Regulation and function of AMPK in physiology and diseases

Jeon, Sang‐Min

doi:10.1038/emm.2016.81

Cited by 880 publications

(806 citation statements)

References 148 publications

(158 reference statements)

Supporting

Mentioning

771

Contrasting

Unclassified

Order By: Relevance

“…LKB1, calmodulin‐dependent protein kinase kinase β (CaMKKβ), and transforming growth factor β‐activated kinase (TAK1) are upstream kinases that can activate AMPK by phosphorylating Thr172, which is situated in the activation loop of the α‐subunit (Jeon, 2016). In our study, we found that LPS stimulation inhibits LKB1 phosphorylation, but it does not affect CaMKKβ and TAK1 phosphorylation.…”

Section: Resultsmentioning

confidence: 99%

Antagonizing peroxisome proliferator‐activated receptor γ facilitates M1‐to‐M2 shift of microglia by enhancing autophagy via the LKB1–AMPK signaling pathway

et al. 2018

View full text Add to dashboard Cite

SummaryMicroglia‐mediated neuroinflammation plays a dual role in various brain diseases due to distinct microglial phenotypes, including deleterious M1 and neuroprotective M2. There is growing evidence that the peroxisome proliferator‐activated receptor γ (PPARγ) agonist rosiglitazone prevents lipopolysaccharide (LPS)‐induced microglial activation. Here, we observed that antagonizing PPARγ promoted LPS‐stimulated changes in polarization from the M1 to the M2 phenotype in primary microglia. PPARγ antagonist T0070907 increased the expression of M2 markers, including CD206, IL‐4, IGF‐1, TGF‐β1, TGF‐β2, TGF‐β3, G‐CSF, and GM‐CSF, and reduced the expression of M1 markers, such as CD86, Cox‐2, iNOS, IL‐1β, IL‐6, TNF‐α, IFN‐γ, and CCL2, thereby inhibiting NFκB–IKKβ activation. Moreover, antagonizing PPARγ promoted microglial autophagy, as indicated by the downregulation of P62 and the upregulation of Beclin1, Atg5, and LC3‐II/LC3‐I, thereby enhancing the formation of autophagosomes and their degradation by lysosomes in microglia. Furthermore, we found that an increase in LKB1–STRAD–MO25 complex formation enhances autophagy. The LKB1 inhibitor radicicol or knocking down LKB1 prevented autophagy improvement and the M1‐to‐M2 phenotype shift by T0070907. Simultaneously, we found that knocking down PPARγ in BV2 microglial cells also activated LKB1–AMPK signaling and inhibited NFκB–IKKβ activation, which are similar to the effects of antagonizing PPARγ. Taken together, our findings demonstrate that antagonizing PPARγ promotes the M1‐to‐M2 phenotypic shift in LPS‐induced microglia, which might be due to improved autophagy via the activation of the LKB1–AMPK signaling pathway.

show abstract

Section: Resultsmentioning

confidence: 99%

Antagonizing peroxisome proliferator‐activated receptor γ facilitates M1‐to‐M2 shift of microglia by enhancing autophagy via the LKB1–AMPK signaling pathway

et al. 2018

View full text Add to dashboard Cite

show abstract

“…In particular, it has been demonstrated that activation of AMPK is responsible for inducing apoptosis via the mitochondrial pathway (12,13). However, AMPK is also known to play a protective role in cancer cells under metabolic stressed conditions by maintenance of energy homeostasis and modulation of autophagy, making the influence of AMPK on cancer progression controversial (14,15).…”

Section: Resultsmentioning

confidence: 99%

Induction of apoptosis by ethanol extract of <i>Evodia rutaecarpa</i> in HeLa human cervical cancer cells <i>via</i> activation of AMP-activated protein kinase

Park

et al. 2016

BST

View full text Add to dashboard Cite

“…This compound, that mimics the intracellular increase in AMP, is capable of phosphorylating AMPK promoting glucose uptake and lipid oxidation in skeletal muscle 26 . Animal experiments also suggest that AMPK activation in skeletal muscle is capable of enhancing lipid oxidation and the glycogen resynthesis rate in response to exercise (having a protective effect on muscle glycogen stores) through the muscle contraction stimulus per se and through the increase of calcium release 27 . Continuous and repetitive muscle contraction that is characteristic of exercise acts as a stressor agent.…”

Section: Physical Exercise and Glucose Uptake Mediated By Ampkmentioning

confidence: 99%

Molecular mechanisms of glucose uptake in skeletal muscle at rest and in response to exercise

Pereira

Moura

Muñoz

et al. 2017

Motriz: rev. educ. fis.

View full text Add to dashboard Cite

-Glucose uptake is an important phenomenon for cell homeostasis and for organism health. Under resting conditions, skeletal muscle is dependent on insulin to promote glucose uptake. Insulin, after binding to its membrane receptor, triggers a cascade of intracellular reactions culminating in activation of the glucose transporter 4, GLUT4, among other outcomes. This transporter migrates to the plasma membrane and assists in glucose internalization. However, under special conditions such as physical exercise, alterations in the levels of intracellular molecules such as ATP and calcium act to regulate GLUT4 translocation and glucose uptake in skeletal muscle, regardless of insulin levels. Regular physical exercise, due to stimulating pathways related to glucose uptake, is an important non-pharmacological intervention for improving glycemic control in obese and diabetic patients. In this mini-review the main mechanisms involved in glucose uptake in skeletal muscle in response to muscle contraction will be investigated.

show abstract

Regulation and function of AMPK in physiology and diseases

Cited by 880 publications

References 148 publications

Antagonizing peroxisome proliferator‐activated receptor γ facilitates M1‐to‐M2 shift of microglia by enhancing autophagy via the LKB1–AMPK signaling pathway

Antagonizing peroxisome proliferator‐activated receptor γ facilitates M1‐to‐M2 shift of microglia by enhancing autophagy via the LKB1–AMPK signaling pathway

Induction of apoptosis by ethanol extract of <i>Evodia rutaecarpa</i> in HeLa human cervical cancer cells <i>via</i> activation of AMP-activated protein kinase

Molecular mechanisms of glucose uptake in skeletal muscle at rest and in response to exercise

Contact Info

Product

Resources

About