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TargetMol hmgb1 levels
Hmgb1 Levels, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hmgb1+levels/HMGB1+Protein%2C+Rat%2C+Recombinant/10__31083_slash_fbl45524-81-12-31
Average 94 stars, based on 2 article reviews

hmgb1 levels - by Bioz Stars, 2026-09

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Activation Assay:

Article Title: Berberine Alleviates Lipopolysaccharide-Induced Acute Lung Injury by Modulating the AMPK-HMGB1-NF-κB Signaling Axis
Article Snippet: Similarly, RAW264.7 cells were pretreated with 2 and 10 μM BBR and then simultaneously treated with 1 μg/mL recombinant mouse HMGB1 (rmHMGB1, 50913-M01H, Sino Biological, Beijing, China) protein for 24 h to evaluate NF-κB activation and the inflammatory response. .. To investigate whether AMPK activation byBBR contributes to the reduction of extracellular HMGB1 levels in LPS-stimulated RAW264.7 cells, we inhibited AMPK activation using RNA silencing or the inhibitor compound C (#T1977, TargetMol, Boston, MA, USA). .. Briefly, either 50 nM negative control siRNA or siRNA targeting AMPKα 1 (target sequence: 5′-ATGATGTCAGATGGTGAATTT-3′), synthesized by Sangon Biotech (Shanghai, China) [20,21] was transiently transfected into RAW264.7 cells via Lipofectamine RNAiMAX reagent (13778, Invitrogen, Carlsbad, CA, USA) and incubated for an additional 24 h. Subsequently, 0.5 μg/mL LPS, with or without 10 μM BBR treatment, was added to the culture medium for another 24 h. The protein expressions of AMPKα1 and p-AMPKα1 were detected by Western blot, while the extracellular HMGB1 content was measured using the ELISA method.

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HMGB1 released from necrotic hepatocytes promotes inflammation and migration in macrophages by activating FASN-mediated DNL. (A) Serum levels of HMGB1 in the AILI model mouse were detected using ELISA. (B, C) AML12 cells were stimulated with APAP (5 mM) for 24 hours, and levels of HMGB1 protein were measured with a western blot. RAW264.7 cells were stimulated with recombinant HMGB1 (100 ng/mL) for 24 hours. (D, E) The expression of FASN was detected with western blot. (F) Representative images of BODIPY493/503 fluorescent dye staining of intracellular neutral lipids. Bar=50 μm. (G) Cell migration was assessed using a transwell assay. bar=50μm. (H) mRNA levels of Tnf-α and Il-1β . AML12 cells were transfected with siRNA to silence Hmgb1 expression, and the cell culture supernatant of AML12 cells with APAP treatment was collected as the CM. RAW246.7 cells were stimulated with CM. Levels of FASN protein (I, J), migration (K), and mRNA levels of Tnf-α and Il-1β. (L) were measured, respectively, bar=50 μm. Data are means±SEMs. Two-tailed unpaired Student t tests were performed for statistical analysis. * p <0.05, ** p <0.01, *** p <0.001. Abbreviations: APAP, acetaminophen; AILI, APAP-induced liver injury; CM, conditioned media; NC, negative control; SiRNA, small interfering RNA.

Journal: Hepatology Communications

Article Title: Targeting fatty acid metabolism in hepatic macrophages mitigates acetaminophen-induced liver injury and promotes regeneration in mice

doi: 10.1097/HC9.0000000000000865

Figure Lengend Snippet: HMGB1 released from necrotic hepatocytes promotes inflammation and migration in macrophages by activating FASN-mediated DNL. (A) Serum levels of HMGB1 in the AILI model mouse were detected using ELISA. (B, C) AML12 cells were stimulated with APAP (5 mM) for 24 hours, and levels of HMGB1 protein were measured with a western blot. RAW264.7 cells were stimulated with recombinant HMGB1 (100 ng/mL) for 24 hours. (D, E) The expression of FASN was detected with western blot. (F) Representative images of BODIPY493/503 fluorescent dye staining of intracellular neutral lipids. Bar=50 μm. (G) Cell migration was assessed using a transwell assay. bar=50μm. (H) mRNA levels of Tnf-α and Il-1β . AML12 cells were transfected with siRNA to silence Hmgb1 expression, and the cell culture supernatant of AML12 cells with APAP treatment was collected as the CM. RAW246.7 cells were stimulated with CM. Levels of FASN protein (I, J), migration (K), and mRNA levels of Tnf-α and Il-1β. (L) were measured, respectively, bar=50 μm. Data are means±SEMs. Two-tailed unpaired Student t tests were performed for statistical analysis. * p <0.05, ** p <0.01, *** p <0.001. Abbreviations: APAP, acetaminophen; AILI, APAP-induced liver injury; CM, conditioned media; NC, negative control; SiRNA, small interfering RNA.

