Ask about this productRelated genes to: PKM2 antibody
- Gene:
- PKM NIH gene
- Name:
- pyruvate kinase M1/2
- Previous symbol:
- PKM2
- Synonyms:
- THBP1, OIP3, PK3
- Chromosome:
- 15q23
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2017-09-15
Related products to: PKM2 antibody
Related articles to: PKM2 antibody
- 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 - Oil foams are emerging as a promising, versatile system in food, cosmetic and pharmaceutical applications. Existing solutions depend on the addition of particles or surfactant crystallization; however, these approaches often require complex processing steps, introduce solid residues that may affect texture, and rely on kinetically trapped interfacial structures that limit reversibility under ambient conditions. Here, we examine the foamability and stability of food-grade, soybean lecithin in oil of different surface tension. We found that edible oil foams can be formed at room temperature only in long-chain triglyceride oils. By combining microscopy, X-ray techniques, and interfacial rheology, we show that the stabilization arises from the formation of inverse lipid bilayers at the air-oil surface, leading to increased surface elastic modulus and dense thin-films that protect the gas bubbles. We also discovered that different self-assembled structures are formed in different oils. These findings uncover a molecular mechanism for non-aqueous foam stabilization under ambient conditions and establish design principles for surfactant-stabilized oil foams, without particle additives or crystallization. - Source: PubMed
Publication date: 2026/04/15
Argyri Smaragda-MariaSaint-Jalmes ArnaudUgarte-Pereyra CarolinaBordes RomainVincent-Bonnieu SébastienLe Coeur ClémenceBinks Bernard PSchneck EmanuelFameau Anne-Laure - The alternative splice isoform of pyruvate kinase M (PKM), PKM2, plays a pivotal role in regulating aerobic glycolysis in tumor cells. Systemic delivery of antisense oligonucleotides (ASOs) that shift PKM splicing from the PKM2 isoform to the PKM1 isoform inhibits tumor progression and reprograms intratumoral metabolism. However, the cellular populations within the tumor microenvironment (TME) are also highly dependent on PKM2 and might likewise be affected by ASO treatment. In this study, we demonstrate that PKM2 is upregulated and PKM1 is downregulated in both human and murine pancreatic ductal adenocarcinoma (PDAC) cells. PKM1 and PKM2 are mutually exclusive and expressed in a cell type-specific manner in various cell types and stages of PDAC tumors. We report that basal-like PDAC cells and their surrounding activated regulatory T cells (T) rely on PKM2 to sustain glycolysis. Although PKM-ASO monotherapy had a limited effect in an immunodeficient mouse model of PDAC, synergy between PKM-ASO and anti-CTLA-4 immune checkpoint blockade (ICB), which targets T, restricted tumor growth in an immunocompetent mouse model. Our findings provide preclinical support for combined antisense therapy and ICB for PDAC patients, highlighting the critical role of PKM2 in the TME and its potential as a therapeutic target. - Source: PubMed
Publication date: 2026/04/21
Han LijieGan LinaSchäfer BalázsVoss Dillon MDanielsen MathiasKostov OndrejLiu JiaWang TingCaruthers Marvin HChen HaoKrainer Adrian R - The aim of this study is to explore how porcine epidemic diarrhea virus (PEDV) infection induces reprogramming of glucose metabolism in host cells and its impact on viral replication. We designed a control group and an infection group [infection of porcine intestinal epithelial cells (IPEC-J2) with PEDV]. First, we determined the infection time and dose of the virus by observing the PEDV titer and the expression of the N protein. Then, through proteomic comparative analysis, we studied the enriched differentially expressed proteins, key proteins, and key metabolic pathways in PEDV-infected cells. RT-qPCR and Western blotting were employed to verify the protein or gene expression of key enzymes in the glycolysis and tricarboxylic acid (TCA) cycle pathways in PEDV-infected cells. Finally, we clarified the impact of PEDV-induced glycolytic changes on viral replication by measuring the content of glucose, ATP, and lactic acid, as well as the expression of glucose transporters (SGLT-1 and GLUT-2) and PEDV N protein in cells. The results indicated that the optimal infection time of PEDV in IPEC-J2 was 48 h and the optimal multiplicity of infection was 1. Proteomics results showed that 342 differentially expressed proteins were screened out and mainly enriched in pathways such as glycolysis, digestion and absorption of carbohydrates, and lipid metabolism. PEDV infection upregulated the protein levels of key glycolysis enzymes HKII (<0.05), LDHA, and PKM (<0.01) in IPEC-J2 and the gene transcription level of (<0.01), while downregulating the gene transcription levels of key enzymes CS, OGDH, and IDH in the TCA cycle pathway (<0.01). In addition, PEDV infection increased intracellular lactate content (<0.01), decreased the ATP content (<0.01), upregulated the expression levels of SGLT-1 and GLUT-2 (<0.05, <0.01). Pre-treatment of IPEC-J2 with the glycolysis inhibitor 2-deoxy- d-glucose (2-DG) reduced the intracellular expression of PEDV N protein (<0.05). In conclusion, PEDV infection can induce reprogramming of glucose metabolism in host cells and enhance the replication of the virus. This is manifested as the activation of the glycolysis pathway and the obstruction of the TCA cycle and oxidative phosphorylation. PEDV promotes glucose uptake and up-regulate the expression of key enzymes in the glycolysis pathway to induce reprogramming of glucose metabolism, thus promote its efficient replication in host cells. This study confirms that PEDV infection can induce reprogramming of host cell glucose metabolism and promote viral replication by activating aerobic glycolysis, providing new insights and approaches for the targeted treatment and prevention of PEDV infection. - Source: PubMed
Chen XueqingWang GongminMa ChangWu GangXu JiajingChen XiwenZhang Yuanshu - PKM serves as a rate-limiting enzyme in glycolysis, which produces two isoforms depending on the inclusion of either exon 9 (PKM1) or exon 10 (PKM2). The M2 pyruvate kinase (PKM2) isoform is commonly upregulated in various cancers, where it plays a pivotal role in regulating Warburg effect. Breast cancer stem cells (BCSCs) exhibit enhanced glycolysis, which is crucial for their self-renewal. However, the specific role of PKM2 in BCSCs remains largely unexplored. Here, we report that PKM2 expression is upregulated in BCSCs. Meanwhile, we identify that LINC00887 is significantly upregulated in BRCA through a genome-wide LNCRNA microarray. Moreover, we recognize that hnRNPA1 interacts with PKM pre-mRNA and regulates its mutually exclusive splicing. Furthermore, we demonstrate that LINC00887 maintains the self-renewal of BCSCs by promoting PKM2 splicing and reprogramming glucose metabolism. Mechanistically, LINC00887 upregulates PKM2 expression by binding hnRNPA1, thereby concealing its ubiquitination site, which blocks its ubiquitination and maintains its stability. Consistently, overexpression of hnRNPA1 almost completely rescues/reverses the inhibitory effects of LINC00887 KD in BRCA. Collectively, our study characterizes the LINC00887/hnRNPA1/PKM1/2 axis in BRCA and reveals the essential role of LINC00887 in BCSCs self-renewal/maintenance through promoting hnRNPA1-mediated PKM2 splicing, highlighting the therapeutic potential of targeting cancer metabolism. - Source: PubMed
Publication date: 2026/04/14
Lv XuemeiHan LiTong Wei-WeiSun XiaoyuXu SuyingYan YuanyuanZhou ShuqiZhang YangyangZhang DikangWang JiaqiLiu JiaZhao HaishanYao WeifanXiao RuixinWang QiXu JiananGong LangWei MinjieChen BoHe Miao