Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Neuron-specific Igfbp2 deficiency in the PFC induces cognitive dysfunction (A) Schematic of the experimental design. (B) Diagram of viral injection into the PFC (top) and representative image of viral expression (bottom); scale bars, 500 μm. (C) Representative western blot bands (top) and quantification of Igfbp2 protein levels in the PFC (bottom); n = 4 mice per group. (D) Schematic of the novel object recognition test, depicting the training phase (top) and the test phase (bottom). (E) Representative trajectory plots from the novel object recognition test. (F) Quantification of time spent investigating the novel object during the test phase; n = 8 mice per group. (G) Quantification of the number of investigations of the novel object during the test phase; n = 8 mice per group. (H) Schematic of the Y-maze test, depicting the training phase (top) and the test phase (bottom). (I) Representative trajectory plots from the Y-maze test. (J) Quantification of time spent in the novel arm during the test phase; n = 8 mice per group. (K) Quantification of the number of entries into the novel arm during the test phase; n = 8 mice per group. Analyzed by unpaired t test; ∗∗ p < 0.01. Data are presented as means ± SEM.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: Injection, Expressing, Western Blot

Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Neuron-specific Igfbp2 deficiency in the PFC reduces excitatory synaptic transmission and neuronal excitability (A) Representative traces of sEPSC recorded from PFC neurons in AAV-scramble (top) and AAV-shRNA (bottom) groups. (B) Cumulative probability plots (main panel) and quantification (insert panel) of sEPSC frequency in AAV-Scramble and AAV-shRNA groups. (C) Cumulative probability plots (main panel) and quantification (insert panel) of sEPSC amplitude in AAV-Scramble and AAV-shRNA groups. (D) Representative traces of sIPSC recorded from PFC neurons in AAV-Scramble (top) and AAV-shRNA (bottom) groups. (E) Cumulative probability plots (main panel) and quantification (insert panel) of sIPSC frequency in AAV-Scramble and AAV-shRNA groups. (F) Cumulative probability plots (main panel) and quantification (insert panel) of sIPSC amplitude in AAV-Scramble and AAV-shRNA groups. (G) Representative traces of AP elicited by 200 pA current injections in PFC neurons from AAV-Scramble (left) and AAV-shRNA (right) groups. (H) Quantification of AP firing frequency in response to a range of current injections in PFC neurons from AAV-Scramble and AAV-shRNA groups. Analyzed by unpaired t test in B, C, E, and F, and two-way repeated-measure ANOVA in H; n = 8 neurons from 4 mice per group; ns: not significant, ∗∗ p < 0.01. Data are presented as means ± SEM.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: Transmission Assay, shRNA

Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Neuron-specific Igfbp2 deficiency in the PFC disrupts synaptic integrity (A) Representative images of dendritic spines in the PFC from AAV-Scramble (left) and AAV-shRNA (right) groups; scale bars, 10 μm. (B) Quantification of dendritic spine density (number per 10 μm) in the PFC from AAV-Scramble and AAV-shRNA groups; n = 9 brain sections from 3 mice per group. (C) Representative western blot bands (top) and quantification of synapsin-1 protein levels (bottom) in the PFC from AAV-scramble and AAV-shRNA groups; n = 4 mice per group. (D) Representative western blot bands (top) and quantification of PSD-95 protein levels (bottom) in the PFC from AAV-Scramble and AAV-shRNA groups; n = 4 mice per group. Analyzed by unpaired t test; ∗ p < 0.05 and ∗∗∗ p < 0.001. Data are presented as means ± SEM.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: shRNA, Western Blot

Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Exogenous supplementation of Igfbp2 in the PFC rescues cognitive deficits induced by neuron-specific Igfbp2 deficiency (A) Schematic of the experimental design. (B) Diagram shows virus injection and cannula placement into the PFC (top), and a representative image of cannula position and viral expression in the PFC (bottom); scale bars, 500 μm. (C) Representative western blot bands (top) and quantification of Igfbp2 protein levels in the PFC (bottom); n = 4 mice per group. (D) Schematic of the novel object recognition test, depicting the training phase (top) and the test phase (bottom). (E) Representative trajectory plots from the novel object recognition test. (F) Quantification of time spent investigating the novel object during the test phase; n = 8 mice per group. (G) Quantification of the number of investigations of the novel object during the test phase; n = 8 mice per group. (H) Schematic of the Y-maze test, depicting the training phase (top) and the test phase (bottom). (I) Representative trajectory plots from the Y-maze test. (J) Quantification of time spent in the novel arm during the test phase; n = 8 mice per group. (K) Quantification of the number of entries into the novel arm during the test phase; n = 8 mice per group. Analyzed by unpaired t test; ∗∗ p < 0.01. Data are presented as means ± SEM.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: Virus, Injection, Expressing, Western Blot

Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Exogenous supplementation of Igfbp2 in the PFC restores excitatory synaptic transmission and neuronal excitability impaired by neuron-specific Igfbp2 deficiency (A) Representative traces of sEPSC recorded from PFC neurons in saline (top) and Igfbp2 (bottom) groups. (B) Cumulative probability plots (main panel) and quantification (insert panel) of sEPSC frequency in saline (top) and Igfbp2 (bottom) groups. (C) Cumulative probability plots (main panel) and quantification (insert panel) of sEPSC amplitude in saline and Igfbp2 groups. (D) Representative traces of sIPSC recorded from PFC neurons in saline (top) and Igfbp2 (bottom) groups. (E) Cumulative probability plots (main panel) and quantification (insert panel) of sIPSC frequency in saline and Igfbp2 groups. (F) Cumulative probability plots (main panel) and quantification (insert panel) of sIPSC amplitude in saline and Igfbp2 groups. (G) Representative traces of AP elicited by 200 pA current injections in PFC neurons from saline (left) and Igfbp2 (right) groups. (H) Quantification of AP firing frequency in response to a range of current injections in PFC neurons from Saline (left) and Igfbp2 (right) groups. Analyzed by unpaired t test in B, C, E, and F, and two-way repeated-measure ANOVA in H; n = 8 neurons from 4 mice per group; ns: not significant, ∗∗ p < 0.01. Data are presented as means ± SEM.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: Transmission Assay, Saline

Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Exogenous supplementation of Igfbp2 in the PFC restores synaptic integrity disrupted by neuron-specific Igfbp2 deficiency (A) Representative images of dendritic spines in the PFC from saline (left) and Igfbp2 (right) groups; scale bars, 10 μm. (B) Quantification of dendritic spine density (number per 10 μm) in the PFC from saline and Igfbp2 groups; n = 9 brain sections from 3 mice per group. (C) Representative western blot bands (top) and quantification of synapsin-1 protein levels (bottom) in the PFC from AAV-Scramble and AAV-shRNA groups; n = 4 mice per group. (D) Representative western blot bands (top) and quantification of PSD-95 protein levels (bottom) in the PFC from AAV-Scramble and AAV-shRNA groups; n = 4 mice per group. Analyzed by unpaired t test; ∗ p < 0.05 and ∗∗∗ p < 0.001. Data are presented as means ± SEM.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: Saline, Western Blot, shRNA

Journal: iScience

Article Title: Neuronal Igfbp2 deficiency in the prefrontal cortex impairs cognition through synaptic dysfunction in male mice

doi: 10.1016/j.isci.2026.115629

Figure Lengend Snippet: Schematic summary of this study Neuron-specific Igfbp2 deficiency in the PFC impairs cognitive function by disrupting synaptic integrity, excitatory transmission, and neuronal activity, whereas exogenous Igfbp2 supplementation mitigates cognitive deficits by restoring synaptic integrity, excitatory transmission, and neuronal activity. PFC prefrontal cortex, sEPSC spontaneous excitatory postsynaptic currents, Igfbp2 insulin-like growth factor-binding protein 2.

Article Snippet: Recombinant Igfbp2 protein (MCE; Cat# HY- P74846 ) was dissolved in sterile saline at 10 μg/μL.

Techniques: Transmission Assay, Activity Assay, Binding Assay

Journal: Hepatology Communications

Article Title: CRISPLD2 protects against liver inflammation and fibrosis via GRP78 to repress HMGB1/TLR4 axis–mediated STING palmitoylation