Article Snippet: HMGB1 levels in mouse serum and culture supernatants of APAP-treated AML12 cells were measured via a mouse HMGB1 ELISA kit (Cusabio, CSB-E08225m) according to the manufacturer’s instructions.

Techniques: Migration, Enzyme-linked Immunosorbent Assay, Western Blot, Recombinant, Expressing, Staining, Transwell Assay, Transfection, Cell Culture, Two Tailed Test, Negative Control, Small Interfering RNA

HMGB1 enhances the inflammatory response and facilitates the migration of macrophages through the PI3K/AKT-SREBP1/FASN signaling pathway. (A, B) HMGB1 was used to stimulate RAW246.7 cells for the indicated durations. The protein levels of PI3K/p-PI3K and AKT/p-AKT were detected with western blot. RAW246.7 cells were pretreated with the PI3K inhibitor, LY294002 (50 μM), then stimulated with HMGB1. (C, D) The levels of FASN protein were detected with western blot. (E) mRNA levels of Tnf-α and Il-1β . (F, G) The protein levels of SREBP1 in HMGB1-treated RAW264.7 cells were detected with western blot. (H, I) After pretreatment with LY294002, SREBP1 protein levels in RAW246.7 cells exposed to HMGB1 were analyzed using western blot. RAW246.7 cells were pretreated with Fatostatin (10 mM), an inhibitor of SREBP1, and stimulated with HMGB1. (J, K) Protein levels of FASN were analyzed using western blot. (L) mRNA levels of Tnf-α and Il-1β . The data are the means±SEMs. Two-tailed unpaired Student t tests were performed for statistical analysis. * p <0.05, ** p <0.01, *** p <0.001. Abbreviations: FASN, fatty acid synthase; HMGB1, high-mobility group protein B1.

Journal: Hepatology Communications

Article Title: Targeting fatty acid metabolism in hepatic macrophages mitigates acetaminophen-induced liver injury and promotes regeneration in mice

doi: 10.1097/HC9.0000000000000865

Figure Lengend Snippet: HMGB1 enhances the inflammatory response and facilitates the migration of macrophages through the PI3K/AKT-SREBP1/FASN signaling pathway. (A, B) HMGB1 was used to stimulate RAW246.7 cells for the indicated durations. The protein levels of PI3K/p-PI3K and AKT/p-AKT were detected with western blot. RAW246.7 cells were pretreated with the PI3K inhibitor, LY294002 (50 μM), then stimulated with HMGB1. (C, D) The levels of FASN protein were detected with western blot. (E) mRNA levels of Tnf-α and Il-1β . (F, G) The protein levels of SREBP1 in HMGB1-treated RAW264.7 cells were detected with western blot. (H, I) After pretreatment with LY294002, SREBP1 protein levels in RAW246.7 cells exposed to HMGB1 were analyzed using western blot. RAW246.7 cells were pretreated with Fatostatin (10 mM), an inhibitor of SREBP1, and stimulated with HMGB1. (J, K) Protein levels of FASN were analyzed using western blot. (L) mRNA levels of Tnf-α and Il-1β . The data are the means±SEMs. Two-tailed unpaired Student t tests were performed for statistical analysis. * p <0.05, ** p <0.01, *** p <0.001. Abbreviations: FASN, fatty acid synthase; HMGB1, high-mobility group protein B1.

Techniques: Migration, Western Blot, Two Tailed Test

Elevated HMGB1 Expression in MM cell lines and xenograft models. ( A ) Relative HMGB1 mRNA levels in MM cell lines (NCI-H2452 and MSTO-211H) compared to normal mesothelial cells (MeT-5A), determined by quantitative real-time PCR. ( B ) Representative Western blot images showing HMGB1 protein expression in MM cell lines (NCI-H2452 and MSTO-211H) and normal mesothelial cells (MeT-5A). ( C ) Representative images of tumors from the MM xenograft model established by subcutaneous injection of MSTO-211H cells into BALB/c nude mice. ( D ) Plasma HMGB1 levels measured by ELISA in xenograft model mice. **, p < 0.01; ***, p < 0.001.

