AI Article Synopsis
- Non-alcoholic fatty liver disease (NAFLD) prevalence has risen alongside obesity, and this study explores the role of heat shock protein 70 (HSP70) in lipid synthesis related to NAFLD.
- In experiments with mice on a high-fat diet and HepG2 cells treated with palmitic acid, HSP70 was found to be significantly expressed and increased lipid synthesis when overexpressed, while knockdown reduced lipid levels.
- The findings suggest that HSP70 plays a crucial role in promoting lipogenesis in liver cells, which could have implications for understanding NAFLD mechanisms.
Article Abstract
Background: The increasing prevalence of non-alcoholic fatty liver disease (NAFLD) has followed the international rise in obesity rates. Multiple mechanisms are involved in NAFLD, including endoplasmic reticulum stress and oxidative stress. Heat shock protein 70 (HSP70), which is abundant in most organisms, is sensitive to stress. However, the role of HSP70 in NAFLD has not been investigated. Here, we investigated the possible role of HSP70 in lipid synthesis.
Methods: C57BL/6 mice were fed a high-fat diet, and HepG2 cells were treated with 0.5 mM palmitic acid (PA). HSP70 expression was detected by qPCR, Western blot and immunohistochemistry. Total cholesterol (TC) and triglyceride (TG) levels were detected by enzyme-linked immunosorbent assay (ELISA). After Hsp70 overexpression and knockdown, TC and TG levels and FAS, SCD, and ACC expression were detected.
Results: HSP70 expression was significantly increased in the livers of obese mice. In vitro, HSP70 expression was markedly induced by PA in HepG2 cells. Notably, HSP70 overexpression in HepG2 cells enhanced TC and TG synthesis, in parallel with the upregulation of lipogenic genes, including FAS, SCD and ACC. By contrast, HSP70 knockdown decreased the levels of cellular lipids and the expression of FAS, SCD, and ACC in HepG2 cells. Together, our results suggest that HSP70 may promote lipogenesis in HepG2 cells.
Conclusions: Heat shock protein 70 promotes lipogenesis in HepG2 cells.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5891916 | PMC |
| http://dx.doi.org/10.1186/s12944-018-0722-8 | DOI Listing |
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