doi: 10.1097/HC9.0000000000000954

Figure Lengend Snippet: Activation of the HMGB1/TLR4 axis induced hepatocyte inflammatory response and fibrosis. (A) Primary hepatocytes were treated with 5 μg/mL HMGB1 for 3, 9, 18, 24, and 48 hours. IL-6, IL-1β, and TNF-α levels in the culture medium were assessed by ELISA. (B) JS-1 cells were co-cultured with primary hepatocytes treated with 5 μg/mL HMGB1 for 3, 9, 18, 24, and 48 hours, and α-SMA, FN, and col1a1 protein abundance in JS-1 cells was determined by western blotting. (C) Primary hepatocytes were added with 5 μg/mL HMGB1 together with or without 10 nM TAK-242 for 24 hours, and IL-6, IL-1β, and TNF-α levels in the culture medium were detected by ELISA. (D) Primary hepatocytes with various treatments were co-cultured with JS-1 cells, and western blotting analysis of α-SMA, FN, and col1a1 protein levels in JS-1 cells. n=3. One-way ANOVA was performed for statistical analysis. * p <0.05, ** p <0.01, and *** p <0.001. Abbreviations: α-SMA, alpha-smooth muscle actin; ANOVA, analysis of variance; COL1A1, collagen type I alpha 1 chain; ELISA, enzyme-linked immunosorbent assay; FN, fibronectin; HMGB1, high mobility group box 1; IL, interleukin; TNF-α, tumor necrosis factor-alpha.

Article Snippet: The primary hepatocytes were treated with 5 μg/mL recombinant mouse HMGB1 protein (50913-M01H; Sino Biological, Beijing, China) for 3, 9, 18, 24, and 48 hours or 1, 5, 10, and 20 μg/mL recombinant mouse CRISPLD2 protein (CSB-YP805372MO; Cusabio, Hubei, Wuhan) for 24 hours.

Techniques: Activation Assay, Enzyme-linked Immunosorbent Assay, Cell Culture, Quantitative Proteomics, Western Blot

Journal: Hepatology Communications

Article Title: CRISPLD2 protects against liver inflammation and fibrosis via GRP78 to repress HMGB1/TLR4 axis–mediated STING palmitoylation

doi: 10.1097/HC9.0000000000000954

Figure Lengend Snippet: STING palmitoylation at the C64 site was involved in HMGB1/TLR4 axis–mediated hepatocyte inflammatory response and fibrosis. (A) Primary hepatocytes were treated with 5 μg/mL HMGB1 combined with or without 10 nM TAK-242 for 24 hours, and the ABE assay evaluated STING palmitoylation level. The cells were added with hydroxylamine (+HAM) buffer or lysis buffer (−HAM). Palm-STING, STING palmitoylation. (B) Primary hepatocytes were treated with 100 μM 2-BP (a palmitoylation inhibitor) for 2–4 hours, and ABE assay analysis of STING palmitoylation level. The cells were added with hydroxylamine (+HAM) buffer or lysis buffer (−HAM). Palm-STING, STING palmitoylation. (C) STING palmitoylation level in primary hepatocytes exposed to 10 μM palmostatin B (a palmitoylation enhancer) for 2, 4, and 8 hours was analyzed by ABE assay. The cells were added with hydroxylamine (+HAM) buffer or lysis buffer (−HAM). Palm-STING, STING palmitoylation. (D) Conservative analysis of STING protein sequences among different species. (E) HEK293T cells were transfected with STING-WT or STING-C64A, and the Acyl-RAC assay determined STING palmitoylation level. Primary hepatocytes infected with lentiviruses carrying STING-WT or STING-C64A and treated with 5 μg/mL HMGB1, followed by co-culture with JS-1 cells. (F) ELISA measured IL-6, IL-1β, and TNF-α levels in the supernatant of primary hepatocytes. (G) Western blotting analysis of α-SMA, FN, and col1a1 protein abundance in JS-1 cells. n=3. One-way ANOVA was performed for statistical analysis. * p <0.05, ** p <0.01, and *** p <0.001. Abbreviations: ABE, Acyl-Biotin Exchange; α-SMA, alpha-smooth muscle actin; ANOVA, analysis of variance; COL1A1, collagen type I alpha 1 chain; ELISA, enzyme-linked immunosorbent assay; FN, fibronectin; HAM, hydroxylamine; HMGB1, high mobility group box 1; 2-BP, 2-bromopalmitate; STING, stimulator of interferon genes; STING-WT, wild-type STING.

Article Snippet: The primary hepatocytes were treated with 5 μg/mL recombinant mouse HMGB1 protein (50913-M01H; Sino Biological, Beijing, China) for 3, 9, 18, 24, and 48 hours or 1, 5, 10, and 20 μg/mL recombinant mouse CRISPLD2 protein (CSB-YP805372MO; Cusabio, Hubei, Wuhan) for 24 hours.

Techniques: Lysis, Transfection, Infection, Co-Culture Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Quantitative Proteomics

Journal: Hepatology Communications

Article Title: CRISPLD2 protects against liver inflammation and fibrosis via GRP78 to repress HMGB1/TLR4 axis–mediated STING palmitoylation

doi: 10.1097/HC9.0000000000000954

Figure Lengend Snippet: CRISPLD2 inactivated the HMGB1/TLR4 axis to repress STING palmitoylation, thus suppressing hepatocyte inflammatory response and fibrosis. HMGB1-treated primary hepatocytes were further stimulated with 1, 5, 10, and 20 μg/mL CRISPLD2 for 24 hours, followed by co-culture with JS-1 cells. (A) ELISA determined IL-6, IL-1β, and TNF-α levels in the supernatant of primary hepatocytes. (B) α-SMA, FN, and col1a1 protein abundance in JS-1 cells was assessed by western blotting. (C) STING palmitoylation levels were evaluated by the ABE assay. The cells were added with hydroxylamine (+HAM) buffer or lysis buffer (−HAM). Palm-STING, STING palmitoylation. n=3. One-way ANOVA was performed for statistical analysis. * p <0.05, ** p <0.01, and *** p <0.001. ABE, Acyl-Biotin Exchange; α-SMA, alpha-smooth muscle actin; ANOVA, analysis of variance; COL1A1, collagen type I alpha 1 chain; CRISPLD2, cysteine-rich secreted protein LCCL domain 2; ELISA, enzyme-linked immunosorbent assay; FN, fibronectin; HAM, hydroxylamine; HMGB1, high mobility group box 1; STING, stimulator of interferon genes.

Article Snippet: The primary hepatocytes were treated with 5 μg/mL recombinant mouse HMGB1 protein (50913-M01H; Sino Biological, Beijing, China) for 3, 9, 18, 24, and 48 hours or 1, 5, 10, and 20 μg/mL recombinant mouse CRISPLD2 protein (CSB-YP805372MO; Cusabio, Hubei, Wuhan) for 24 hours.

Techniques: Co-Culture Assay, Enzyme-linked Immunosorbent Assay, Quantitative Proteomics, Western Blot, Lysis

Journal: Hepatology Communications

Article Title: CRISPLD2 protects against liver inflammation and fibrosis via GRP78 to repress HMGB1/TLR4 axis–mediated STING palmitoylation

doi: 10.1097/HC9.0000000000000954

Figure Lengend Snippet: CRISPLD2 degraded TLR4 via an autophagic–lysosomal pathway. (A) Primary hepatocytes were treated with 5 μg/mL HMGB1, 10 μg/mL CRISPLD2, or a combination of them. Western blotting analysis of TLR4 protein level. (B) Primary hepatocytes were treated with 10 μg/mL CRISPLD2, or combined with 20 μM MG132 or 10 mM CQ, and TLR4 protein level was assessed by western blotting. Primary hepatocytes treated with 5 μg/mL HMGB1, 10 μg/mL CRISPLD2, or a combination of them. (C) Western blotting analysis of the protein levels of ATG3, ATG7, ATG12, ATG16L1, LC3 II/I, and p62. (D) The protein interaction between TLR4 and LC3 or p62 was confirmed by Co-IP. n=3. One-way ANOVA was performed for statistical analysis. * p <0.05, ** p <0.01, and *** p <0.001. Abbreviations: ANOVA, analysis of variance; ATG, autophagy-related protein; CQ, chloroquine; Co-IP, co-immunoprecipitation; CRISPLD2, cysteine-rich secreted protein LCCL domain 2; HMGB1, high mobility group box 1; LC3, microtubule-associated protein 1 light chain 3; MG132, proteasome inhibitor; TLR4, toll-like receptor 4.

Article Snippet: The primary hepatocytes were treated with 5 μg/mL recombinant mouse HMGB1 protein (50913-M01H; Sino Biological, Beijing, China) for 3, 9, 18, 24, and 48 hours or 1, 5, 10, and 20 μg/mL recombinant mouse CRISPLD2 protein (CSB-YP805372MO; Cusabio, Hubei, Wuhan) for 24 hours.