Journal: Toxics

Article Title: HMGB1 as a Key Mediator in Malignant Mesothelioma and a Potential Target for Asbestos-Related Cancer Therapy

doi: 10.3390/toxics13060448

Figure Lengend Snippet: Elevated HMGB1 Expression in MM cell lines and xenograft models. ( A ) Relative HMGB1 mRNA levels in MM cell lines (NCI-H2452 and MSTO-211H) compared to normal mesothelial cells (MeT-5A), determined by quantitative real-time PCR. ( B ) Representative Western blot images showing HMGB1 protein expression in MM cell lines (NCI-H2452 and MSTO-211H) and normal mesothelial cells (MeT-5A). ( C ) Representative images of tumors from the MM xenograft model established by subcutaneous injection of MSTO-211H cells into BALB/c nude mice. ( D ) Plasma HMGB1 levels measured by ELISA in xenograft model mice. **, p < 0.01; ***, p < 0.001.

Article Snippet: Plasma HMGB1 levels were quantified using a Mouse HMGB1 ELISA kit (Wuhan Huamei Cusabio Biotech Co., Wuhan, China).

Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Injection, Clinical Proteomics, Enzyme-linked Immunosorbent Assay

Effect of HMGB1 silencing on MM cell migration and invasion. Scratch wound healing assays showing the migration of MSTO-211H ( A ) and NCI-H2452 cells ( B ) treated with blank control, siRNA control, and HMGB1 siRNA at 0, 24, 48, and 72 h. Representative images and quantification of Transwell assays assessing invasion in MSTO-211H and NCI-H2452 cells ( C ) treated with blank control, siRNA control, and HMGB1 siRNA. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. black group; ## p < 0.01, ### p < 0.001 vs. siRNA control group.

Journal: Toxics

Article Title: HMGB1 as a Key Mediator in Malignant Mesothelioma and a Potential Target for Asbestos-Related Cancer Therapy

doi: 10.3390/toxics13060448

Figure Lengend Snippet: Effect of HMGB1 silencing on MM cell migration and invasion. Scratch wound healing assays showing the migration of MSTO-211H ( A ) and NCI-H2452 cells ( B ) treated with blank control, siRNA control, and HMGB1 siRNA at 0, 24, 48, and 72 h. Representative images and quantification of Transwell assays assessing invasion in MSTO-211H and NCI-H2452 cells ( C ) treated with blank control, siRNA control, and HMGB1 siRNA. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. black group; ## p < 0.01, ### p < 0.001 vs. siRNA control group.

Article Snippet: Plasma HMGB1 levels were quantified using a Mouse HMGB1 ELISA kit (Wuhan Huamei Cusabio Biotech Co., Wuhan, China).

Techniques: Migration, Control

Effect of HMGB1 silencing and EP treatment on cell cycle arrest and apoptosis. Comparison of apoptosis in MSTO-211H ( A ) and NCI-H2452 ( B ) cells treated with blank control, siRNA control, and HMGB1 siRNA. Cell cycle distribution in MSTO-211H ( C ) and NCI-H2452 ( D ) cells treated with 0, 2.5, 5, and 10 mM EP. Apoptosis analysis of MSTO-211H ( E ) and NCI-H2452 ( F ) cells treated with 0, 2.5, 5, 10, and 20 mM EP. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01 vs. siRNA control group.

Journal: Toxics

Article Title: HMGB1 as a Key Mediator in Malignant Mesothelioma and a Potential Target for Asbestos-Related Cancer Therapy

doi: 10.3390/toxics13060448

Figure Lengend Snippet: Effect of HMGB1 silencing and EP treatment on cell cycle arrest and apoptosis. Comparison of apoptosis in MSTO-211H ( A ) and NCI-H2452 ( B ) cells treated with blank control, siRNA control, and HMGB1 siRNA. Cell cycle distribution in MSTO-211H ( C ) and NCI-H2452 ( D ) cells treated with 0, 2.5, 5, and 10 mM EP. Apoptosis analysis of MSTO-211H ( E ) and NCI-H2452 ( F ) cells treated with 0, 2.5, 5, 10, and 20 mM EP. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01 vs. siRNA control group.

Article Snippet: Plasma HMGB1 levels were quantified using a Mouse HMGB1 ELISA kit (Wuhan Huamei Cusabio Biotech Co., Wuhan, China).

Techniques: Comparison, Control

Effect of TAK-242 and TLR4 siRNA treatment on HMGB1-TLR4 signaling pathway in MM cells. The mRNA expression of key molecules in the HMGB1-TLR4 signaling axis in MSTO-211H ( A ) and NCI-H2452 ( B ) cells treated with 0 and 100 μM TAK-242. The mRNA expression of key molecules in the HMGB1-TLR4 signaling axis in MSTO-211H ( C ) and NCI-H2452 ( D ) cells treated with TLR4 siRNA. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01, ### p < 0.001 vs. siRNA control group.

