Antimicrobial Peptide Epinecidin-1 Modulates MyD88 Protein Levels via the Proteasome Degradation Pathway
AbstractThe cationic antimicrobial peptide epinecidin-1 was identified from Epinephelus coioides and possesses multiple biological functions, including antibacterial, antifungal, anti-tumor, and immunomodulatory effects. In addition, epinecidin-1 suppresses lipopolysaccharide (LPS)-induced inflammation by neutralizing LPS and ameliorating LPS/Toll-like receptor (TLR)-4 internalization. However, it is unclear whether the actions of epinecidin-1 depend on the regulation of TLR adaptor protein MyD88 or endogenous TLR signaling antagonists, which include A20, interleukin-1 receptor associated kinase (IRAK)-M, and suppressor of cytokine signaling (SOCS)-1. Our results demonstrate that epinecidin-1 alone does not affect A20, IRAK-M, or SOCS-1 protein levels. However, pre-incubation of epinecidin-1 significantly inhibits LPS-induced upregulation of A20, IRAK-M, and SOCS-1. In addition, epinecidin-1 significantly reduces the abundance of MyD88 protein. Both MG132 (a specific proteasome inhibitor) and Heclin (a specific Smurf E3 ligase inhibitor) are able to abolish epinecidin-1-mediated MyD88 degradation. Thus, our data suggest that epinecidin-1 directly inhibits MyD88 via induction of the Smurf E3 ligase proteasome pathway. View Full-Text
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Su, B.-C.; Chen, J.-Y. Antimicrobial Peptide Epinecidin-1 Modulates MyD88 Protein Levels via the Proteasome Degradation Pathway. Mar. Drugs 2017, 15, 362.
Su B-C, Chen J-Y. Antimicrobial Peptide Epinecidin-1 Modulates MyD88 Protein Levels via the Proteasome Degradation Pathway. Marine Drugs. 2017; 15(11):362.Chicago/Turabian Style
Su, Bor-Chyuan; Chen, Jyh-Yih. 2017. "Antimicrobial Peptide Epinecidin-1 Modulates MyD88 Protein Levels via the Proteasome Degradation Pathway." Mar. Drugs 15, no. 11: 362.
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