Multi-Omics Integration to Reveal the Mechanism of Sericin Inhibiting LPS-Induced Inflammation.
Int J Mol Sci
; 24(1)2022 Dec 23.
Article
en En
| MEDLINE
| ID: mdl-36613700
ABSTRACT
Sericin is a natural protein with high application potential, but the research on its efficacy is very limited. In this study, the anti-inflammatory mechanism of sericin protein was investigated. Firstly, the protein composition of sericin extracts was determined by Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS). This was then combined with Enzyme-linked Immunosorbent Assay (ELISA) and Quantitative Real-time PCR (qRT-PCR), and it was confirmed that the anti-inflammation ability of sericin was positively correlated with the purity of sericin 1 protein. Finally, RNA-seq was performed to quantify the inhibitory capacity of sericin sample SS2 in LPS-stimulated macrophages. The gene functional annotation showed that SS2 suppressed almost all PRRs signaling pathways activated by lipopolysaccharides (LPS), such as the Toll-like receptors (TLRs) and NOD-like receptors (NLRs) signaling pathways. The expression level of adaptor gene MyD88 and receptor gene NOD1 was significantly down-regulated after SS2 treatment. SS2 also reduced the phosphorylation levels of NF-κB P65, P38, and JNK, thereby reducing the expressions of IL-1ß, IL-6, INOS, and other inflammatory cytokines. It was confirmed that sericin inhibited LPS-induced inflammation through MyD88/NF-κB pathway. This finding provides necessary theoretical support for sericin development and application.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Sericinas
/
Inflamación
/
Antiinflamatorios
Límite:
Humans
Idioma:
En
Revista:
Int J Mol Sci
Año:
2022
Tipo del documento:
Article
País de afiliación:
China