Journal: Toxics

Article Title: HMGB1 as a Key Mediator in Malignant Mesothelioma and a Potential Target for Asbestos-Related Cancer Therapy

doi: 10.3390/toxics13060448

Figure Lengend Snippet: Effect of TAK-242 and TLR4 siRNA treatment on HMGB1-TLR4 signaling pathway in MM cells. The mRNA expression of key molecules in the HMGB1-TLR4 signaling axis in MSTO-211H ( A ) and NCI-H2452 ( B ) cells treated with 0 and 100 μM TAK-242. The mRNA expression of key molecules in the HMGB1-TLR4 signaling axis in MSTO-211H ( C ) and NCI-H2452 ( D ) cells treated with TLR4 siRNA. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01, ### p < 0.001 vs. siRNA control group.

Article Snippet: Plasma HMGB1 levels were quantified using a Mouse HMGB1 ELISA kit (Wuhan Huamei Cusabio Biotech Co., Wuhan, China).

Techniques: Expressing, Control

Effect of EP and TAK-242 treatment on MM xenograft model in vivo. ( A ) Representative images of mice and tumors after treatment treated with PBS, EP, or TAK-242. ( B ) Changes in body weight of mice over time after PBS, EP, or TAK-242 treatment. ( C ) Tumor volume measurements over time in mice treated with PBS, EP, or TAK-242. ( D ) Tumor weights in mice treated with PBS, EP, or TAK-242. ( E ) H&E staining of tumor tissues from PBS, EP, and TAK-242 treated groups. ( F ) Immunohistochemical staining showing HMGB1 expression in tumor tissues from the three treatment groups. ( G ) Plasma HMGB1 levels measured by ELISA in the three treatment groups. * p < 0.05.

Journal: Toxics

Article Title: HMGB1 as a Key Mediator in Malignant Mesothelioma and a Potential Target for Asbestos-Related Cancer Therapy

doi: 10.3390/toxics13060448

Figure Lengend Snippet: Effect of EP and TAK-242 treatment on MM xenograft model in vivo. ( A ) Representative images of mice and tumors after treatment treated with PBS, EP, or TAK-242. ( B ) Changes in body weight of mice over time after PBS, EP, or TAK-242 treatment. ( C ) Tumor volume measurements over time in mice treated with PBS, EP, or TAK-242. ( D ) Tumor weights in mice treated with PBS, EP, or TAK-242. ( E ) H&E staining of tumor tissues from PBS, EP, and TAK-242 treated groups. ( F ) Immunohistochemical staining showing HMGB1 expression in tumor tissues from the three treatment groups. ( G ) Plasma HMGB1 levels measured by ELISA in the three treatment groups. * p < 0.05.

Article Snippet: Plasma HMGB1 levels were quantified using a Mouse HMGB1 ELISA kit (Wuhan Huamei Cusabio Biotech Co., Wuhan, China).

Techniques: In Vivo, Staining, Immunohistochemical staining, Expressing, Clinical Proteomics, Enzyme-linked Immunosorbent Assay

Fig. 4 HMGB1 induction in brain tissue, PMNs, and serum after PTS. A, B HMGB1 levels in the cortical cores or penumbras of ischemic hemispheres were measured 6, 12, and 24 h post-PTS using immunoblotting. C, D HMGB1 levels in blood PMNs (C) and serum (D) were assessed 1, 3, 6, 12, and 24 h after PTS using immunoblotting and ELISA, respectively. Results are presented as mean ± SEM (n = 4). *p < 0.05, **p < 0.01, ***p < 0.001 compared to sham controls in the core and PMNs and #p < 0.05, ##p < 0.01 compared to sham controls in the penumbra, and &p < 0.05 between indicated groups

Journal: Molecular medicine (Cambridge, Mass.)

Article Title: Platelet-derived HMGB1 induces NETosis, exacerbating brain damage in the photothrombotic stroke model.

doi: 10.1186/s10020-025-01107-7

Figure Lengend Snippet: Fig. 4 HMGB1 induction in brain tissue, PMNs, and serum after PTS. A, B HMGB1 levels in the cortical cores or penumbras of ischemic hemispheres were measured 6, 12, and 24 h post-PTS using immunoblotting. C, D HMGB1 levels in blood PMNs (C) and serum (D) were assessed 1, 3, 6, 12, and 24 h after PTS using immunoblotting and ELISA, respectively. Results are presented as mean ± SEM (n = 4). *p < 0.05, **p < 0.01, ***p < 0.001 compared to sham controls in the core and PMNs and #p < 0.05, ##p < 0.01 compared to sham controls in the penumbra, and &p < 0.05 between indicated groups

Article Snippet: Serum HMGB1 levels were assessed using ELISA kits (Cusabio, Houston, TX, USA), according to the manufacturer’s instructions.

