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TargetMol y-27632
Y 27632, supplied by TargetMol, used in various techniques. Bioz Stars score: 95/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/y+27632/Y-27632/custom%40t1870%4042784458
Average 95 stars, based on 99 article reviews

y-27632 - by Bioz Stars, 2026-10

95/100 stars

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Inhibition:

Article Title: A Human Neural Tube Model Using 4D Self‐Folding Smart Scaffolds
Article Snippet: .. Cells were then centrifuged at 200 x g for 3 min. After pellet resuspension, cells were counted and plated at a density of 0.7 × 10 5 cells cm −2 in neural induction medium (DMEM‐F12/Neurobasal mixture 1:1, 1% N2, 2% B27, 20 μg mL −1 insulin, 1% MEM‐nonessential amino acids, 1% L‐glutamine, 0.1% 2‐mercaptoethanol) supplemented with Dual SMAD inhibition factors, i.e., 10 μ m SB431542 (TargetMol; #T1726), 100 n m LDN193189 (STEMCELL Technologies; #72144), 2 μ m XAV939 (STEMCELL Technologies; #72674), and 10 μ m Y‐27632 (TargetMol; #T1725) to increase cell survival. ..

Article Title: A Human Neural Tube Model Using 4D Self-Folding Smart Scaffolds.
Article Snippet: .. Cells were then centrifuged at 200 x g for 3 min. After pellet resuspension, cells were counted and plated at a density of 0.7 × 105 cells cm−2 in neural induction medium (DMEM-F12/Neurobasal mixture 1:1, 1% N2, 2% B27, 20 μg mL−1 insulin, 1% MEM-nonessential amino acids, 1% L-glutamine, 0.1% 2-mercaptoethanol) supplemented with Dual SMAD inhibition factors, i.e., 10 μm SB431542 (TargetMol; #T1726), 100 nm LDN193189 (STEMCELL Technologies; #72144), 2 μmXAV939 (STEMCELL Technologies; #72674), and 10 μm Y-27632 (TargetMol; #T1725) to increase cell survival. ..

Cell Culture:

Article Title: BHLHE40 Cooperates with GATA2/3 to Control Human Syncytiotrophoblast Lineage Differentiation
Article Snippet: .. TSCs were cultured in Matrigel‐coated (354277, Corning) plates and maintained in Advanced DMEM/F‐12 medium with 0.2% fetal bovine serum (FBS), 0.3% bovine serum albumin (BSA; Sigma–Aldrich, A9418), 1% ITS‐X (Gibco, 51500), 50 ng mL −1 recombinant human epidermal growth factor (EGF; Peprotech, AF‐100‐15), 2 μM m CHIR99021 (TargetMol, T2301), 0.5 μM m A83‐01 (PeproTech, 90943360), 5 μM Y‐27632 (TargetMol, T1870), 1 μM m SB431542 (TargetMol, T1726), 0.8 mM m valproic acid (TargetMol, T7064), 1.5 mg mL −1 L‐ascorbic acid (TargetMol, T0928), 0.1 mM m β‐mercaptoethanol (Thermo Fisher Scientific, 21985023), and 0.5% penicillin‐streptomycin. .. For cell passages, TSCs were washed with phosphate‐buffered saline (PBS) and dissociated by TrypLE Express (Thermo Fisher Scientific) for 5 min, followed by seeding at a 1:3 to 1:4 ratio.

Recombinant:

Centrifugation:

Article Title: Cell-of-Origin, not Oncogenic Effect, Determines Desmoplastic Immune Exclusion in KRAS-Driven Liver Cancer
Article Snippet: [ ] The pBabe-KrasG12D plasmid was reconstructed from pBabe-Kras G12D -puro (Addgene #58902) by removing the puromycin resistance gene through digestion with HindIII-HF and BspDI, blunt-ended by Klenow and re-ligation to restore plasmid circularity. .. After quenching with cold DMEM and centrifugation, cells were resuspended in chol GF+ media with 10μM of Y-27632 (TargetMol, #TMO-T1725-50mg) and plated at 450 μL/well in a 48-well plate. .. The Lenti-CRISPR-sgRNA( Trp53 ), pBabe- Kras G12D , or Lenti-luciferase-P2A-Neo plasmid (Addgene #105621) was co-transfected with packaging plasmid psPAX2 and pMD2.G (both from PlasmidFactory GmbH & Co. KG, Bielefeld, Germany) into HEK293T cells by TransIT LT1 transfection reagent according to the manufacturer’s instructions (Mirus Bio, Madison, WI, USA).

Image Search Results

LSS triggers m/lEV release via Ca 2+ ‐CaMKII‐MLC signalling. (A) LSS (15 dyn/cm 2 for 300 s) induced Piezo1 translocation to the cell periphery colocalising with the microvesicle formation site ( n = 3). PKH26, a lipophilic membrane dye for labelling the membrane structures of EVs and cells. (B) Piezo1 reduction by siRNA suppressed LSS‐induced Piezo1 translocation to the cell periphery ( n = 3). (C) Inhibition of Ca 2+ signal through Thapsigargin (TG, 1 µM) and BAPTA (10 µM) blocked Yoda1 (Piezo1 agonist, 2 µM)‐induced Piezo1 translocation to the cell periphery ( n = 3). (D) TG and BAPTA inhibited Yoda1‐induced m/lEV release as imaged by confocal microscope ( n = 200 cells from three independent experiments). (E) TG and BAPTA suppressed Yoda1‐induced m/lEV release as detected by Western blot ( n = 3). (F) TG and BAPTA inhibited Yoda1‐induced MLC phosphorylation in HUVECs ( n = 3). (G) MLC reduction did not affect the Yoda1‐induced Piezo1 translocation to the cell periphery ( n = 3). (H) MLC reduction reduced Yoda1‐induced m/lEV release as visualized by confocal microscope ( n = 200 cells from three independent experiments). (I) MLC reduction attenuated Yoda1‐induced m/lEV release as detected by Western blot ( n = 3). (J) MLC reduction decreased Yoda1‐induced MLC phosphorylation ( n = 3). (K) Pharmacological inhibition of MLC phosphorylation by Y27632 (2 µM) did not affect the Yoda1‐induced Piezo1 translocation to the cell periphery ( n = 3). (L) Y27632 reduced Yoda1‐induced m/lEV release as visualized by confocal microscope ( n = 200 cells from three independent experiments). (M) Y27632 attenuated Yoda1‐induced m/lEV release and MLC phosphorylation as detected by Western blot ( n = 3). (N) KN‐62 (CaMKII inhibitor, 1 µM), but not PD150606 (Calpain inhibitor, 10 µM), blocked Yoda1‐induced Piezo1 translocation to the cell periphery ( n = 3). (O) KN‐62 reduced Yoda1‐induced m/lEV release as imaged by confocal microscope ( n = 200 cells from three independent experiments). (P) KN‐62 attenuated Yoda1‐induced m/lEV release and MLC phosphorylation as detected by Western blot ( n = 3). (Q) Schematic diagram showing that Piezo1 activation‐induced Piezo1 translocation to the cell periphery and m/lEV release are mediated by Ca 2+ ‐CaMKII signalling. In imaging experiments and subsequent quantitative analysis, HUVECs were subjected to either 15 dyn/cm 2 LSS for 300 s or Yoda1 for 10 min. For Western blot analysis, HUVECs were treated with Yoda1 for 24 h to ensure adequate EV collection. The quantified results of the Western blot were shown in Figure . All inhibitors were added 5 min prior to Yoda1 stimulation. Data are presented as mean ± SEM. ** p < 0.01.

