Human phosphoglycerate mutase 2,PGAM2 ELISA Kit
- Known as:
- Human phosphoglycerate mutase 2,PGAM2 Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- 201-12-0757
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Sunredbio SunBT Sun red bio
- Gene target:
- Human phosphoglycerate mutase 2 PGAM2 ELISA Kit
Related genes to: Human phosphoglycerate mutase 2,PGAM2 ELISA Kit
- Gene:
- PGAM2 NIH gene
- Name:
- phosphoglycerate mutase 2
- Previous symbol:
- -
- Synonyms:
- PGAM-M
- Chromosome:
- 7p13
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2016-10-05
Related products to: Human phosphoglycerate mutase 2,PGAM2 ELISA Kit
Related articles to: Human phosphoglycerate mutase 2,PGAM2 ELISA Kit
- Most spinal muscular atrophy (SMA) patients develop severe scoliosis by late adolescence. Given that the paraspinal muscles-particularly the multifidus-are indispensable for maintaining spinal stability, their site-specific multi-omics characteristics in SMA remain insufficiently defined. Herein, integrated multi-omics sequencing was performed on bilateral multifidus samples from SMA patients and surgical controls. We identified 5219 differentially expressed genes, 1063 differentially expressed proteins and 370 differential metabolites between the control and SMA, showing significant enrichment in glucose and amino acid metabolism pathways, specifically key steps of glycolysis/gluconeogenesis. Key enzymes in the glycolytic process such as PFKM, ENO3 and PKM1 were markedly downregulated. Notably, a comparative analysis of the bilateral paraspinal muscles in SMA revealed asymmetrical metabolic signatures in carbohydrate and amino acid processing between the concave and convex sides. Key regulatory enzymes exhibited significant differential expression: PYGL, a central driver of starch and sucrose metabolism; creatine kinase, involved in arginine and proline metabolism; and PGAM2, a key mediator of glycine, serine, and threonine metabolism. These metabolic signatures indicate a complex metabolic reprogramming in the multifidus, where asymmetric disparities point to the influence of mechanical loading, while systemic dysregulation aligns with the effects of SMN depletion. - Source: PubMed
Wang ZhenZhao JunduoHuang Xu'anChen WeiyunShen Jianxiong - Improving feed efficiency in dairy cattle requires a better understanding of tissue-specific mechanisms that support energy and nutrient utilization. Skeletal muscle represents a major proportion of body mass in dairy cows and plays a major role in post-absorptive metabolism. Our previous liver proteomics study highlighted that high-efficiency (HE) cows exhibit enhanced hepatic fatty acid oxidation, supporting lower feed intake without compromising productivity. This study aimed to identify muscle-based metabolic adaptations associated with feed efficiency. Skeletal muscle samples from 8 HE (low residual feed intake, RFI) and 8 low-efficiency (LE; high-RFI) mid-lactation (119 ± 33 DIM) Holstein cows, ranked at the top and bottom 10% of RFI, were analyzed using tandem mass tag proteomics and RT-qPCR to identify differences in skeletal muscle related to feed efficiency. HE cows had significantly greater muscle glycogen content and exhibited a coordinated metabolic shift favoring lipid utilization. RT-qPCR showed increased expression of β-oxidation (PPARA, ACADS, ACADVL, ACOX1) and triglyceride mobilization (ATGL) in HE cows. In contrast, proteomics revealed lower abundance of glycolytic and glycogenolytic enzymes (e.g., ALDOA, PFKM, PGAM2, PYGM, AGL) in HE muscle, indicating reduced glucose and glycogen catabolism. Proteins involved in the SLC2A4 (GLUT4) translocation pathway (ACTG1, YWHAH, YWHAZ) were more abundant in HE cows, suggesting an increased capacity for insulin-stimulated GLUT4 translocation, which may contribute to greater glycogen storage. Proteomics also showed enhanced redox regulation in HE cows, with greater abundance of GSR, CAT, GPX1, and PRDX2, and lower abundance of mitochondrial complexes I (NDUFB8) and III (UQCRC2), major sites of reactive oxygen species formation. These results indicate that skeletal muscle in HE cows adopts a metabolic phenotype characterized by increased reliance on lipid-derived fuels, glucose sparing, and improved oxidative homeostasis. Together with previously reported hepatic adaptations, these muscle-specific responses likely contribute to whole-animal feed efficiency in lactating dairy cows. - Source: PubMed
Publication date: 2026/05/30
Daddam Jayasimha RSura MounicaSarmikasoglou EfstathiosAhmad GhayyoorNaughton SarahMills MorganWhite Heather MVandeHaar MichaelZhou Zheng - : Sepsis-induced systemic inflammation often leads to diaphragmatic dysfunction and muscle atrophy, contributing to impaired respiratory function. Phosphoglycerate mutase 2 (PGAM2), a key enzyme in glycolysis, plays a significant role in muscle energy metabolism but has not been previously linked to sepsis-induced diaphragmatic dysfunction. This study aims to investigate the role of PGAM2 in sepsis-induced diaphragmatic atrophy and its underlying mechanisms. : A murine sepsis model was established using cecal ligation and puncture (CLP) in C57BL/6 mice. Body and diaphragm weights, along with muscle fiber cross-sectional areas, were measured. PGAM2 expression was evaluated using