Techniques: Western Blot, Enzyme-linked Immunosorbent Assay

Fig. 5 Localization of HMGB1 induction in brain tissue after PTS and its intravascular localization. Coronal brain sections were prepared from sham controls (A, D) and the penumbra of the ischemic hemisphere of PTS animals at 3 h (B) and 24 h post-PTS (C, E, F). Immunofluorescence staining was performed with anti-NeuN antibody, anti-HMGB1 antibody, and DAPI (A–C) or with anti-Ly6G antibody, anti-HMGB1 antibody, anti-CD42b antibody, and DAPI (D–F). Arrows indicate co-localization of anti-HMGB1 with anti-NeuN (B, C1–C4), and arrowheads point to localization of anti-HMGB1 in NeuN-negative cells (A, B, C1, C3, C4), double arrows indicate co-localization of anti-HMGB1 with Ly6G-positive cells (F2-1), double arrowheads point to co-localization of anti-HMGB1 in CD42b-positive cells (F2-2), and asterisks and double asterisks point to localization of HMGB1 in the blood vessel (B, C2, C4, F1, F2). Scale bars represent 20 µm in D–F or 50 µm in A, B, C, F1, F2, and F2-1-F2-3

Journal: Molecular medicine (Cambridge, Mass.)

Article Title: Platelet-derived HMGB1 induces NETosis, exacerbating brain damage in the photothrombotic stroke model.

doi: 10.1186/s10020-025-01107-7

Figure Lengend Snippet: Fig. 5 Localization of HMGB1 induction in brain tissue after PTS and its intravascular localization. Coronal brain sections were prepared from sham controls (A, D) and the penumbra of the ischemic hemisphere of PTS animals at 3 h (B) and 24 h post-PTS (C, E, F). Immunofluorescence staining was performed with anti-NeuN antibody, anti-HMGB1 antibody, and DAPI (A–C) or with anti-Ly6G antibody, anti-HMGB1 antibody, anti-CD42b antibody, and DAPI (D–F). Arrows indicate co-localization of anti-HMGB1 with anti-NeuN (B, C1–C4), and arrowheads point to localization of anti-HMGB1 in NeuN-negative cells (A, B, C1, C3, C4), double arrows indicate co-localization of anti-HMGB1 with Ly6G-positive cells (F2-1), double arrowheads point to co-localization of anti-HMGB1 in CD42b-positive cells (F2-2), and asterisks and double asterisks point to localization of HMGB1 in the blood vessel (B, C2, C4, F1, F2). Scale bars represent 20 µm in D–F or 50 µm in A, B, C, F1, F2, and F2-1-F2-3

Article Snippet: Serum HMGB1 levels were assessed using ELISA kits (Cusabio, Houston, TX, USA), according to the manufacturer’s instructions.

Techniques: Immunofluorescence, Staining

Fig. 6 Intranasal administration of HMGB1 A box at 4 h after PTS suppresses NETosis induction in the post-PTS brain. HMGB1 A box (5 µg/kg) was administered intranasally at 30 min before or 2 or 4 h after PTS. A–C CitH3 and MPO levels were examined in PMNs isolated 12 h after PTS. D Levels of cell-free DNA in serum were measured 12 h after PTS. E, F Coronal brain sections were obtained 24 h after PTS and stained with TTC to visualize the infarcts. Representative images (E) and mean infarct volumes (F) are shown. G Neurological deficits, measured using modified neurological severity scores, were evaluated 24 h post-PTS. Data are presented as the mean ± SEM (n = 4 or 6). Sham, sham-operated animals (n = 4); MCAO, saline-treated PTS control animals (n = 4); PTS + -30 min, PTS animals administered HMGB1 A box 30 min before PTS (n = 6); PTS + 2 h, PTS animals administered HMGB1 A box 2 h after PTS (n = 6); PTS + 4 h, PTS animals administered HMGB1 A box 4 h after PTS (n = 6). *p < 0.05, **p < 0.01, ***p < 0.001 compared to the sham controls and #p < 0.05, ###p < 0.001, $p < 0.05 between indicated groups

Journal: Molecular medicine (Cambridge, Mass.)

