Ask about this productRelated genes to: Pfkfb2 Blocking Peptide
- 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 Blocking Peptide
Related articles to: Pfkfb2 Blocking Peptide
- Adverse historical conditions shape biodiversity by driving demographic shifts and genomic divergence through evolutionary mechanisms. Selective pressures foster adaptive strategies in response to extreme environments, with hibernation as a key example. The expression of torpor and its various forms exemplify such adaptations. However, the genomic basis of these processes and the influence of evolutionary forces, particularly natural selection, remain largely unexplored. The Monito del Monte (), a small marsupial considered a living fossil, exhibits torpor, hibernation, and aestivation as key survival strategies. In this study, we investigated genomic adaptations in and their potential relationship with the physiological state of torpor and hibernation. Historical climate change, along with varying expansions and bottlenecks, appears to have shaped the genetic diversity and local adaptation of . At the ancestral node, positive selection was detected in , and , alongside enrichment in the MAPK signaling and steroid hormone biosynthesis pathways-both previously implicated in hibernation physiology. Gene family expansions further converged on mitochondrial maintenance and redox regulation. At the species level, and show no overlap in positively selected genes: presents additional signals in LSS and RASL11B, related to sterol and stress-response metabolism, while shows signatures of broad thermal stress tolerance through HSPA2. These findings underscore unique adaptations possibly linked to hibernation in and species-specific differences. - Source: PubMed
Publication date: 2026/08/02
Gonzalez-Ugalde ElisaAvendaño Paula MQuintero-Galvis Julián FPizarro Eduardo JCubillos Francisco ANespolo Roberto FLeón FabiolaVianna Juliana A - As a bifunctional enzyme, phosphofructokinase-2/fructose 2,6-bisphosphatase (PFKFB or PFK-2) produces and degrades fructose-2,6-bisphosphate (Fru-2,6-P). Because Fru-2,6-P is a strong allosteric activator of glycolysis, PFKFB is critical to glycolytic regulation. Four isoenzymes of PFKFB have been identified (PFKFB1-4). PFKFB2 is considered the cardiac isoenzyme and is distinct among the isoforms because of its complex regulation via multi-site phosphorylation. It plays critical roles in cardiac physiological responses to stress, with its loss a key driver of pathophysiology in metabolic cardiac diseases. However, PFKFB2 is also expressed in multiple additional tissues and is involved in noncardiac pathologies including cancer. Therefore, an ongoing area of research is the regulation of PFKFB2 activity and abundance. Here, we review the history and present knowledge of the structure, function, tissue distribution, and roles of PFKFB2 in physiology, stress response, and pathophysiology, both in the heart and other tissues systemically. - Source: PubMed
Publication date: 2026/06/25
Harold Kylene MYoon Wan HeeHumphries Kenneth M - Pre- and postpartum environments and genetic effects influence childhood internalising problems, which increase depression risk. DNA methylation (DNAm) may capture some of these effects. We therefore investigated associations between child blood DNAm and internalising problems. - Source: PubMed
Publication date: 2026/06/16
Schellhas LauraLuo MannanFelix Janine FPage Christian MBekkhus MonaMunafò Marcus RZuccolo LuisaHavdahl AlexandraCecil Charlotte A MSharp Gemma C - The role of circulating pyruvate in diabetic retinopathy (DR) progression is poorly defined. Unravelling its cell-specific genomic regulation is vital. - Source: PubMed
Publication date: 2026/06/10
Lin JiaqiongChen HonglingYang MengChen LihengLi Xiaoyong - 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