immunofluorescence, Western blotting, and real-time quantitative polymerase chain reaction (RT-qPCR). In vitro, CC myotubes were treated with tumor necrosis factor alpha (TNF-α), and PGAM2 expression was manipulated via small interfering RNA (siRNA) knockdown and plasmid overexpression. Atrophy markers (MuRF1, MAFbx/atrogin-1) and JAK2/STAT3 pathway activation were assessed. : CLP induced significant diaphragmatic atrophy, as reflected by an approximately 38% reduction in diaphragm weight and an approximately 37% decrease in muscle fiber cross-sectional area compared with the sham group. In contrast, PGAM2 protein expression was increased by approximately 105% in septic diaphragms. PGAM2 expression was also significantly elevated in TNF-α-treated myotubes. PGAM2 knockdown resulted in reduced MuRF1 and MAFbx expression, attenuating myotube atrophy, while PGAM2 overexpression exacerbated atrophy. Moreover, PGAM2 knockdown suppressed activation of the JAK2/STAT3 signaling pathway. : These findings demonstrate that PGAM2 contributes to sepsis-induced diaphragmatic atrophy through the activation of the JAK2/STAT3 signaling pathway. PGAM2 may therefore serve as a potential therapeutic target for sepsis-associated diaphragmatic dysfunction. - Source: PubMed
Publication date: 2026/05/09
Chu YunYuan XinrunGao XiaopoLuo Jinlong - This study used proteomic analysis to evaluate how four cooking methods impact the quality of beef from Rikaze humped cattle. Conventional boiling, high-pressure boiling, roasting and frying produced varying numbers of differentially abundant proteins (DAPs) in and hind leg beef samples compared to the raw meat. Principal component analysis, hierarchical clustering and correlation analysis revealed 11 and 18 proteins significantly associated with meat tenderness and colour, respectively. Myosin heavy chain 7 (MYH7), myosin light chain 2 (MYL2) and myosin light chain 6B (MYL6B), involved in the sarcomere (GO:0030017) and cardiac muscle contraction (map04260) pathways were negatively correlated with tenderness, indicating that their decreased abundance contributes to improved tenderness after cooking. The cytoskeletal protein α-crystallin B chain (CRYAB) showed a positive correlation with shear force, suggesting a role in toughness. PGAM2, ALDOA and PKM, participating in ADP metabolism (GO:0046031) and glycolysis (map00010), influenced meat texture, while glycolytic enzymes ALDOA, CKM and PKM promoted changes in lightness (*). MYBPC2 and VDAC2 were negatively correlated with *. EEF1G, PGP, PPIA and PRDX2 were negatively correlated with redness (*), and DES was positively correlated with yellowness (*). Overall, wet-heat cooking altered mainly skeletal, heat-shock and cytoskeletal proteins and enhanced tenderness, while proteins related to energy metabolism and oxidative stress were closely linked to colour development. These key proteins could serve as potential biomarkers for predicting the eating quality of humped cattle beef and provide a basis for the development of high-value beef products. - Source: PubMed
Publication date: 2026/04/15
Zheng HaoZhao XiaolongLi JingWang PingLi SiminLi LiangLiu Zhendong - To characterize the transcriptional and physiological alterations induced by manganese stress in , juveniles (mean weight 5.0 ± 0.2 g) were subjected to either manganese exposure (5.50 ± 0.03 mg/L) or control (0 mg/L) for a 12 h period. Subsequently, gill tissues were excised for evaluation of antioxidant parameters and RNA-Seq analysis. A total of 753 DEGs were identified in the manganese exposure group compared to controls, comprising 287 up-regulated and 466 down-regulated genes. GO and KEGG enrichment analysis of DEGs showed that most of the DEGs were involved in immune and metabolic pathways, which disturbed the biological processes related to immunity and metabolism at the molecular level. The acute manganese stress initiated a multi-level antioxidant response to cope with oxidative stress in . This finding was further supported by the significant increase in MDA content and significant decrease in GSH content and GSH-Px activity under manganese exposure, while SOD and CAT activities were significantly increased. Simultaneously, the acute manganese stress triggered profound metabolic reprogramming to cope with energy pressure in , which showed that manganese exposure significantly down-regulated energy metabolism-related genes (, , , , , , , ); furthermore, the overall energy metabolism network was widely inhibited, while lipid metabolism-related genes (, ) were significantly up-regulated to compensatorily activate fatty acid transport and β-oxidation pathways. In addition, the acute manganese stress initiated a complex immune response pattern to cope with cell damage in , which showed that manganese exposure significantly enhanced the expression of inflammatory signaling genes (, , ); furthermore, certain inflammatory pathways were activated, while the expressions of immune regulatory genes (, ) were significantly decreased. In summary, these results indicated that manganese exposure could impair immune function, disrupt metabolism, and induce oxidative stress in . - Source: PubMed
Publication date: 2026/03/20
Shen XiaoluWang YongliRen MingchunHuang DongyuGu JiazeZhang LeiminLiang HualiangChen Xiaoru