Journal: Journal of Extracellular Vesicles

Article Title: Shear Stress‐Stimulated Trafficking of Endothelial Piezo1 to Splenic Capsule Boosts Spleen Contraction and Exercise Endurance

doi: 10.1002/jev2.70375

Figure Lengend Snippet: LSS triggers m/lEV release via Ca 2+ ‐CaMKII‐MLC signalling. (A) LSS (15 dyn/cm 2 for 300 s) induced Piezo1 translocation to the cell periphery colocalising with the microvesicle formation site ( n = 3). PKH26, a lipophilic membrane dye for labelling the membrane structures of EVs and cells. (B) Piezo1 reduction by siRNA suppressed LSS‐induced Piezo1 translocation to the cell periphery ( n = 3). (C) Inhibition of Ca 2+ signal through Thapsigargin (TG, 1 µM) and BAPTA (10 µM) blocked Yoda1 (Piezo1 agonist, 2 µM)‐induced Piezo1 translocation to the cell periphery ( n = 3). (D) TG and BAPTA inhibited Yoda1‐induced m/lEV release as imaged by confocal microscope ( n = 200 cells from three independent experiments). (E) TG and BAPTA suppressed Yoda1‐induced m/lEV release as detected by Western blot ( n = 3). (F) TG and BAPTA inhibited Yoda1‐induced MLC phosphorylation in HUVECs ( n = 3). (G) MLC reduction did not affect the Yoda1‐induced Piezo1 translocation to the cell periphery ( n = 3). (H) MLC reduction reduced Yoda1‐induced m/lEV release as visualized by confocal microscope ( n = 200 cells from three independent experiments). (I) MLC reduction attenuated Yoda1‐induced m/lEV release as detected by Western blot ( n = 3). (J) MLC reduction decreased Yoda1‐induced MLC phosphorylation ( n = 3). (K) Pharmacological inhibition of MLC phosphorylation by Y27632 (2 µM) did not affect the Yoda1‐induced Piezo1 translocation to the cell periphery ( n = 3). (L) Y27632 reduced Yoda1‐induced m/lEV release as visualized by confocal microscope ( n = 200 cells from three independent experiments). (M) Y27632 attenuated Yoda1‐induced m/lEV release and MLC phosphorylation as detected by Western blot ( n = 3). (N) KN‐62 (CaMKII inhibitor, 1 µM), but not PD150606 (Calpain inhibitor, 10 µM), blocked Yoda1‐induced Piezo1 translocation to the cell periphery ( n = 3). (O) KN‐62 reduced Yoda1‐induced m/lEV release as imaged by confocal microscope ( n = 200 cells from three independent experiments). (P) KN‐62 attenuated Yoda1‐induced m/lEV release and MLC phosphorylation as detected by Western blot ( n = 3). (Q) Schematic diagram showing that Piezo1 activation‐induced Piezo1 translocation to the cell periphery and m/lEV release are mediated by Ca 2+ ‐CaMKII signalling. In imaging experiments and subsequent quantitative analysis, HUVECs were subjected to either 15 dyn/cm 2 LSS for 300 s or Yoda1 for 10 min. For Western blot analysis, HUVECs were treated with Yoda1 for 24 h to ensure adequate EV collection. The quantified results of the Western blot were shown in Figure . All inhibitors were added 5 min prior to Yoda1 stimulation. Data are presented as mean ± SEM. ** p < 0.01.

Article Snippet: Pantethine (150 mg/kg, HY‐B1028, MCE, USA) or Y27632 (5 mg/kg, HY‐10071, MCE, USA) was dissolved in saline and injected intraperitoneally at 30 min before each exercise.

Techniques: Translocation Assay, Membrane, Inhibition, Confocal, Microscopy, Western Blot, Phospho-proteomics, Activation Assay, Imaging, Analysis

$Inhibition of m/lEV release inhibits the effects of shear stress on promoting endothelial function. (A) Treatment with Yoda1 (Piezo1 agonist, 2 µM) for 24 h increased m/lEV release, whereas both pantethine and Y27632 attenuated this effect ( n = 5). (B, C) Inhibition of m/lEV release by pantethine (50 µM) and Y27632 (2 µM) abolished Yoda1‐induced benefits in HUVECs, as determined by cell migration (B) and cell viability (C) ( n = 5). HUVECs were pre‐treated with pantethine or Y27632 for 5 min followed by Yoda1 treatment for 24 h. (D) Pantethine (150 mg/kg, i.p.) and Y27632 (5 mg/kg, i.p.) were used to test whether inhibiting m/lEV release causes vascular endothelial dysfunction in vivo. Pantethine or Y27632 was injected to mice at 30 min prior to each exercise. The mice were subjected to treadmill exercise at 18 m/min, 60 min/d, 5 days a week, for 1 month. All indices were tested after 1 month of exercise. (E) Schematic diagram of plasma m/lEV isolation and purification. (F) The presence of the EV markers Annexin A1, CD9, MMP2 and TSG101 were determined in SEC fractions 7–9 (500 µL/fraction) using Western blotting. Fractions 7–9 were identified as the m/lEV‐rich fractions ( n = 4). (G) Both pantethine and Y27632 blocked the upregulation of circulating m/lEVs induced by exercise, as determined by NTA ( n = 8). (H) The exercise‐induced increase in exhaustion distance on the treadmill was abolished by pantethine and Y27632 ( n = 8). (I) Pantethine or Y27632 suppressed exercise‐promoted endurance of forelimb grip strength ( n = 6). (J) Pantethine and Y27632 reduced the effect of exercise on decreasing aortic intima‐media thickness ( n = 8). (K) Treatment with pantethine or Y27632 blocked the effect of exercise on reducing blood pressure ( n = 8). (L) Pantethine and Y27632 suppressed the effect of exercise on improving endothelium‐dependent vasodilation in isolated arteries ( n = 6). Data are presented as mean ± SEM. * p < 0.05, ** p < 0.01.$

Journal: Journal of Extracellular Vesicles

Article Title: Shear Stress‐Stimulated Trafficking of Endothelial Piezo1 to Splenic Capsule Boosts Spleen Contraction and Exercise Endurance

doi: 10.1002/jev2.70375

Figure Lengend Snippet: Inhibition of m/lEV release inhibits the effects of shear stress on promoting endothelial function. (A) Treatment with Yoda1 (Piezo1 agonist, 2 µM) for 24 h increased m/lEV release, whereas both pantethine and Y27632 attenuated this effect ( n = 5). (B, C) Inhibition of m/lEV release by pantethine (50 µM) and Y27632 (2 µM) abolished Yoda1‐induced benefits in HUVECs, as determined by cell migration (B) and cell viability (C) ( n = 5). HUVECs were pre‐treated with pantethine or Y27632 for 5 min followed by Yoda1 treatment for 24 h. (D) Pantethine (150 mg/kg, i.p.) and Y27632 (5 mg/kg, i.p.) were used to test whether inhibiting m/lEV release causes vascular endothelial dysfunction in vivo. Pantethine or Y27632 was injected to mice at 30 min prior to each exercise. The mice were subjected to treadmill exercise at 18 m/min, 60 min/d, 5 days a week, for 1 month. All indices were tested after 1 month of exercise. (E) Schematic diagram of plasma m/lEV isolation and purification. (F) The presence of the EV markers Annexin A1, CD9, MMP2 and TSG101 were determined in SEC fractions 7–9 (500 µL/fraction) using Western blotting. Fractions 7–9 were identified as the m/lEV‐rich fractions ( n = 4). (G) Both pantethine and Y27632 blocked the upregulation of circulating m/lEVs induced by exercise, as determined by NTA ( n = 8). (H) The exercise‐induced increase in exhaustion distance on the treadmill was abolished by pantethine and Y27632 ( n = 8). (I) Pantethine or Y27632 suppressed exercise‐promoted endurance of forelimb grip strength ( n = 6). (J) Pantethine and Y27632 reduced the effect of exercise on decreasing aortic intima‐media thickness ( n = 8). (K) Treatment with pantethine or Y27632 blocked the effect of exercise on reducing blood pressure ( n = 8). (L) Pantethine and Y27632 suppressed the effect of exercise on improving endothelium‐dependent vasodilation in isolated arteries ( n = 6). Data are presented as mean ± SEM. * p < 0.05, ** p < 0.01.

Article Snippet: Pantethine (150 mg/kg, HY‐B1028, MCE, USA) or Y27632 (5 mg/kg, HY‐10071, MCE, USA) was dissolved in saline and injected intraperitoneally at 30 min before each exercise.

Techniques: Inhibition, Shear, Migration, In Vivo, Injection, Clinical Proteomics, Isolation, Purification, Western Blot

LSS‐induced m/lEV release maintains endothelial Piezo1 homeostasis. (A) Immunoelectron microscope visualized that Piezo1 was packaged into the m/lEVs ( n = 15 cells from three independent experiments). (B) Left panel: Confocal microscope visualized that LSS (15 dyn/cm 2 for 300 s) increased the content of Piezo1 in m/lEVs ( n = 60 cells from six independent experiments). Right panel: LSS increased the percentage of Piezo1‐positive m/lEVs ( n = 6). (C) Both LSS and Yoda1increased the content of Piezo1 in m/lEVs ( n = 4). (D) Dual stimulation with Yoda1 (Piezo1 agonist, 2 µM) and m/lEV release inhibitor (500 nM pantethine or 2 µM Y27632) induced Piezo1 over accumulation in HUVECs ( n = 4). HUVECs were pre‐treated with pantethine or Y27632 for 5 min followed by Yoda1 treatment for 24 h. (E) Dual stimulation with Yoda1 and m/lEV release inhibitor induced Ca 2+ overload in HUVECs ( n = 5). (F) Piezo1 overexpression (OE) reduced the phosphorylation of eNOS and VEGFR2 ( n = 3). Plasmid transfection for Piezo1 OE was performed 60 h prior to the cell functional analysis. (G) Piezo1 OE impaired EC migration ( n = 5). (H) Piezo1 OE impaired EC tube formation ( n = 5). (I) Piezo1 OE impaired ACh‐induced NO production ( n = 5). (J) Piezo1 OE induced Ca 2+ overload in ECs ( n = 5). (K) Treatment with either pantethine (150 mg/kg, i.p.) or Y27632 (5 mg/kg, i.p.) abolished the effect of exercise on upregulating Piezo1 in circulating m/lEVs from mice ( n = 6). The experimental schemes for m/lEV release inhibitor treatment and the exercise model were showed in Figure . (L) Chronic exercise mildly upregulated Piezo1 expression, whereas treatment with either pantethine or Y27632 induced Piezo1 over accumulation in aorta from mice with exercise ( n = 6). (M) Schematic diagram showing that LSS‐induced m/lEV release contributes to intracellular Piezo1 homeostasis. Data are presented as mean ± SEM. * p < 0.05, ** p < 0.01.

Journal: Journal of Extracellular Vesicles

Article Title: Shear Stress‐Stimulated Trafficking of Endothelial Piezo1 to Splenic Capsule Boosts Spleen Contraction and Exercise Endurance

doi: 10.1002/jev2.70375

Figure Lengend Snippet: LSS‐induced m/lEV release maintains endothelial Piezo1 homeostasis. (A) Immunoelectron microscope visualized that Piezo1 was packaged into the m/lEVs ( n = 15 cells from three independent experiments). (B) Left panel: Confocal microscope visualized that LSS (15 dyn/cm 2 for 300 s) increased the content of Piezo1 in m/lEVs ( n = 60 cells from six independent experiments). Right panel: LSS increased the percentage of Piezo1‐positive m/lEVs ( n = 6). (C) Both LSS and Yoda1increased the content of Piezo1 in m/lEVs ( n = 4). (D) Dual stimulation with Yoda1 (Piezo1 agonist, 2 µM) and m/lEV release inhibitor (500 nM pantethine or 2 µM Y27632) induced Piezo1 over accumulation in HUVECs ( n = 4). HUVECs were pre‐treated with pantethine or Y27632 for 5 min followed by Yoda1 treatment for 24 h. (E) Dual stimulation with Yoda1 and m/lEV release inhibitor induced Ca 2+ overload in HUVECs ( n = 5). (F) Piezo1 overexpression (OE) reduced the phosphorylation of eNOS and VEGFR2 ( n = 3). Plasmid transfection for Piezo1 OE was performed 60 h prior to the cell functional analysis. (G) Piezo1 OE impaired EC migration ( n = 5). (H) Piezo1 OE impaired EC tube formation ( n = 5). (I) Piezo1 OE impaired ACh‐induced NO production ( n = 5). (J) Piezo1 OE induced Ca 2+ overload in ECs ( n = 5). (K) Treatment with either pantethine (150 mg/kg, i.p.) or Y27632 (5 mg/kg, i.p.) abolished the effect of exercise on upregulating Piezo1 in circulating m/lEVs from mice ( n = 6). The experimental schemes for m/lEV release inhibitor treatment and the exercise model were showed in Figure . (L) Chronic exercise mildly upregulated Piezo1 expression, whereas treatment with either pantethine or Y27632 induced Piezo1 over accumulation in aorta from mice with exercise ( n = 6). (M) Schematic diagram showing that LSS‐induced m/lEV release contributes to intracellular Piezo1 homeostasis. Data are presented as mean ± SEM. * p < 0.05, ** p < 0.01.

Article Snippet: Pantethine (150 mg/kg, HY‐B1028, MCE, USA) or Y27632 (5 mg/kg, HY‐10071, MCE, USA) was dissolved in saline and injected intraperitoneally at 30 min before each exercise.

Techniques: Microscopy, Confocal, Over Expression, Phospho-proteomics, Plasmid Preparation, Transfection, Functional Assay, Analysis, Migration, Expressing

Piezo1 transportation to the splenic capsule promotes spleen contraction and maintains exercise endurance. (A) Schematic diagram of the ultrasonographic measurements before and after acute exercise. (B) Inhibition of Piezo1 transportation through EC‐specific KO (Piezo1 EC −/− ) and Y27632 (5 mg/kg, i.p., 30 min prior to exercise) abolished the effect of exercise on upregulating splenic Piezo1 contents ( n = 6). (C) Piezo1 EC −/− , Y27632 and GsMTx4 (10 mg/kg, i.p., 30 min prior to exercise) suppressed exercise‐induced spleen contraction ( n = 10). Left panel: Representative ultrasound images of the spleen pre‐ and post‐exercise. Middle panel: Quantification of spleen area pre‐ and post‐exercise from ultrasound images. Right panel: Percentage change in spleen contraction in response to exercise. (D) Piezo1 EC −/− , Y27632 and GsMTx4 decreased circulating blood volume during exercise ( n = 6). (E) Piezo1 EC −/− , Y27632 and GsMTx4 showed no significant effect on motor coordination quantified from average latency to fall from rotarod ( n = 8). (F, G) Piezo1 EC −/− , Y27632 and GsMTx4 decreased exercise endurance in mice, as detected by cumulative numbers of falls binned every 5 min of mice during 1 h rotarod endurance test (F), and distance and time run to exhaustion during a treadmill endurance test (G) ( n = 8). (H) α1AR antagonist (Prazosin, 1 mg/kg, i.p., 30 min prior to exercise) abolished exercise‐induced spleen contraction ( n = 10). (I) Schematic illustration of splenic denervation via absolute ethanol ablation. (J) Representative images of sham‐operated (upper) and denervated (lower) spleens 5 weeks post‐surgery. Tyrosine hydroxylase (TH) was used to label neural fibers. (K) Splenic denervation abolished exercise‐induced spleen contraction ( n = 10). (L) Yoda1 (2 mg/kg, i.p.) induced spleen contraction even with ablation of the splenic nerve plexus ( n = 10). Ultrasonographic measurements were performed before and at 1 h after Yoda1 injection. Data are presented as mean or mean ± SEM. * p < 0.05, ** p < 0.01.

Journal: Journal of Extracellular Vesicles

Article Title: Shear Stress‐Stimulated Trafficking of Endothelial Piezo1 to Splenic Capsule Boosts Spleen Contraction and Exercise Endurance

doi: 10.1002/jev2.70375

Figure Lengend Snippet: Piezo1 transportation to the splenic capsule promotes spleen contraction and maintains exercise endurance. (A) Schematic diagram of the ultrasonographic measurements before and after acute exercise. (B) Inhibition of Piezo1 transportation through EC‐specific KO (Piezo1 EC −/− ) and Y27632 (5 mg/kg, i.p., 30 min prior to exercise) abolished the effect of exercise on upregulating splenic Piezo1 contents ( n = 6). (C) Piezo1 EC −/− , Y27632 and GsMTx4 (10 mg/kg, i.p., 30 min prior to exercise) suppressed exercise‐induced spleen contraction ( n = 10). Left panel: Representative ultrasound images of the spleen pre‐ and post‐exercise. Middle panel: Quantification of spleen area pre‐ and post‐exercise from ultrasound images. Right panel: Percentage change in spleen contraction in response to exercise. (D) Piezo1 EC −/− , Y27632 and GsMTx4 decreased circulating blood volume during exercise ( n = 6). (E) Piezo1 EC −/− , Y27632 and GsMTx4 showed no significant effect on motor coordination quantified from average latency to fall from rotarod ( n = 8). (F, G) Piezo1 EC −/− , Y27632 and GsMTx4 decreased exercise endurance in mice, as detected by cumulative numbers of falls binned every 5 min of mice during 1 h rotarod endurance test (F), and distance and time run to exhaustion during a treadmill endurance test (G) ( n = 8). (H) α1AR antagonist (Prazosin, 1 mg/kg, i.p., 30 min prior to exercise) abolished exercise‐induced spleen contraction ( n = 10). (I) Schematic illustration of splenic denervation via absolute ethanol ablation. (J) Representative images of sham‐operated (upper) and denervated (lower) spleens 5 weeks post‐surgery. Tyrosine hydroxylase (TH) was used to label neural fibers. (K) Splenic denervation abolished exercise‐induced spleen contraction ( n = 10). (L) Yoda1 (2 mg/kg, i.p.) induced spleen contraction even with ablation of the splenic nerve plexus ( n = 10). Ultrasonographic measurements were performed before and at 1 h after Yoda1 injection. Data are presented as mean or mean ± SEM. * p < 0.05, ** p < 0.01.

