Eicosapentaenoic acid regulates glucose uptake in skeletal muscle and significantly affects whole-body energy metabolism. However, the underlying molecular mechanism remains unclear. Here we report that eicosapentaenoic acid activates phosphoglycerate mutase 2, which mediates the conversion of 2-phosphoglycerate into 3-phosphoglycerate. This enzyme plays a pivotal role in glycerol degradation, thereby facilitating the proliferation and differentiation of satellite cells in skeletal muscle. Interestingly, phosphoglycerate mutase 2 inhibits mitochondrial metabolism, promoting the formation of fast-type muscle fibers. Treatment with eicosapentaenoic acid and phosphoglycerate mutase 2 knockdown induced opposite transcriptomic changes, most of which were enriched in the PI3K-AKT signaling pathway. Phosphoglycerate mutase 2 activated the PI3K-AKT signaling pathway, which inhibited the phosphorylation of FOXO1, and, in turn, inhibited mitochondrial function and promoted the formation of fast-type muscle fibers. Our results suggest that eicosapentaenoic acid promotes skeletal muscle growth and regulates glucose metabolism by targeting phosphoglycerate mutase 2 and activating the PI3K/AKT signaling pathway.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.ijbiomac.2024.131547 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Enzymes in a human cytoplasm model organize into submetabolon complexes.
Proc Natl Acad Sci U S A
February 2025
Department of Chemistry, University of Illinois Urbana-Champaign, Urbana, IL 61801.
Enzyme-enzyme interactions are fundamental to the function of cells. Their atomistic mechanisms remain elusive mainly due to limitations of in-cell measurements. We address this challenge by atomistically modeling, for a total of ≈80 μs, a slice of the human cell cytoplasm that includes three successive enzymes along the glycolytic pathway: glyceraldehyde-3-phosphate dehydrogenase (GAPDH), phosphoglycerate kinase (PGK), and phosphoglycerate mutase (PGM).
View Article and Find Full Text PDFWe report the first implementation of ion mobility mass spectrometry combined with an ultra-high throughput sample introduction technology for high throughput screening (HTS). The system integrates differential ion mobility (DMS) with acoustic ejection mass spectrometry (AEMS), termed DAEMS, enabling the simultaneous quantitation of structural isomers that are the sub-strates and products of isomerase mediated reactions in intermediary metabolism. We demonstrate this potential by comparing DAEMS to a luminescence assay for the isoform of phosphoglycerate mutase (iPGM) distinctively present in pathogens offering an opportunity as a drug target for a variety of microbial and parasite borne diseases.
View Article and Find Full Text PDFA Cerium Oxide Loaded Hyaluronic Acid Nanosystem Remits Glucose Oxidative Stress-Induced Odontoblasts Mitochondrial Apoptosis through Regulation of PGAM5 Pathway.
ACS Appl Mater Interfaces
January 2025
School and Hospital of Stomatology, Wenzhou Medical University, Wenzhou 325027, China.
Diabetes mellitus (DM) induced mitochondrial oxidative stress (OS) can lead to severe injury of dental pulp. The cerium oxide nanoparticles (CNP) have been proven to have excellent antioxidative activity. However, whether CNP can relieve dental pulp damage caused by DM and the underlying mechanisms remain unclear.
View Article and Find Full Text PDFTargeting PGAM5 attenuates airway inflammation in asthma by inhibiting HMGB1 release in bronchial epithelium.
Free Radic Biol Med
January 2025
Chronic Airways Diseases Laboratory, Department of Respiratory and Critical Care Medicine, Nanfang Hospital, Southern Medical University, Guangzhou, 510515, China. Electronic address:
Article Synopsis
- Previous studies linked high HMGB1 levels to the development of steroid-insensitive asthma caused by toluene diisocyanate (TDI), highlighting mitochondrial dysfunction in bronchial epithelia.
- This study aims to determine if PGAM5, a mitochondrial protein, influences HMGB1 release in TDI-induced asthma by comparing its levels in asthma patients and healthy individuals and conducting various animal and in vitro experiments.
- Findings showed that inhibiting PGAM5 reduced airway inflammation and HMGB1 release in TDI-exposed mice, illustrating a potential regulatory mechanism involving mitochondrial apoptosis-related processes.
Oral exposure to ovalbumin alters glucose metabolism in sensitized mice: upregulation of HIF-1α-mediated glycolysis.
Food Funct
January 2025
State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, Jiangxi, PR China.
Food allergies are pathological adverse reactions against harmless dietary proteins. While studies have shown the involvement of host metabolic changes (, lipid metabolism and amino acid metabolism) in the development of food allergy (FA), the adaptive changes in glucose metabolism induced by food allergen exposure remain largely unclear. In this study, BALB/c mice were sensitized intraperitoneally with an ovalbumin (OVA)/aluminum adjuvant, followed by oral OVA challenges to induce anaphylaxis.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!