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1.
Allergol Immunopathol (Madr) ; 51(1): 159-167, 2023.
Article in English | MEDLINE | ID: mdl-36617836

ABSTRACT

INTRODUCTION: Inflammatory bowel disease (IBD), which mainly leads to diarrhea, fatigue, stool blood, abdominal pain, and cramping, is threatening public health. Tripartite motif-containing 52 (TRIM52) has been reported to play an important role in inflammatory responses via activating the toll-like receptor 4 (TLR4)/nuclear factor-κB (NF-κB) pathway. However, the causes of IBD need to be elucidated, and the function of TRIM52 in IBD remains unclear. Here, we demonstrated that TRIM52 aggravated inflammation and pyroptosis in dextran sulfate sodium (DSS)-induced IBD by activating TLR4/NF-κBs pathway. METHODS: The colitis model was established on mice through DSS induction. For the TRIM52 knockdown, the mice were infected with a recombinant adenoviral vector expressing sgRNAs targeting TRIM52. RT-qPCR, western blot, and immunohistochemistry were performed to verify TRIM52 expression in DSS-induced IBD. The body weight, disease activity index, colon length, and H&E staining were used to assess the IBD symptoms in mice with TRIM52 knockdown. The inflammatory responses were examined by RT-qPCR and ELISA measuring tumor necrosis factor-α (TNF-α), inter-leukin 6 (IL-6), and interleukin 1ß (IL-1ß). Furthermore, the pyroptosis in colon tissue was detected by western blot. Finally, the TLR4/NF-κBs pathway activity was also examined by western blot. RESULTS: TRIM52 expression was up-regulated in DSS-induced IBD, and knockdown of TRIM52 could alleviate the symptoms of IBD. TRIM52 knockdown retarded DSS-induced inflammatory response and inhibited DSS-induced pyroptosis in colon tissue. In addition, TRIM52 played a role in activating TLR4/NF-κBs pathway. CONCLUSION: Knockdown of TRIM52 alleviated inflammation and pyroptosis in IBD by regulating TLR4/NF-κBs pathway. TRIM52 is expected to be a novel diagnostic indicator for IBD and a target of therapeutic treatment.


Subject(s)
Colitis , Inflammatory Bowel Diseases , Pyroptosis , Tripartite Motif Proteins , Animals , Mice , Colitis/chemically induced , Colitis/metabolism , Colitis/pathology , Dextran Sulfate/adverse effects , Disease Models, Animal , Inflammation , Inflammatory Bowel Diseases/chemically induced , Inflammatory Bowel Diseases/metabolism , Inflammatory Bowel Diseases/pathology , Mice, Inbred C57BL , NF-kappa B/metabolism , Signal Transduction , Toll-Like Receptor 4/genetics , Toll-Like Receptor 4/metabolism , Tripartite Motif Proteins/metabolism
2.
Allergol. immunopatol ; 51(1): 159-167, ene. 2023. tab, graf
Article in English | IBECS | ID: ibc-214032

ABSTRACT

Introduction: Inflammatory bowel disease (IBD), which mainly leads to diarrhea, fatigue, stool blood, abdominal pain, and cramping, is threatening public health. Tripartite motif-containing 52 (TRIM52) has been reported to play an important role in inflammatory responses via activating the toll-like receptor 4 (TLR4)/nuclear factor-κB (NF-κB) pathway. However, the causes of IBD need to be elucidated, and the function of TRIM52 in IBD remains unclear. Here, we demonstrated that TRIM52 aggravated inflammation and pyroptosis in dextran sulfate sodium (DSS)-induced IBD by activating TLR4/NF-κBs pathway. Methods: The colitis model was established on mice through DSS induction. For the TRIM52 knockdown, the mice were infected with a recombinant adenoviral vector expressing sgRNAs targeting TRIM52. RT-qPCR, western blot, and immunohistochemistry were performed to verify TRIM52 expression in DSS-induced IBD. The body weight, disease activity index, colon length, and H&E staining were used to assess the IBD symptoms in mice with TRIM52 knockdown. The inflammatory responses were examined by RT-qPCR and ELISA measuring tumor necrosis factor-α (TNF-α), inter-leukin 6 (IL-6), and interleukin 1β (IL-1β). Furthermore, the pyroptosis in colon tissue was detected by western blot. Finally, the TLR4/NF-κBs pathway activity was also examined by western blot. Results: TRIM52 expression was up-regulated in DSS-induced IBD, and knockdown of TRIM52 could alleviate the symptoms of IBD. TRIM52 knockdown retarded DSS-induced inflammatory response and inhibited DSS-induced pyroptosis in colon tissue. In addition, TRIM52 played a role in activating TLR4/NF-κBs pathway. Conclusion: Knockdown of TRIM52 alleviated inflammation and pyroptosis in IBD by regulating TLR4/NF-κBs pathway. TRIM52 is expected to be a novel diagnostic indicator for IBD and a target of therapeutic treatment (AU)


Subject(s)
Animals , Mice , Tripartite Motif Proteins/metabolism , Inflammatory Bowel Diseases/metabolism , Toll-Like Receptor 4/metabolism , NF-kappa B/metabolism , Colitis/metabolism , Disease Models, Animal , Mice, Inbred C57BL , Signal Transduction , Mice, Transgenic , Dextran Sulfate
3.
J Agric Food Chem ; 66(3): 563-570, 2018 Jan 24.
Article in English | MEDLINE | ID: mdl-29280631

ABSTRACT

Ultrasonication is an emerging technology applied in food processing and biological experimental pretreatments. Cavitation phenomena induced during ultrasonic treatment can generate localized high temperature and pressure, which can result in glycation reaction between protein and reducing sugars. In this study, the mixture of bovine serum albumin (BSA) and d-ribose was treated under 600 W for different times. Interestingly, a large amount of carbonized black materials appeared after ultrasonication, while the UV absorbance and intrinsic fluorescence spectra reflecting conformational changes were not obvious. Only 12 sites (11 lysines and 1 arginine) of the BSA with ribose under ultrasonic treatment for 35 min were identified through liquid chromatography high-resolution mass spectrometry (LCHR-MS). K547, K548, R359/R360, and K587 were the most reactive glycated sites, with the average degree of substitution per peptide molecule (DSP) value ranging from 15 to 35%. The glycated modification was distributed not only in domain III, but also in domains I and II. The glycated modification could occur during ultrasonic treatment, thereby influencing the properties of biomacromolecule after extraction.


Subject(s)
Ribose/chemistry , Serum Albumin, Bovine/chemistry , Amino Acid Motifs , Animals , Chromatography, Liquid , Glycosylation , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Ultrasonics
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