Techniques: Western Blot, Co-Immunoprecipitation Assay, Immunoprecipitation

Journal: Hepatology Communications

Article Title: CRISPLD2 protects against liver inflammation and fibrosis via GRP78 to repress HMGB1/TLR4 axis–mediated STING palmitoylation

doi: 10.1097/HC9.0000000000000954

Figure Lengend Snippet: CRISPLD2 facilitated the cytomembrane translocation of GRP78. Primary hepatocytes were exposed to 5 μg/mL HMGB1, 10 μg/mL CRISPLD2, or a combination of them. (A) GRP78 protein level was analyzed by western blotting. (B) Interplay between CRISPLD2 and GRP78 proteins was evaluated by Co-IP. (C) The binding of CRISPLD2 to GRP78 protein in the cytomembrane of primary hepatocytes was validated by a biotin pull-down assay. (D) Co-IP validated the interaction between CRISPLD2 and GRP78 proteins in the cytomembrane. (E) The co-localization of CRISPLD2 and GRP78 in CRISPLD2-treated primary hepatocytes was observed by immunofluorescent staining (scale bar=25 μm). (F) The subcellular localization of GRP78 in primary hepatocytes was evaluated by immunofluorescent staining, and the cytomembrane was labeled by WGA staining (scale bar=25 μm). n=3. One-way ANOVA was performed for statistical analysis. Abbreviations: ANOVA, analysis of variance; Co-IP, co-immunoprecipitation; CRISPLD2, cysteine-rich secreted protein LCCL domain 2; GRP78, 78 kDa glucose-regulated protein; HMGB1, high mobility group box 1; WGA, wheat germ agglutinin.

Article Snippet: The primary hepatocytes were treated with 5 μg/mL recombinant mouse HMGB1 protein (50913-M01H; Sino Biological, Beijing, China) for 3, 9, 18, 24, and 48 hours or 1, 5, 10, and 20 μg/mL recombinant mouse CRISPLD2 protein (CSB-YP805372MO; Cusabio, Hubei, Wuhan) for 24 hours.

Techniques: Translocation Assay, Western Blot, Co-Immunoprecipitation Assay, Binding Assay, Pull Down Assay, Staining, Labeling, Immunoprecipitation

Journal: Redox Biology

Article Title: A novel photosensitizer-based photodynamic therapy reprograms the Kynurenine–AhR axis to boost antitumor immunity in breast cancer

doi: 10.1016/j.redox.2026.104171

Figure Lengend Snippet: DTP-PDT attenuates the IDO–Kyn–AhR axis and relieves immune-suppression in the TME. (A-D) Targeted metabolomics analysis of Trp, Kyn, QA, and 5-HT in cell samples. (E) Targeted metabolomics of Kyn in tumor tissue samples. (F) Levels of Kyn in culture supernatants after the indicated various treatments under IFN-γ priming (n = 3). (G) Representative immunofluorescence images of tumor sections stained for CD3 (green), AhR (red), and DAPI (blue). Scale bar = 20 μm. (H) RT-qPCR analysis of Cyp1a1, Cyp1b1, and Ahrr mRNA expression in tumor-infiltrating CD3 + T cells (n = 4). (I-J) Proportion of intratumoral CD8 + T cells (gated on CD3 + T cells, n = 5). (K-L) Proportion of intratumoral Treg cells (gated on CD3 + CD4 + Foxp3 + T cells, n = 5). (M) Representative immunofluorescence images of tumor sections stained for CD3 (green), AhR (red), and DAPI (blue) in the Kyn rescue experiment. Scale bar = 20 μm. (N) RT-qPCR analysis of Cyp1a1, Cyp1b1, and Ahrr mRNA expression in tumor-infiltrating CD3 + T cells from the Kyn rescue experiment (n = 4). (O–P) Proportion of intratumoral CD8 + T cells in the Kyn rescue experiment (gated on CD3 + T cells, n = 5). (Q-R) Proportion of intratumoral Treg cells in the Kyn rescue experiment (gated on CD3 + CD4 + Foxp3 + T cells, n = 5). Data are shown as mean ± SD. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Article Snippet: 4T1 cells (5 × 10 5 cells/well) were seeded in 6-well plates and allowed to adhere for 24 h. To activate IDO1 activity, cells were pretreated with recombinant mouse interferon-γ (IFN-γ) (50 ng/mL, 485-MI, R&D System) for 24 h. After IFN-γ priming, cells were treated with DTP-PDT and/or the IDO1 inhibitor (NLG919, Aladdin).

