Article Publish Status: FREE
Abstract Title:

Regulation of immune response by-1-propenylcysteine through autophagy-mediated protein degradation.

Abstract Source:

Exp Ther Med. 2020 Feb ;19(2):1570-1573. Epub 2019 Dec 27. PMID: 32010341

Abstract Author(s):

Jun-Ichiro Suzuki, Satomi Miki, Mitsuyasu Ushijima, Yukihiro Kodera

Article Affiliation:

Jun-Ichiro Suzuki


Autophagy is a key event in cellular recycling processes due to its involvement in the intracellular degradation of proteins. It has been demonstrated that-1-propenylcysteine (S1PC), a characteristic sulfur compound in aged garlic extract, induces the activation of autophagy. S1PC degrades the adaptor protein myeloid differentiation response protein 88 (MyD88) of downstream of Toll-like receptor (TLR) by activating autophagyand. The degradation of MyD88 inhibits the TLR signaling pathway, including the phosphorylation of interleukin 1 receptor associated kinase 4 (IRAK4) and nuclear factor (NF)-κB p65, and eventually leads to the inhibition of interleukin (IL)-6 productionand C-C motif chemokine ligand 2 () mRNA expression. S1PC also increases the level of intestinal immunoglobulin A (IgA) and the number of IgA-producing cells in Peyer's patches. In addition, S1PC triggers the mRNA expression of X-box binding protein 1 (), an inducer of IgA-producing cell differentiation via the phosphorylation of extracellular signal-regulated kinase (ERK)1/2 and the degradation of paired box protein 5 (Pax5), a suppressor ofmRNA expression. The present review summarizes the mechanisms through which the activation of autophagy by S1PC modulates the immune response.

Study Type : Animal Study, In Vitro Study

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