Disease relevance of Pfkm

• We show that these drugs cause a detachment of the glycolytic enzymes, phosphofructokinase (ATP: D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13), from cytoskeleton of B16 melanoma cells [1].

High impact information on Pfkm

• However, it remains unknown whether Cav-3 expression is required for the plasma membrane recruitment and caveolar targeting of PFK-M [2].
• Analysis of skeletal muscle tissue samples from Cav-3(-/-) mice directly demonstrates that Cav-3 expression regulates the phenotypic behavior of PFK-M [2].
• In addition, we show that the membrane recruitment and caveolar targeting of PFK-M appears to be strictly dependent on the concentration of extracellular glucose [2].
• The deduced amino acid sequence is highly homologous to PFK-M (muscle) and PFK-L (liver), 69 and 65% amino acid identity, respectively, especially at substrate binding and catalytic sites, while the allosteric binding sites are less conserved [3].
• The relative rate of PFK-A synthesis increased sharply (5-fold) at an initial period of differentiation (8 h) and reached maximum of 10-fold at 48 h, to make PFK-A the major isoform synthesized in myotubes [4].

Biological context of Pfkm

• Taken together, our results suggest that glucose-dependent plasma membrane recruitment of activated PFK-M by caveolin-3 could have important implications for understanding the mechanisms that regulate energy metabolism in skeletal muscle fibers [5].
• Four transcription initiation sites have been identified by full-length RNA ligase-mediated rapid amplification of cDNA ends (RLM-RACE) between -61 and -32 bp from the translation initiation codon.Reverse transcription-PCR analysis revealed that PFK-A, PFK-B and PFK-C genes were expressed, in all mouse tissues tested, at varying levels [6].
• The results suggested that the mouse phosphofructokinase-M gene was transcribed through alternative splicing by the multiple promoters [7].
• The level of phosphofructokinase-M gene expression in mouse cardiac and skeletal muscles decreased in the ketotic diabetic state [7].
• The elasticity coefficients for hexokinase and phosphofructokinase at Cu2+ equal to the IC50 were also -1 [8].

Anatomical context of Pfkm

• The hybridizable mRNA level for PFK-A increased gradually, reaching 13-fold at 48 h when 80% of cells was fused to myotubes [4].
• The PFK-A mRNA level at 96 h was 90-fold of that for myoblasts [4].
• These isoforms are expressed specifically in the testis and in the mid-gestation embryo, and have been termed TE-PFK-M (testis- and embryo-specific PFK-M) [9].

Associations of Pfkm with chemical compounds

• The activities of pyruvate kinase (PK), phosphofructokinase (PFK), lactic acid (LD) and the level of lactate dehydroenase (LDH) and ATP were detected, and the mRNA and protein levels of EPO in the cortices were analyzed [10].

Physical interactions of Pfkm

• The combination of modeling data obtained with purified and extract systems suggests that aldolase binds to an intermediate dimer of phosphofructokinase and within this heterocomplex the kinase is completely active [11].

Other interactions of Pfkm

• The mouse PFK-C gene organization is similar to that of the human and rabbit PFK-A and human and mouse PFK-B genes [6].
• The same values of flux control coefficients for hexokinase and for phosphofructokinase (0.8 and 0.2 respectively) were found in absence and in presence of copper [8].

Analytical, diagnostic and therapeutic context of Pfkm

• Molecular cloning of the 5' part of mouse phosphofructokinase-M cDNA was performed [7].
• Compared to the control group, the mouse in the group treated with the PO extracts by 1 g/d had significantly higher activities of PF, PFK, LDH and higher levels of ATP in the cortices, especially under the hypoxic environment for 24 hours [10].

References