Techniques: Immunofluorescence, Staining, Quantitative RT-PCR, Expressing

Journal: JID Innovations

Article Title: A neuroimmune axis linking S100A8/9 to itch sensitization in both bullous pemphigoid and atopic dermatitis

doi: 10.1016/j.xjidi.2026.100470

Figure Lengend Snippet: Increased S100A8/9 expression in the skin and serum of patients with BP and AD. ( a ) Immunohistochemical analysis with anti-S100A8/9 antibody showing the expression of S100A8/9 in keratinocytes and infiltrating inflammatory cells of lesional skin of patients with BP and AD. S100A8/9 expression was not observed in the healthy skin. Scale bar: 100 μm. (b) Quantification of the expression level of S100A8/9. (control, n = 2; BP, n = 5; AD n = 2). Inter-patient heterogeneity of the expression level of S100A8/9 was observed in the BP skin samples, and representative images of both low and high S100A8/9 expression were shown in A. (c) ELISA analysis showing increased S100A8/9 concentrations in the serum of patients with BP. (control, n = 8; BP, n = 16; P = .0087, Mann-Whitney test). Data are reported as mean ± SD. AD, atopic dermatitis; BP, bullous pemphigoid.

Article Snippet: Chemicals used are listed as follows: S100A8, S100A9, and S100A8/9 (100 ng/ml, R&D Systems, 9877-S8, 2065-S9, 8916-S8), Bam8-22 (1 μM, custom synthesized by Genscript), and capsaicin (Sigma M2028, 1 μM).

Techniques: Expressing, Immunohistochemical staining, Control, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY

Journal: JID Innovations

Article Title: A neuroimmune axis linking S100A8/9 to itch sensitization in both bullous pemphigoid and atopic dermatitis

doi: 10.1016/j.xjidi.2026.100470

Figure Lengend Snippet: S100A8/9 directly activates small-diameter, nociceptive DRG sensory neurons. ( a ) Representative fluorescent images of cultured DRG sensory neurons isolated from Pirt GCaMP3/+ mice before and after S100A8/9 (100 ng/ml) application. Arrows point to sensory neurons showing increased GCaMP3 fluorescence levels after S100A8/9 application. (b) Histogram showing size distribution of S100A8/9-responsive neurons. (c–e) Representative traces of DRG neurons evoked by indicated chemicals, including S100A8/9 (100 ng/ml), S100A8 (100 ng/ml), S100A9 (100 ng/ml), capsaicin (1 μM), and KCl (75 mM) in a calcium imaging assay. All S100A8/9-sensitive neurons responded to capsaicin and KCl. The majority of S100A8- and S100A9-responsive neurons also responded to S100A8/9. The three different colors (Red, Green, and Blue) represent individual cells in C-E. (f) TAK-242 inhibited S100A8/9-induced calcium responses in sensory neurons. (n = 3 for both groups P = .018, Welch’s t -test). Data are reported as mean ± SD. AD, atopic dermatitis; BP, bullous pemphigoid; DRG, dorsal root ganglia.

Article Snippet: Chemicals used are listed as follows: S100A8, S100A9, and S100A8/9 (100 ng/ml, R&D Systems, 9877-S8, 2065-S9, 8916-S8), Bam8-22 (1 μM, custom synthesized by Genscript), and capsaicin (Sigma M2028, 1 μM).

Techniques: Cell Culture, Isolation, Fluorescence, Imaging

Journal: JID Innovations

Article Title: A neuroimmune axis linking S100A8/9 to itch sensitization in both bullous pemphigoid and atopic dermatitis

doi: 10.1016/j.xjidi.2026.100470

Figure Lengend Snippet: S100A8/9 potentiate histamine-induced itch. ( a ) Subcutaneous injection of S100A8/9 (20 μg/ml) into the nape of the neck of wild-type mice does not induce scratching behavior. (n = 7 for both groups, P = .97, Welch’s t test). (b) Co-injection of S100A8/9 increased histamine (20 mM)-induced scratching behavior. (n = 11 for both groups, P = .038, Welch’s t test). Data are reported as mean ± SD.

Article Snippet: Chemicals used are listed as follows: S100A8, S100A9, and S100A8/9 (100 ng/ml, R&D Systems, 9877-S8, 2065-S9, 8916-S8), Bam8-22 (1 μM, custom synthesized by Genscript), and capsaicin (Sigma M2028, 1 μM).

Techniques: Injection