PFKFB2
- Known as:
- PFKFB2
- Catalog number:
- Y214374
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- PFKFB2
Related genes to: PFKFB2
- Gene:
- PFKFB2 NIH gene
- Name:
- 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 1q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 1991-05-09
- Date modifiied:
- 2016-10-05
Related products to: PFKFB2
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- The heart 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFKFB2) plays a critical role in glucose homeostasis and the pathophysiology of diabetes mellitus. However, the FBPase-2 domain remains less studied than its PFK-2 kinase counterpart. Therefore, in this study, PFKFB2 was overexpressed with molecular chaperones, and the kinetic properties of the FBPase-2 domain were studied. The purified PFKFB2 showed maximum activity at pH 7.5 in Tris-HCl buffer with Mg as the optimal cofactor. The FBPase-2 domain showed a classical Michaelis-Menten curve with a K of 0.73 μM and a V of 0.164 U/mg for F2,6BP. k and k/K were calculated to be 0.366 × 10 s and 6.99 × 10 M s, respectively. Circular Dichroism analyses of the purified enzyme showed 9.6% α-helix, 24.09% β-sheets, 28.9% turns, and 37.0% others as the secondary-structure composition of PFKFB2. The chaperone, GrpE, showed the lowest HADDOCK score (-267.2 ± 15.7) among all PFKFB2-chaperone docking complexes. Virtual screening identified citrate as a high-affinity modulator with a K of 14.9 μM. In silico mutagenesis indicated that single (Arg351Ala) and double (Arg351Ala and Tyr337Ala) mutations in Chain A of PFKFB2 (a homodimer protein) potentially destabilizes binding of citrate. In HepG2 and HEK293 cell lines, citrate decreased the activity of the FBPase-2 domain of PFKFB2, mRNA expression of PFKFB2, and glucose uptake and glucose production in a concentration-dependent manner. Thus, the characterisation of the FBPase-2 domain of PFKFB2 highlights its potential as a metabolic target for regulation of glucose homeostasis in diabetes mellitus. - Source: PubMed
Publication date: 2026/03/28
Nongkhlaw JoplinSingh Sumit KumarMarwein LydianaDas Kuheli BiswasDas Bidyadhar - Lactylation modification serves as a critical link between metabolic reprogramming and epigenetic regulation, playing a significant role in the progression of both malignant tumors and inflammatory diseases. Nevertheless, its specific function in the pathogenesis of ulcerative colitis (UC) remains poorly understood. - Source: PubMed
Publication date: 2026/03/11
Liu JianKang XiaoyunZhou YanxiangLi Jiao - In recent years, the prevalence of diabetic nephropathy (DN) has been increasing year by year. Here, this experiment investigated the effects of PFKFB2 in DN and its molecular mechanisms of DN. DN mice were fed a high-fat diet for 12 weeks, and then injected with STZ. DN mice were transfected with negative or sh-DPP9 lentivirus using Lipofectamine 3000 (Invitrogen, Carlsbad, CA, USA). Human proximal tubular HK-2 cells stimulated with 20 mmol/L d-glucose. Analysis revealed a significant downregulation of PFKFB2 expression in DN patients. PFKFB2 was expression in renal cell of DN model using single-cell RNA sequencing. Sh-PFKFB2 aggravated DN in mice model. PFKFB2 up-regulation reduced oxidative stress and glycolysis in model of DN. The inhibition of PFKFB2 aggravated mitochondria-dependent ferroptosis in model of DN. Ferroptosis inhibitor reduced the effects of PFKFB2 down-regulation in mitochondria-dependent ferroptosis in model of DN. PFKFB2 suppressed HIF-1α expression in model of DN by the inhibition of HIF-1α ubiquitination. HIF-1α inhibitor reduced the effects of PFKFB2 down-regulation in mitochondria-dependent ferroptosis in model of DN. In conclusion, PFKFB2 reduced oxidative stress and glycolysis of DN through the inhibition of HIF-1α signaling pathway by the induction of Nrf2 ubiquitination, further elucidating the role of PFKFB2 regulated mitochondrial ROS-induced ferroptosis for DN. Targeting PFKFB2 is thus a potentially effective therapeutic strategy for DN. - Source: PubMed
Tan YayinZhou JiajunLiu Yong - Glycolytic reprogramming has been implicated in rheumatoid arthritis (RA) pathogenesis, yet the underlying causal genes and epigenetic mechanisms remain unclear. This study aimed to systematically identify glycolysis-related genes and their methylation-regulated expression that may causally influence RA susceptibility. - Source: PubMed
Publication date: 2026/01/22
A XinyuXin PengfeiZheng LinXu BoWang JianyeSun SongtaoXie JunGao ChenxinPan PeijunQiu GuoweiJin LangShen JunXu XiruiCheng YiweiPei ShaoqiangRan LeiBian YanqinXiao Lianbo - The cardiac isoform of phosphofructokinase-2/fructose 2,6-bisphosphatase (PFKFB2) is the heart's strongest glycolytic regulator but is degraded in the absence of insulin signaling. This makes PFKFB2 loss critical to understand in metabolic heart disease, of which impaired insulin signaling is a hallmark. Prolongation of the QT interval, risk of arrhythmia, and sudden cardiac death are also augmented in metabolic heart disease, raising a question as to whether potential crosstalk between glycolytic dysregulation and electrophysiological dysfunction exists. - Source: PubMed
Publication date: 2026/01/22
Harold Kylene MBlankenship Harris EMinor KeatonMulligan AbigailLoveland BrookeLee Chi FungKinter MichaelKass DavidStavrakis StavrosBeckstead Michael JHumphries Kenneth M