Article Title: Platelet-derived HMGB1 induces NETosis, exacerbating brain damage in the photothrombotic stroke model.

doi: 10.1186/s10020-025-01107-7

Figure Lengend Snippet: Fig. 6 Intranasal administration of HMGB1 A box at 4 h after PTS suppresses NETosis induction in the post-PTS brain. HMGB1 A box (5 µg/kg) was administered intranasally at 30 min before or 2 or 4 h after PTS. A–C CitH3 and MPO levels were examined in PMNs isolated 12 h after PTS. D Levels of cell-free DNA in serum were measured 12 h after PTS. E, F Coronal brain sections were obtained 24 h after PTS and stained with TTC to visualize the infarcts. Representative images (E) and mean infarct volumes (F) are shown. G Neurological deficits, measured using modified neurological severity scores, were evaluated 24 h post-PTS. Data are presented as the mean ± SEM (n = 4 or 6). Sham, sham-operated animals (n = 4); MCAO, saline-treated PTS control animals (n = 4); PTS + -30 min, PTS animals administered HMGB1 A box 30 min before PTS (n = 6); PTS + 2 h, PTS animals administered HMGB1 A box 2 h after PTS (n = 6); PTS + 4 h, PTS animals administered HMGB1 A box 4 h after PTS (n = 6). *p < 0.05, **p < 0.01, ***p < 0.001 compared to the sham controls and #p < 0.05, ###p < 0.001, $p < 0.05 between indicated groups

Article Snippet: Serum HMGB1 levels were assessed using ELISA kits (Cusabio, Houston, TX, USA), according to the manufacturer’s instructions.

Techniques: Isolation, Staining, Modification, Saline, Control

Fig. 7 Rapid activation of platelet following PTS. Platelets were isolated 1, 3, 6, 12, and 24 h post-PTS, and protein levels of P-selectin (A), CD42b (B, C), phospho-AKT and AKT (D), and HMGB1 (E) were examined by immunoblotting. C Levels of CD42b were also examined in serum at 1, 3, 6, 12, and 24 h post-PTS by immunoblotting. Representative images are shown and quantified data are presented as mean ± SEM (n = 6 for A, D, E and n = 4 for C). *p < 0.05, **p < 0.01, ***p < 0.001 compared to sham group. F Platelets were isolated from sham-operated or at 1 and 3 h post-PTS and stained with anti-HMGB1 antibody. Arrows indicate concentrated HMGB1 immunoreactivity in plasma membrane. Double arrows indicate diffused HMGB1 immunoreactivity outer surface of plasma membrane. Scale bars represent 10 µm

Journal: Molecular medicine (Cambridge, Mass.)

Article Title: Platelet-derived HMGB1 induces NETosis, exacerbating brain damage in the photothrombotic stroke model.

doi: 10.1186/s10020-025-01107-7

Figure Lengend Snippet: Fig. 7 Rapid activation of platelet following PTS. Platelets were isolated 1, 3, 6, 12, and 24 h post-PTS, and protein levels of P-selectin (A), CD42b (B, C), phospho-AKT and AKT (D), and HMGB1 (E) were examined by immunoblotting. C Levels of CD42b were also examined in serum at 1, 3, 6, 12, and 24 h post-PTS by immunoblotting. Representative images are shown and quantified data are presented as mean ± SEM (n = 6 for A, D, E and n = 4 for C). *p < 0.05, **p < 0.01, ***p < 0.001 compared to sham group. F Platelets were isolated from sham-operated or at 1 and 3 h post-PTS and stained with anti-HMGB1 antibody. Arrows indicate concentrated HMGB1 immunoreactivity in plasma membrane. Double arrows indicate diffused HMGB1 immunoreactivity outer surface of plasma membrane. Scale bars represent 10 µm

Article Snippet: Serum HMGB1 levels were assessed using ELISA kits (Cusabio, Houston, TX, USA), according to the manufacturer’s instructions.