Article Snippet: Pantethine (150 mg/kg, HY‐B1028, MCE, USA) or Y27632 (5 mg/kg, HY‐10071, MCE, USA) was dissolved in saline and injected intraperitoneally at 30 min before each exercise.

Techniques: Inhibition, Injection

Neutrophils develop a lipid‐laden state through free fatty acid uptake. (A–C) Neutrophils uptake free fatty acids (FAs). Human neutrophils were exposed to free fatty acids (PA, palmitic acid, 50 µM; OA, oleic acid, 50 µM; LA, linoleic acid, 50 µM). Lipid droplets (LDs) were visualized by BODIPY staining and immunofluorescence microscopy. SSO, sulfo‐ N ‐succinimidyl esters (CD36 inhibitor, 100 µM); Lipo, lipofermata (FATP2 inhibitor, 5 µM). (A) Schematic illustration of free FAs uptake by neutrophils. Representative immunofluorescence images (B) and quantification of LDs (C) in neutrophils exposed to free FAs. (D–F) Neutrophils acquire lipids from adipocytes. Mouse neutrophils were co‐cultured with differentiated 3T3‐L1 (d3T3‐L1) in the presence of TNF‐α, and LDs within the neutrophils were examined using immunofluorescence microscopy. (D) Schematic illustration of adipocyte‐to‐neutrophil lipid transfer. (E) Representative immunofluorescence images of neutrophils co‐cultured with adipocytes. Adipocytes are delineated by dashed lines, and neutrophils surrounding the adipocytes are indicated by arrowheads. (F) Quantification of LDs in neutrophils co‐cultured with adipocytes. Neutrophils co‐cultured with adipocytes were harvested, and intracellular LDs were measured using BODIPY staining. (G and H) Metabolic pathways in lipid‐laden neutrophils. (G) qPCR analysis of lipid metabolism‐related genes in vehicle‐ and OA‐treated neutrophils. (H) Heatmap showing the relative mRNA expression levels in OA‐treated neutrophils compared with the vehicle‐treated neutrophils. (I) Intracellular concentrations of FAs and TGs in OA‐treated neutrophils. (J–M) Lipidomics analysis in neutrophils exposed to OA. (J) Principal component analysis of glycerolipids in neutrophils. (K) Differential metabolite analysis in OA‐treated neutrophils. Scatter plot showing the log2 fold change of metabolites between OA‐ and vehicle‐treated neutrophils, with upregulated DG and TG species marked. (L and M) Heatmap showing the relative expression levels of selected DG and TG species enriched in OA‐treated neutrophils. Each heatmap annotates lipid species and their fatty acid composition. ABHD5, Abhydrolase domain containing 5; ACAA2, Acetyl‐CoA acyltransferase; ACACA, Acetyl‐CoA carboxylase alpha; ACAT, Acetyl‐CoA: cholesterol acyltransferase; ACLY, ATP citrate lyase; AGPAT, 1‐acylglycerol‐3‐phosphate O‐acyltransferase; ACSL, Acyl‐CoA synthetase long‐chain family member; CD36, Cluster of differentiation 36; CPT, Carnitine palmitoyltransferase; DGAT, (Diacylglycerol O‐acyltransferase); FABP, Fatty acid‐binding protein; FASN, Fatty acid synthase; G0S2, G0/G1 switch gene 2; HADHA, Hydroxyacyl‐CoA dehydrogenase / 3‐ketoacyl‐CoA thiolase / enoyl‐CoA hydratase alpha subunit; HILPDA, Hypoxia‐inducible lipid droplet‐associated protein; LIPE, Lipase E; MGAT, Mannosyl‐glycoprotein beta‐1,2‐N‐acetylglucosaminyltransferase; MGLL, Monoglyceride lipase; PLIN, Perilipin; PNPLA, Patatin‐like phospholipase domain containing; SLC27A4, Solute carrier family 27 member 4. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Journal: Journal of Extracellular Vesicles

Article Title: Neutrophils Promote Metabolic Dysfunction‐Associated Steatotic Liver Disease Through Extracellular Vesicle‐mediated Lipid Transfer

