Redd1 −/− ( a , n = 8 mice/group), Redd1 fl/fl and Redd1 ΔEC ( b , n = 7 mice/group), or WT and miR-214-3p −/− ( c , n = 6 mice/group). Glomerular size was quantified in four randomly selected fields per section using ImageJ. Scale bar = 50 µm. d , e Fibrotic area in renal tissues (Masson′s trichrome staining; ( d )) and serum creatinine levels ( e ) were quantified using ImageJ and ELISA, respectively ( n = 8, 7, and 6 mice for Redd1 −/− , Redd1 ΔEC , miR-214-3p −/− groups, respectively; same mice as in ( a – c )). f Representative Western blots using target-specific antibodies from four mice per group with similar results. Target proteins were analyzed independently three times, with tubulin probed on the same membrane as a loading control. g Graphical representation illustrating the role of REDD1 in obesity-induced vascular senescence and hypertension based on our current and previous findings . FFA free fatty acid, IR insulin resistance, TG triglyceride, VLDL very-low-density lipoprotein, LPL lipoprotein lipase, CE cholesteryl ester, ROS reactive oxygen species, Glc glucose, Retn resistin, GLG glycogen. Data are presented as mean ± s.e.m. Statistical significance was determined using two-way ANOVA with Holm–Sidak’s multiple comparisons test ( a – e ).

Article Snippet: Cells were then treated with or without oxLDL (50 μg/ml), prepared by incubating native LDL (1.019 mg protein) with 10 μM CuSO4 for 4 h , cholesterol (100 μM, #C8667; Sigma-Aldrich, St. Louis, MO, USA), glucose (25 mM, 25 mM L -glucose used for osmotic control), recombinant human resistin (100 ng/ml, #1359-RN; R&D systems, Minneapolis, MN, USA), recombinant human leptin (10 μg/ml, #398-LP; R&D Systems), recombinant human TNF-α (10 ng/ml, #10291-TA; R&D Systems), recombinant human IL-6 (40 ng/ml, #206-IL; R&D Systems), palmitate-BSA (300 μM), or H 2 O 2 (50–150 μM) for 48 h. Palmitic acid-BSA solution (5 mM) was prepared by mixing 10 μL of palmitate solution (500 mM in ethanol, #P9767; Sigma-Aldrich) with 1 mL of BSA solution (10%, w/v in serum-free M199, #A8806; Sigma-Aldrich).

Techniques: Staining, Enzyme-linked Immunosorbent Assay, Western Blot, Membrane, Control

Journal: Frontiers in Immunology

Article Title: Single-cell RNA sequencing unraveled immune-related expression heterogeneity and lymphoid cell development dysregulation in childhood asthma

doi: 10.3389/fimmu.2025.1606650

Figure Lengend Snippet: Cell communication pattern for asthma patients and healthy controls, serum resistin expression level and its PPI network. (A) The number of cell-cell interactions and interaction strength for four sample groups. (B) The annexin signaling pathway network of three sample groups. The annexin signaling pathway network in all cell types is shown for healthy controls, Asthma 1 and Asthma 3. The line thickness represents the signal strength, e.g. CD14 + monocytes have an annexin strength of 0.00006 in control, 0.0009 in asthma 1, and 0.0007 in asthma 3, respectively. The signal strength was estimated with the gene expression data of ligand-receptor pair. (C) The resistin signaling pathway network of three sample groups. The resistin signaling pathway network in all cell types is shown for healthy controls, Asthma 2 and Asthma 3. The line thickness represents the signal strength, e.g. CD14 + monocytes have a resistin strength of 0.0005 in control, 0.0025 in asthma 2, and 0.006 in asthma 3, respectively. The signal strength was estimated with the gene expression data of ligand-receptor pair. (D) The expression of RETN gene in two sample groups. The level of serum resistin between asthma patients and healthy controls (*** p < 0.001). (E) Protein–protein interaction network of RETN, its directly interacting genes and their neighbors. RETN is marked with red color and SQSTM1, HSPA5, and A2M are marked with light green color. RETN has a network degree of 8. SQSTM1, HSPA5, and A2M have a network degree of 109, 44, and 37, respectively. Network degree represents the number of neighbors (genes) connected to a hub, which is a core metric for measuring node importance and connection strength in complex network analysis.

Article Snippet: We followed a human resistin ELISA kit (Signalway Antibody, Maryland, USA, Catalog No: EK2351) protocol to analyze peripheral blood serums.

Techniques: Expressing, Control, Gene Expression