Techniques: Activation Assay, Isolation, Western Blot, Staining, Clinical Proteomics, Membrane

Fig. 8 Platelet HMGB1 triggers NETosis following PTS in TLR4- and CXCR4-dependent manner. A Schematic illustration of the co-culture protocol for normal PMNs and platelets isolated from PTS animals. B–E Normal PMNs were seeded onto six-well-plate and cultured for 24 h and then co-cultured with platelets isolated from sham-operated or at 1 or 3 h post-PTS animals for 3 h. (B–E) PMNs were pre-incubated with HMGB1 A box (100 ng/mL) or A438079 (20 µM) for 30 min before co-culture with platelets. ATP treatment (25 µM) was used as a positive control. Protein expression of CitH3, MPO, and HMGB1 was assessed by immunoblotting (B, C, E) and levels of cell-free DNA in serum were measured (D). F PMNs were pre-incubated with TLR4-IN-C34 (20 µM), AMD3100 (20 µM), or FPS-ZM1 (150 nM) for 30 min before co-culture with platelets. Representative images are shown and quantified data are presented as mean ± SEM (n = 4–6). *p < 0.05, ***p < 0.001 compared to sham group and #p < 0.05, ##p < 0.01, ###p < 0.001, &p < 0.05, &&&p < 0.001, $p < 0.05 between indicated groups

Journal: Molecular medicine (Cambridge, Mass.)

Article Title: Platelet-derived HMGB1 induces NETosis, exacerbating brain damage in the photothrombotic stroke model.

doi: 10.1186/s10020-025-01107-7

Figure Lengend Snippet: Fig. 8 Platelet HMGB1 triggers NETosis following PTS in TLR4- and CXCR4-dependent manner. A Schematic illustration of the co-culture protocol for normal PMNs and platelets isolated from PTS animals. B–E Normal PMNs were seeded onto six-well-plate and cultured for 24 h and then co-cultured with platelets isolated from sham-operated or at 1 or 3 h post-PTS animals for 3 h. (B–E) PMNs were pre-incubated with HMGB1 A box (100 ng/mL) or A438079 (20 µM) for 30 min before co-culture with platelets. ATP treatment (25 µM) was used as a positive control. Protein expression of CitH3, MPO, and HMGB1 was assessed by immunoblotting (B, C, E) and levels of cell-free DNA in serum were measured (D). F PMNs were pre-incubated with TLR4-IN-C34 (20 µM), AMD3100 (20 µM), or FPS-ZM1 (150 nM) for 30 min before co-culture with platelets. Representative images are shown and quantified data are presented as mean ± SEM (n = 4–6). *p < 0.05, ***p < 0.001 compared to sham group and #p < 0.05, ##p < 0.01, ###p < 0.001, &p < 0.05, &&&p < 0.001, $p < 0.05 between indicated groups

Article Snippet: Serum HMGB1 levels were assessed using ELISA kits (Cusabio, Houston, TX, USA), according to the manufacturer’s instructions.

Techniques: Co-Culture Assay, Isolation, Cell Culture, Incubation, Positive Control, Expressing, Western Blot

Fig. 9 Diagram of the interplay between activated platelets and neutrophils in PTS and the function of HMGB1. HMGB1 is released from neurons and glia during the acute phase after PTS. This released HMGB1 accumulates within blood vessels, activating platelets and inducing NETosis. Activated platelets release HMGB1, further amplifying NETosis. Platelets adhere to the endothelium and interact with NETs, trapping circulating procoagulant factors and red blood cells (RBCs). This leads to the formation of neutrophils-platelets aggregates, where HMGB1 derived from both activated platelets and NETosed neutrophils likely plays a critical role. Administration of BBCA or HMGB1 A box can suppress this process. HMGB1, High mobility group box 1; BBCA, BB-Cl-amidine; RBCs, red blood cells

Journal: Molecular medicine (Cambridge, Mass.)

Article Title: Platelet-derived HMGB1 induces NETosis, exacerbating brain damage in the photothrombotic stroke model.

doi: 10.1186/s10020-025-01107-7

Figure Lengend Snippet: Fig. 9 Diagram of the interplay between activated platelets and neutrophils in PTS and the function of HMGB1. HMGB1 is released from neurons and glia during the acute phase after PTS. This released HMGB1 accumulates within blood vessels, activating platelets and inducing NETosis. Activated platelets release HMGB1, further amplifying NETosis. Platelets adhere to the endothelium and interact with NETs, trapping circulating procoagulant factors and red blood cells (RBCs). This leads to the formation of neutrophils-platelets aggregates, where HMGB1 derived from both activated platelets and NETosed neutrophils likely plays a critical role. Administration of BBCA or HMGB1 A box can suppress this process. HMGB1, High mobility group box 1; BBCA, BB-Cl-amidine; RBCs, red blood cells

Article Snippet: Serum HMGB1 levels were assessed using ELISA kits (Cusabio, Houston, TX, USA), according to the manufacturer’s instructions.

Techniques: Derivative Assay

Comparison of biomarkers in different phases and groups.

Journal: Frontiers in Immunology

Article Title: Assessing the inflammation in pediatric MOGAD: Significance of CSF HMGB1 and related biomarkers

doi: 10.3389/fimmu.2025.1534172

Figure Lengend Snippet: Comparison of biomarkers in different phases and groups.