doi: 10.1002/jev2.70350

Figure Lengend Snippet: Neutrophils develop a lipid‐laden state through free fatty acid uptake. (A–C) Neutrophils uptake free fatty acids (FAs). Human neutrophils were exposed to free fatty acids (PA, palmitic acid, 50 µM; OA, oleic acid, 50 µM; LA, linoleic acid, 50 µM). Lipid droplets (LDs) were visualized by BODIPY staining and immunofluorescence microscopy. SSO, sulfo‐ N ‐succinimidyl esters (CD36 inhibitor, 100 µM); Lipo, lipofermata (FATP2 inhibitor, 5 µM). (A) Schematic illustration of free FAs uptake by neutrophils. Representative immunofluorescence images (B) and quantification of LDs (C) in neutrophils exposed to free FAs. (D–F) Neutrophils acquire lipids from adipocytes. Mouse neutrophils were co‐cultured with differentiated 3T3‐L1 (d3T3‐L1) in the presence of TNF‐α, and LDs within the neutrophils were examined using immunofluorescence microscopy. (D) Schematic illustration of adipocyte‐to‐neutrophil lipid transfer. (E) Representative immunofluorescence images of neutrophils co‐cultured with adipocytes. Adipocytes are delineated by dashed lines, and neutrophils surrounding the adipocytes are indicated by arrowheads. (F) Quantification of LDs in neutrophils co‐cultured with adipocytes. Neutrophils co‐cultured with adipocytes were harvested, and intracellular LDs were measured using BODIPY staining. (G and H) Metabolic pathways in lipid‐laden neutrophils. (G) qPCR analysis of lipid metabolism‐related genes in vehicle‐ and OA‐treated neutrophils. (H) Heatmap showing the relative mRNA expression levels in OA‐treated neutrophils compared with the vehicle‐treated neutrophils. (I) Intracellular concentrations of FAs and TGs in OA‐treated neutrophils. (J–M) Lipidomics analysis in neutrophils exposed to OA. (J) Principal component analysis of glycerolipids in neutrophils. (K) Differential metabolite analysis in OA‐treated neutrophils. Scatter plot showing the log2 fold change of metabolites between OA‐ and vehicle‐treated neutrophils, with upregulated DG and TG species marked. (L and M) Heatmap showing the relative expression levels of selected DG and TG species enriched in OA‐treated neutrophils. Each heatmap annotates lipid species and their fatty acid composition. ABHD5, Abhydrolase domain containing 5; ACAA2, Acetyl‐CoA acyltransferase; ACACA, Acetyl‐CoA carboxylase alpha; ACAT, Acetyl‐CoA: cholesterol acyltransferase; ACLY, ATP citrate lyase; AGPAT, 1‐acylglycerol‐3‐phosphate O‐acyltransferase; ACSL, Acyl‐CoA synthetase long‐chain family member; CD36, Cluster of differentiation 36; CPT, Carnitine palmitoyltransferase; DGAT, (Diacylglycerol O‐acyltransferase); FABP, Fatty acid‐binding protein; FASN, Fatty acid synthase; G0S2, G0/G1 switch gene 2; HADHA, Hydroxyacyl‐CoA dehydrogenase / 3‐ketoacyl‐CoA thiolase / enoyl‐CoA hydratase alpha subunit; HILPDA, Hypoxia‐inducible lipid droplet‐associated protein; LIPE, Lipase E; MGAT, Mannosyl‐glycoprotein beta‐1,2‐N‐acetylglucosaminyltransferase; MGLL, Monoglyceride lipase; PLIN, Perilipin; PNPLA, Patatin‐like phospholipase domain containing; SLC27A4, Solute carrier family 27 member 4. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Article Snippet: To examine the functional contribution of EV biogenesis and uptake to neutrophil‐mediated lipid transfer HepG2 cells (1 × 10 6 cells) were co‐cultured with lipid‐laden neutrophils (1 × 10 7 cells) for 2 h in the presence of ROCK inhibitor Y‐27632 (50 μM, MedChemExpress, #HY‐10071) to suppress EV formation, or cytochalasin D (50 μg/mL) to inhibit EV uptake.

Techniques: Staining, Immunofluorescence, Microscopy, Cell Culture, Expressing, Binding Assay

Lipid‐laden neutrophils transfer lipids to the hepatocytes. (A–C) Lipid transfer from lipid‐laden neutrophils (LNs) to hepatocytes. Mouse neutrophils were co‐cultured with either undifferentiated 3T3‐L1 or differentiated 3T3‐L1 (d3T3‐L1) and subsequently co‐cultured with AML12 cells for 2 h. Neutrophils were removed and intracellular fat levels in AML12 cells were quantified using BODIPY staining. NNs, normal neutrophils; LNs, lipid‐laden neutrophils; AML12+OA, AML12 cells treated with oleic acid (OA, 50 µM); AML12+LA, AML12 cells treated with linoleic acid (LA, 50 µM); AML12+d3T3L1, AML12 cells co‐cultured with d3T3‐L1 cells at the ratio of 1:1; AML12+NNs, AML12 cells co‐cultured with NNs; AML12+LNs, AML12 cells co‐cultured with LNs. (A) Schematic representation of the experiment. (B) Left, representative immunofluorescence images. Right, quantification of BODIPY fluorescence in AML12 cells. (C) qPCR analysis of the metabolic genes in AML12 cells. (D–F) Lipid transfer from neutrophils exposed to free FAs to hepatocytes. Human neutrophils exposed to OA were subsequently co‐cultured with human HepG2 cells for 2 h. Neutrophils were removed and intracellular fat levels were quantified using BODIPY staining. HepG2+Veh; HepG2 cells treated with vehicle, HepG2+OA; HepG2 cells treated with OA (50 µM), HepG2+NNs, HepG2 cells co‐cultured with NNs; HepG2+LNs, HepG2 cells co‐cultured with LNs. (D) Schematic representation of the experiment. (E) Quantification of BODIPY fluorescence in HepG2 cells (F) qPCR analysis of metabolic pathway genes in HepG2 cells. Dgat1, Diacylglycerol O‐Acyltransferase 1; LPIN, Lipin family member; Scd, Stearoyl‐CoA Desaturase. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Journal: Journal of Extracellular Vesicles

Article Title: Neutrophils Promote Metabolic Dysfunction‐Associated Steatotic Liver Disease Through Extracellular Vesicle‐mediated Lipid Transfer

doi: 10.1002/jev2.70350

Figure Lengend Snippet: Lipid‐laden neutrophils transfer lipids to the hepatocytes. (A–C) Lipid transfer from lipid‐laden neutrophils (LNs) to hepatocytes. Mouse neutrophils were co‐cultured with either undifferentiated 3T3‐L1 or differentiated 3T3‐L1 (d3T3‐L1) and subsequently co‐cultured with AML12 cells for 2 h. Neutrophils were removed and intracellular fat levels in AML12 cells were quantified using BODIPY staining. NNs, normal neutrophils; LNs, lipid‐laden neutrophils; AML12+OA, AML12 cells treated with oleic acid (OA, 50 µM); AML12+LA, AML12 cells treated with linoleic acid (LA, 50 µM); AML12+d3T3L1, AML12 cells co‐cultured with d3T3‐L1 cells at the ratio of 1:1; AML12+NNs, AML12 cells co‐cultured with NNs; AML12+LNs, AML12 cells co‐cultured with LNs. (A) Schematic representation of the experiment. (B) Left, representative immunofluorescence images. Right, quantification of BODIPY fluorescence in AML12 cells. (C) qPCR analysis of the metabolic genes in AML12 cells. (D–F) Lipid transfer from neutrophils exposed to free FAs to hepatocytes. Human neutrophils exposed to OA were subsequently co‐cultured with human HepG2 cells for 2 h. Neutrophils were removed and intracellular fat levels were quantified using BODIPY staining. HepG2+Veh; HepG2 cells treated with vehicle, HepG2+OA; HepG2 cells treated with OA (50 µM), HepG2+NNs, HepG2 cells co‐cultured with NNs; HepG2+LNs, HepG2 cells co‐cultured with LNs. (D) Schematic representation of the experiment. (E) Quantification of BODIPY fluorescence in HepG2 cells (F) qPCR analysis of metabolic pathway genes in HepG2 cells. Dgat1, Diacylglycerol O‐Acyltransferase 1; LPIN, Lipin family member; Scd, Stearoyl‐CoA Desaturase. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Techniques: Cell Culture, Staining, Immunofluorescence, Fluorescence

