Activation of AMPK in Human Placental Explants Impairs Mitochondrial Function and Cellular Metabolism.

ABSTRACT:

Objective

Adenosine monophosphate-activated protein kinase (AMPK) is a cellular energy sensor whose phosphorylation increases energy production. We sought to evaluate the placenta-specific effect of AMPK activation on the handling of nutrients required for fetal development.

Methods

Explants were isolated from term placenta of 29 women (pregravid body mass index: 29.1 ± 9.9 kg/m²) and incubated for 24 hours with 0 to 100 µmol/L resveratrol or 0 to 1 mmol/L of 5-aminoimidazole-4-carboxyamide ribonucleoside (AICAR). Following treatment, uptake and metabolism of radiolabeled fatty acids and glucose were measured. Phosphorylation of AMPK was measured by Western blotting. Adenosine diphosphate (ATP) production was assessed using the mitochondrial ToxGlo assay kit. P <

SUBMITTER: Landau D 

PROVIDER: S-EPMC6421623 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature