Baicalein protects rat insulinoma INS-1 cells from palmitate-induced lipotoxicity by inducing HO-1

PLoS One. 2017 Apr 26;12(4):e0176432. doi: 10.1371/journal.pone.0176432. eCollection 2017.

Abstract

Objective: β-Cell dysfunction plays a central role in the pathogenesis of type 2 diabetes (T2D), and the identification of novel approaches to improve β-cell function is essential to treat this disease. Baicalein, a flavonoid originally isolated from the root of Scutellaria Baicalensis, has been shown to have beneficial effects on β-cell function. Here, the authors investigated the molecular mechanism responsible for the protective effects of baicalein against palmitate (PA)-induced impaired β-cell function, and placed focus on the role of heme oxygenase (HO)-1.

Methods: Rat pancreatic β-cell line INS-1 cells or mouse pancreatic islets were cultured with PA (500 μM) to induce lipotoxicity in the presence or absence of baicalein (50 μM), and the expressions of the ER stress markers, ATF-3, CHOP and GRP78 were detected by Western blotting and/or qPCR. The involvement of HO-1 was evaluated by HO-1 siRNA transfection and using the HO-1 inhibitor ZnPP.

Results: Baicalein reduced PA-induced ER stress and inflammation and enhanced insulin secretion, and these effects were associated with the induction of HO-1. Furthermore, these protective effects were attenuated by ZnPP and by HO-1 siRNA. Pretreatment of PD98059 (an ERK inhibitor) significantly inhibited the protective effects of baicalein and blocked HO-1 induction. On the other hand, CO production by RuCO (a CO donor) ameliorated PA-induced ER stress, suggesting that CO production followed by HO-1 induction may contribute to the protective effects of baicalein against PA-induced β-cell dysfunction.

Conclusion: Baicalein protects pancreatic β-cells from PA-induced ER stress and inflammation via an ERK-HO-1 dependent pathway. The authors suggest HO-1 induction in pancreatic β-cells appears to be a promising therapeutic strategy for T2D.

MeSH terms

  • Animals
  • Cell Survival / drug effects
  • Cells, Cultured
  • Cytokines / analysis
  • DNA Fragmentation / drug effects
  • Endoplasmic Reticulum Chaperone BiP
  • Endoplasmic Reticulum Stress / drug effects*
  • Extracellular Signal-Regulated MAP Kinases / antagonists & inhibitors
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • Flavanones / pharmacology*
  • Flavonoids / pharmacology
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Heme Oxygenase-1 / antagonists & inhibitors
  • Heme Oxygenase-1 / genetics
  • Heme Oxygenase-1 / metabolism*
  • Insulin-Secreting Cells / cytology
  • Insulin-Secreting Cells / drug effects
  • Insulin-Secreting Cells / metabolism
  • Insulinoma / metabolism
  • Insulinoma / pathology
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Palmitates / toxicity*
  • Protective Agents / pharmacology*
  • Protoporphyrins / pharmacology
  • RNA Interference
  • Rats

Substances

  • Cytokines
  • Endoplasmic Reticulum Chaperone BiP
  • Flavanones
  • Flavonoids
  • Heat-Shock Proteins
  • Hspa5 protein, mouse
  • Palmitates
  • Protective Agents
  • Protoporphyrins
  • zinc protoporphyrin
  • baicalein
  • Heme Oxygenase-1
  • Extracellular Signal-Regulated MAP Kinases
  • 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one

Grants and funding

This research was supported by a grant from the Korean Health Technology R&D Project through the Korean Health Industry Development Institute (KHIDI), funded by the Ministry of Health & Welfare, Republic of Korea (grant number: HI14C1135), and by Basic Science Research Program through the National Research Foundation of Korea (NRF), funded by the Ministry of Education (Grant no. 2015R1D1A1A01058235). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.