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KMID : 1034820190150040399
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Molecular & Cellular Toxicology
2019 Volume.15 No. 4 p.399 ~ p.406
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Curcumin inhibits poly(dA:dT)-induced IL-18 secretion by inhibiting the ASC oligomerization in human keratinocytes
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Lee Yu-Jin
Kang Jung-Hoon
Yun Mi-Hee
Lee Seong-Beom
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Abstract
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Backgrounds: Interleukin (IL)-18, a member of the IL-1 family, has been implicated in the development of a variety of inflammatory skin diseases. The binding of double-stranded (ds) DNA to absent in melanoma (AIM) 2 induces the oligomerization of apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) and the recruitment of pro-caspase-1, which leads to the activation of caspase-1, subsequently resulting in the secretion of IL-1β and IL-18. Curcumin is a naturally occurring polyphenolic compound in Curcuma longa and is also well known to have anti-oxidant and anti-inflammatory properties. In the current study, we focused on the inhibitory effect of curcumin on ASC oligo-merization in human keratinocytes.
Methods: The IL-18 level was measured by using an ELISA kit. The protein levels of AIM2 inflammasome components, such as AIM2, ASC, and pro-caspase-1, were determined by using a western blot. The level of ASC oligomerization was also determined by using a western blot.
Results: Our results show pre-treatment with curcumin attenuated poly (dA:dT)-induced secretion of IL-18 in IFN-γ-primed human keratinocytes. Pre-treatment with 10 μM curcumin was also found to inhibit ASC oligomerization in IFN-γ-primed cells.
Conclusion: These collective results show that curcumin inhibits the poly (dA:dT)-induced secretion of IL-18 via the suppression of ASC oligomerization in IFN-γ-primed human keratinocytes.
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KEYWORD
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Curcumin, AIM 2, Inflammasome, Keratinocytes, ASC
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