Lipid‐laden neutrophils transfer lipids to hepatocytes via extracellular vesicles. (A, B) LNs transfer lipids to HepG2 cells in the absence of direct cell to cell contact. (A) HepG2 cells were co‐cultured with either NNs or LNs in a transwell chamber, and intracellular BODIPY fluorescence was quantified. (B) Conditioned media from LNs mediate lipid transfer to HepG2 cells. HepG2 cells were treated with supernatants derived from either NNs or LNs, and intracellular BODIPY fluorescence was quantified. (C) Extracellular vesicles (EVs) mediate lipid transfer from LNs to hepatocytes. HepG2 cells were treated with EVs isolated from either NNs (NNEVs) or LNs (LNEVs), and intracellular BODIPY fluorescence was quantified. Veh, HepG2 cells treated with vehicle; +NNEVs, HepG2 cells treated with NNEVs; +LNEVs, HepG2 cells treated with LNEVs. (D) LNEVs exhibit increased lipid content. Left, representative immunofluorescence images. Right, quantification of BODIPY fluorescence in neutrophil‐derived EVs. (E) Quantification of lipid contents in neutrophil‐derived EVs. (F) In vivo distribution of fluorescence‐labeled neutrophil‐derived EVs. Mice were intravenously injected with fluorescence‐tagged neutrophil‐derived EVs, and bioluminescence was assessed 24 h after administration using IVIS spectrum in vivo imaging system. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Journal: Journal of Extracellular Vesicles

Article Title: Neutrophils Promote Metabolic Dysfunction‐Associated Steatotic Liver Disease Through Extracellular Vesicle‐mediated Lipid Transfer

doi: 10.1002/jev2.70350

Figure Lengend Snippet: Lipid‐laden neutrophils transfer lipids to hepatocytes via extracellular vesicles. (A, B) LNs transfer lipids to HepG2 cells in the absence of direct cell to cell contact. (A) HepG2 cells were co‐cultured with either NNs or LNs in a transwell chamber, and intracellular BODIPY fluorescence was quantified. (B) Conditioned media from LNs mediate lipid transfer to HepG2 cells. HepG2 cells were treated with supernatants derived from either NNs or LNs, and intracellular BODIPY fluorescence was quantified. (C) Extracellular vesicles (EVs) mediate lipid transfer from LNs to hepatocytes. HepG2 cells were treated with EVs isolated from either NNs (NNEVs) or LNs (LNEVs), and intracellular BODIPY fluorescence was quantified. Veh, HepG2 cells treated with vehicle; +NNEVs, HepG2 cells treated with NNEVs; +LNEVs, HepG2 cells treated with LNEVs. (D) LNEVs exhibit increased lipid content. Left, representative immunofluorescence images. Right, quantification of BODIPY fluorescence in neutrophil‐derived EVs. (E) Quantification of lipid contents in neutrophil‐derived EVs. (F) In vivo distribution of fluorescence‐labeled neutrophil‐derived EVs. Mice were intravenously injected with fluorescence‐tagged neutrophil‐derived EVs, and bioluminescence was assessed 24 h after administration using IVIS spectrum in vivo imaging system. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Techniques: Cell Culture, Fluorescence, Derivative Assay, Isolation, Immunofluorescence, In Vivo, Labeling, Injection, In Vivo Imaging

Transcriptomic profiling of HepG2 cells exposed to extracellular vesicles derived from lipid‐laden neutrophils. HepG2 cells were treated with extracellular vesicles (EVs) derived from NNs (+NNEVs) or LNs (+LNEVs) for 2 h and subsequently subjected to bulk RNA sequencing. (A) Schematic representation of the experimental procedure. (B) Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis highlighting enrichment of human disease‐associated pathways in EV‐treated HepG2 cells. (C) KEGG pathway analysis of metabolic processes altered by neutrophil‐derived EVs. (D) Gene Ontology (GO) Biological Process enrichment analysis of differentially expressed genes. (E) Metabolic pathways modulated by LNEVs in HepG2 cells. Upper panel, a heatmap depicting differentially expressed genes (DEGs) in +LNEVs relative to vehicle‐treated HepG2 cells. Lower panel, a schematic summary illustrating alterations in lipid metabolic genes in +LNEVs based on KEGG metabolic pathway mapping.

Journal: Journal of Extracellular Vesicles

Article Title: Neutrophils Promote Metabolic Dysfunction‐Associated Steatotic Liver Disease Through Extracellular Vesicle‐mediated Lipid Transfer

doi: 10.1002/jev2.70350

Figure Lengend Snippet: Transcriptomic profiling of HepG2 cells exposed to extracellular vesicles derived from lipid‐laden neutrophils. HepG2 cells were treated with extracellular vesicles (EVs) derived from NNs (+NNEVs) or LNs (+LNEVs) for 2 h and subsequently subjected to bulk RNA sequencing. (A) Schematic representation of the experimental procedure. (B) Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis highlighting enrichment of human disease‐associated pathways in EV‐treated HepG2 cells. (C) KEGG pathway analysis of metabolic processes altered by neutrophil‐derived EVs. (D) Gene Ontology (GO) Biological Process enrichment analysis of differentially expressed genes. (E) Metabolic pathways modulated by LNEVs in HepG2 cells. Upper panel, a heatmap depicting differentially expressed genes (DEGs) in +LNEVs relative to vehicle‐treated HepG2 cells. Lower panel, a schematic summary illustrating alterations in lipid metabolic genes in +LNEVs based on KEGG metabolic pathway mapping.