Article Snippet: NLRP3 (ElAab, Wuhan, China) and HMGB1 levels (Elabscience, Wuhan, China) in CSF samples were quantified using enzyme-linked immunosorbent assay (ELISA) kits, according to the manufacturer’s instructions.

Techniques: Comparison, Control

Comparison of NLRP3, HMGB1, IL-6, and IL-33 levels in CSF samples of patients with MOGAD during the acute stage, in remission, and with controls. NLRP3 (A) , HMGB1 (B) , and IL-6 (C) levels in the CSF of patients with MOGAD during the acute stage were significantly higher than those in the controls and remission (* P < 0.05, ** P < 0.01, *** P < 0.001). No significant difference was observed in IL-33 (D) levels in the CSF of patients with MOGAD at different time points ( P >0.05).

Journal: Frontiers in Immunology

Article Title: Assessing the inflammation in pediatric MOGAD: Significance of CSF HMGB1 and related biomarkers

doi: 10.3389/fimmu.2025.1534172

Figure Lengend Snippet: Comparison of NLRP3, HMGB1, IL-6, and IL-33 levels in CSF samples of patients with MOGAD during the acute stage, in remission, and with controls. NLRP3 (A) , HMGB1 (B) , and IL-6 (C) levels in the CSF of patients with MOGAD during the acute stage were significantly higher than those in the controls and remission (* P < 0.05, ** P < 0.01, *** P < 0.001). No significant difference was observed in IL-33 (D) levels in the CSF of patients with MOGAD at different time points ( P >0.05).

Techniques: Comparison

Correlation among NLRP3, HMGB1, IL-6, and IL-33 levels in the CSF of patients with MOGAD during the acute phase. HMGB1 levels (A) in the CSF were found to be significantly correlated with NLRP3 levels ( P < 0.01, r ² = 0.410). However, no significant correlations were observed among other inflammatory factors ( P >0.05) (B–F) .

Journal: Frontiers in Immunology

Article Title: Assessing the inflammation in pediatric MOGAD: Significance of CSF HMGB1 and related biomarkers

doi: 10.3389/fimmu.2025.1534172

Figure Lengend Snippet: Correlation among NLRP3, HMGB1, IL-6, and IL-33 levels in the CSF of patients with MOGAD during the acute phase. HMGB1 levels (A) in the CSF were found to be significantly correlated with NLRP3 levels ( P < 0.01, r ² = 0.410). However, no significant correlations were observed among other inflammatory factors ( P >0.05) (B–F) .

Techniques:

Correlation between inflammatory markers in the CSF and EDSS scores in patients with MOGAD during the acute phase. HMGB1 levels (A) were highly correlated with EDSS neural function scores ( P < 0.05, r ² = 0.200). However, no significant correlations were observed among CSF NLRP3 (B) , IL-6 (C) , IL-33 (D) levels and EDSS scores ( P > 0.05).

Journal: Frontiers in Immunology

Article Title: Assessing the inflammation in pediatric MOGAD: Significance of CSF HMGB1 and related biomarkers

doi: 10.3389/fimmu.2025.1534172

Figure Lengend Snippet: Correlation between inflammatory markers in the CSF and EDSS scores in patients with MOGAD during the acute phase. HMGB1 levels (A) were highly correlated with EDSS neural function scores ( P < 0.05, r ² = 0.200). However, no significant correlations were observed among CSF NLRP3 (B) , IL-6 (C) , IL-33 (D) levels and EDSS scores ( P > 0.05).

Techniques:

Correlation between inflammatory factors in the CSF and MOGAD recurrence during the acute phase. IL-6 levels (A) in the CSF were closely related to MOGAD recurrence ( P < 0.05, r ² = 0.204). However, no significant correlations were observed between NLRP3 (B) , HMGB1 (C) , and IL-33 (D) levels and number of attacks ( P > 0.05).

Journal: Frontiers in Immunology

Article Title: Assessing the inflammation in pediatric MOGAD: Significance of CSF HMGB1 and related biomarkers

doi: 10.3389/fimmu.2025.1534172

Figure Lengend Snippet: Correlation between inflammatory factors in the CSF and MOGAD recurrence during the acute phase. IL-6 levels (A) in the CSF were closely related to MOGAD recurrence ( P < 0.05, r ² = 0.204). However, no significant correlations were observed between NLRP3 (B) , HMGB1 (C) , and IL-33 (D) levels and number of attacks ( P > 0.05).

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