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The role of interleukin-1β and extracellular signal-regulated kinase 1/2 in glucose-stimulated insulin secretion.

The role of interleukin-1β and extracellular signal-regulated kinase 1/2 in glucose-stimulated insulin secretion.
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Niu B, Su H, Xia XS, He Q, Xue YM, Yan XM,


Niu B, Su H, Xia XS, He Q, Xue YM, Yan XM, (click to view)

Niu B, Su H, Xia XS, He Q, Xue YM, Yan XM,

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The Kaohsiung journal of medical sciences 2017 04 0733(5) 224-228 pii S1607-551X(17)30152-3
Abstract

Glucose-stimulated insulin secretion (GSIS) is one of the important physiological characteristics of islet β cells, and extracellular-regulated protein kinase 1/2 (ERK1/2) is an important member of the mitogen-activated protein kinase family that regulates this process. The inflammatory cytokine interleukin (IL)-1β can inhibit the insulin secretion of pancreatic β cells, but the exact mechanism is unclear. This study was designed to investigate the inhibitory effect of IL-1β on GSIS in βTC-6 cells and its relation with the ERK1/2 signal transduction pathway. β-TC6 cells were cultured and stimulated with 0mM, 1.38mM, or 5.5mM glucose. In addition, GSIS in β-TC6 cells was blocked by IL-1β at concentrations of 0.15 ng/mL, 1.5 ng/mL, and 15 ng/mL. After glucose stimulation and IL-1β intervention, the insulin level in the cell supernatant was detected by radioimmunoassay, and the phosphorylation level of ERK1/2 was detected by western blotting assay. The insulin level in the 1.38mM glucose group was 108.52 ± 5.94 uIU/mL, which was significantly higher than the 0mM and 5.5mM glucose groups (p < 0.05). Compared with the 0mM glucose group, the level of ERK1/2 phosphorylation was increased in the 1.38mM and 5.5mM glucose groups. After intervention by 0.15 ng/mL, 1.5 ng/mL, and 15 ng/mL IL-1β, the level of ERK1/2 phosphorylation induced by 1.38mM glucose stimulation decreased in a dose-dependent manner, and the insulin level correspondingly decreased. IL-1β can inhibit GSIS in βTC-6 cells, which is related to its inhibition of the phosphorylation of ERK1/2.

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