Techniques: Derivative Assay, RNA Sequencing

Lipid‐laden neutrophils contribute to hepatic fat accumulation in vivo. (A–E) Effect of neutrophil depletion on hepatic fat accumulation in a murine model of diet‐induced obesity. (A) Schematic representation of the experimental design. C57BL/6J mice were fed either a high‐fat diet (HFD) or normal chow (NC). Neutrophils were depleted via intraperitoneal administration of an anti‐Ly6G antibody. (B) Representative immunofluorescence images showing BODIPY staining of peripheral neutrophils isolated from mice. ( C ) Immunofluorescence analysis of liver sections, showing the presence of BODIPY + Ly6G + lipid‐laden neutrophils in livers of HFD‐fed mice. (D and E) Visualization of hepatic lipid accumulation using Oil Red O staining (D) and BODIPY immunofluorescence staining (E). (F–J) Effects of adoptive transfer of LNs on hepatic fat accumulation. (F) Schematic illustration of the experimental design. C57BL/6J mice were intravenously injected with either LNs or NNs at two‐day intervals for 10 days. (G and H) Representative images and quantification of hepatic lipid accumulation assessed by Oil Red O staining. (I and J) Representative images and quantification of hepatic lipid accumulation assessed by BODIPY fluorescence. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Journal: Journal of Extracellular Vesicles

Article Title: Neutrophils Promote Metabolic Dysfunction‐Associated Steatotic Liver Disease Through Extracellular Vesicle‐mediated Lipid Transfer

doi: 10.1002/jev2.70350

Figure Lengend Snippet: Lipid‐laden neutrophils contribute to hepatic fat accumulation in vivo. (A–E) Effect of neutrophil depletion on hepatic fat accumulation in a murine model of diet‐induced obesity. (A) Schematic representation of the experimental design. C57BL/6J mice were fed either a high‐fat diet (HFD) or normal chow (NC). Neutrophils were depleted via intraperitoneal administration of an anti‐Ly6G antibody. (B) Representative immunofluorescence images showing BODIPY staining of peripheral neutrophils isolated from mice. ( C ) Immunofluorescence analysis of liver sections, showing the presence of BODIPY + Ly6G + lipid‐laden neutrophils in livers of HFD‐fed mice. (D and E) Visualization of hepatic lipid accumulation using Oil Red O staining (D) and BODIPY immunofluorescence staining (E). (F–J) Effects of adoptive transfer of LNs on hepatic fat accumulation. (F) Schematic illustration of the experimental design. C57BL/6J mice were intravenously injected with either LNs or NNs at two‐day intervals for 10 days. (G and H) Representative images and quantification of hepatic lipid accumulation assessed by Oil Red O staining. (I and J) Representative images and quantification of hepatic lipid accumulation assessed by BODIPY fluorescence. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Techniques: In Vivo, Immunofluorescence, Staining, Isolation, Adoptive Transfer Assay, Injection, Fluorescence

Neutrophils from patients with MASLD exhibit a lipid‐laden phenotype. (A) Schematic overview of the experimental workflow for the isolation and analysis of neutrophils and EVs from patients with MASLD and healthy volunteers. (B–E) Phenotypic and metabolic characterization of neutrophils isolated from patients with MASLD. Neutrophils were isolated from healthy volunteers and patients with MASLD and subjected to BODIPY staining, intracellular TG quantification, and qPCR analysis of the lipid metabolic genes. (B) Representative immunofluorescence images of neutrophils isolated from healthy volunteers and patients with MASLD stained with BODIPY to visualize LDs, with LDs indicated by arrows. (C) Quantification of LD counts per neutrophils from healthy volunteers and patients with MASLD. (D) Intracellular TG levels in neutrophils isolated from healthy volunteers and patients with MASLD. (E) qPCR analysis of lipid metabolism‐related genes in neutrophils, comparing expression levels between patients with MASLD and healthy volunteers. (F and G) Characterization of circulating EVs isolated from patients with MASLD. EVs were isolated from serum of healthy volunteers (HV EVs) and patients with MASLD (MASLD EVs) and analyzed for miRNAs expression and TG content. (F) qPCR analysis of selected miRNAs in HV EVs and MASLD EVs. (G) Quantification of TG concentrations in HV EVs and MASLD EVs. (H) qPCR analysis of selected miRNAs in neutrophils isolated from HV (HV Neu) and MASLD patients (MASLD Neu). (I) Spearman correlation analysis between miRNA levels in circulating EVs and neutrophils from patients with MASLD. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Journal: Journal of Extracellular Vesicles

Article Title: Neutrophils Promote Metabolic Dysfunction‐Associated Steatotic Liver Disease Through Extracellular Vesicle‐mediated Lipid Transfer

doi: 10.1002/jev2.70350

Figure Lengend Snippet: Neutrophils from patients with MASLD exhibit a lipid‐laden phenotype. (A) Schematic overview of the experimental workflow for the isolation and analysis of neutrophils and EVs from patients with MASLD and healthy volunteers. (B–E) Phenotypic and metabolic characterization of neutrophils isolated from patients with MASLD. Neutrophils were isolated from healthy volunteers and patients with MASLD and subjected to BODIPY staining, intracellular TG quantification, and qPCR analysis of the lipid metabolic genes. (B) Representative immunofluorescence images of neutrophils isolated from healthy volunteers and patients with MASLD stained with BODIPY to visualize LDs, with LDs indicated by arrows. (C) Quantification of LD counts per neutrophils from healthy volunteers and patients with MASLD. (D) Intracellular TG levels in neutrophils isolated from healthy volunteers and patients with MASLD. (E) qPCR analysis of lipid metabolism‐related genes in neutrophils, comparing expression levels between patients with MASLD and healthy volunteers. (F and G) Characterization of circulating EVs isolated from patients with MASLD. EVs were isolated from serum of healthy volunteers (HV EVs) and patients with MASLD (MASLD EVs) and analyzed for miRNAs expression and TG content. (F) qPCR analysis of selected miRNAs in HV EVs and MASLD EVs. (G) Quantification of TG concentrations in HV EVs and MASLD EVs. (H) qPCR analysis of selected miRNAs in neutrophils isolated from HV (HV Neu) and MASLD patients (MASLD Neu). (I) Spearman correlation analysis between miRNA levels in circulating EVs and neutrophils from patients with MASLD. All results are expressed as mean ± SEM. * p < .05; ** p < .01; *** p < .001.

Techniques: Isolation, Staining, Immunofluorescence, Expressing

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