Journal: Cell Biology and Toxicology
Article Title: Neutrophil-derived heparin-binding protein increases endothelial permeability in acute lung injury by promoting TRIM21 and the ubiquitination of P65
doi: 10.1007/s10565-025-10005-x
Figure Lengend Snippet: HBP promotes the interaction between TRIM21 and P65, and regulates endothelial cell permeability and glycolysis through TRIM21-induced ubiquitination of P65. A The effect of recombinant HBP and sepsis-derived PMNs on the interaction between TRIM21 and P65. Data are represented as mean ± SD, n = 3, * P < 0.05, ** P < 0.01,*** P < 0.001. B, C Impact of HBP overexpression and TRIM21 knockdown on P65 phosphorylation and nuclear translocation. Data are represented as mean ± SD, n = 3, * P < 0.05, ** P < 0.01, *** P < 0.001. D, E The effects of HBP overexpression and knockdown TRIM21 on TEER values and FITC-dextran measurements. F, G Western blot detects the effects of HBP overexpression and knockdown TRIM21 on tight junction protein expression in ECs. Data are represented as mean ± SD, n = 3, * P < 0.05, *** P < 0.001. H-J ECAR, lactate production, and glycolysis in ECs with altered HBP and TRIM21 expression. Data are represented as mean ± SD, n = 3, ** P < 0.01, *** P < 0.001
Article Snippet: Cells were incubated with primary antibodies against HBP (MAB461Hu24,Cloud-clone,1:100) and TRIM21(12,108–1-AP, proteintech,1:100) at 4 °C overnight.
Techniques: Permeability, Ubiquitin Proteomics, Recombinant, Derivative Assay, Over Expression, Knockdown, Phospho-proteomics, Translocation Assay, Western Blot, Expressing