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Gene Review

Pfkp  -  phosphofructokinase, platelet

Mus musculus

Synonyms: 1200015H23Rik, 6-phosphofructokinase type C, 9330125N24Rik, ATP-PFK, ATP-dependent 6-phosphofructokinase, platelet type, ...
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Disease relevance of Pfkp

  • Specific activation by fructose 2,6-bisphosphate and inhibition by P-enolpyruvate of ascites tumor phosphofructokinase [1].

High impact information on Pfkp

  • The phosphofructokinase (PFK) C (Pfkp) and the pitrilysin metalloprotease 1 (Pitrm1) genes are compelling positional candidate genes in this region that show coding sequence differences between the parental strains in functional domains [2].
  • Fructose 2,6-bisphosphate, a potent activator of PFK, decreased the Km of PFK-C for fructose 6-phosphate from 200 to 60 microM while decreasing that of PFK-L from 300 to 55 microM [3].
  • PFK-C mRNA was detected in several brain regions and the anterior pituitary but not in liver, skeletal muscle, or several other tissues [3].
  • Expression plasmids containing PFK-C and PFK-L coding sequences were constructed and expressed by transient transfection into CMT cells [3].
  • To elucidate the structure, tissue-specific expression, and allosteric properties of phosphofructokinase-C (PFK-C), we cloned the cDNA for PFK-C from a rat hypothalamic cDNA library [3].

Biological context of Pfkp


Anatomical context of Pfkp

  • Based on the mouse PFK-C signal normalized to 18S rRNA, the PFK-C mRNA was expressed at the highest levels in the brain, heart, thymus and testicles, whereas low levels were observed in the kidney, liver, muscle, and lung [4].
  • In situ hybridization showed that PFK-C is expressed at a higher level in higher brain regions such as the cortex, compared with the midbrain and basal ganglia, while PFK-L is expressed at approximately equal levels throughout the brain [3].
  • K562 cells exhibit a relatively low phosphofructokinase and high pyruvate kinase activity [8].
  • Phosphofructokinase in K562 cells is mainly composed of the L- and F-types of which the F-type is characteristic for platelets and granulocytes and not for erythrocytes [8].
  • Metabolic evaluation of sexual dimorphism. V. Action of testosterone on the phosphofructokinase of mice submaxillary gland cells in vitro [7].

Associations of Pfkp with chemical compounds

  • Furthermore, equilibrium binding studies of modified phosphofructokinase B showed a greatly diminished capacity and affinity for cyclic AMP [9].
  • 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].
  • Many of the test analogues also showed inhibition of glyceraldehyde 3-phosphate dehydrogenase activity, the highest inhibitory potency being seen with acrylamide, but no compounds inhibited phosphofructokinase [11].
  • 4) The testosterone modifies the growth rate and the kinetic properties of the phosphofructokinase and these modifications depend on the sex [7].
  • 5. The specific activity of hexokinase (EC, phosphofructokinase (EC and pyruvate kinase (EC was not stimulated by 5-HT [12].

Other interactions of Pfkp

  • PFK-A mRNA was more abundantly expressed in all tissues than were the PFK-B and PFK-C genes [4].

Analytical, diagnostic and therapeutic context of Pfkp

  • Tissue-specific expression of PFK-C was investigated by Northern blot analysis [3].
  • Phosphofructokinase B, modified by radiolabeled FSBAdo, was digested by trypsin, and the digest separated by high-pressure liquid chromatography [9].
  • 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].


  1. Specific activation by fructose 2,6-bisphosphate and inhibition by P-enolpyruvate of ascites tumor phosphofructokinase. Boscá, L., Aragón, J.J., Sols, A. Biochem. Biophys. Res. Commun. (1982) [Pubmed]
  2. Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x SM/J murine model of obesity. Ehrich, T.H., Hrbek, T., Kenney-Hunt, J.P., Pletscher, L.S., Wang, B., Semenkovich, C.F., Cheverud, J.M. Diabetes (2005) [Pubmed]
  3. Structure, distribution, and functional expression of the phosphofructokinase C isozyme. Gekakis, N., Johnson, R.C., Jerkins, A., Mains, R.E., Sul, H.S. J. Biol. Chem. (1994) [Pubmed]
  4. Genomic organization, 5'flanking region and tissue-specific expression of mouse phosphofructokinase C gene. Gunasekera, D., Kemp, R.G. Gene (2000) [Pubmed]
  5. Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology. Bigl, M., Apelt, J., Eschrich, K., Schliebs, R. Journal of neural transmission (Vienna, Austria : 1996) (2003) [Pubmed]
  6. Regulation of glycolysis in the mouse blastocyst during delayed implantation. Nieder, G.L., Weitlauf, H.M. J. Exp. Zool. (1984) [Pubmed]
  7. Metabolic evaluation of sexual dimorphism. V. Action of testosterone on the phosphofructokinase of mice submaxillary gland cells in vitro. Floridi, A., Marcante, M.L., Benassi, M. Ital. J. Biochem. (1976) [Pubmed]
  8. Glycolytic enzymes of an erythroleukemic cell line, K562, before and after hemoglobin induction. Jansen, G., Rijksen, G., de Gast, G.C., Staal, G.E. Exp. Hematol. (1983) [Pubmed]
  9. Identification of the AMP binding sites of rabbit phosphofructo-1-kinase isozymes B and C. Valaitis, A.P., Kwiatkowska, D., Krishnaraj, R., Kemp, R.G. Biochim. Biophys. Acta (1988) [Pubmed]
  10. Protective effect of Portulaca oleracea extracts on hypoxic nerve tissue and its mechanism. Wang, W., Gu, L., Dong, L., Wang, X., Ling, C., Li, M. Asia Pacific journal of clinical nutrition (2007) [Pubmed]
  11. Effect of acrylamide and related compounds on glycolytic enzymes in mouse brain in vitro. Sakamoto, J., Hashimoto, K. Arch. Toxicol. (1985) [Pubmed]
  12. 5-hydroxytryptamine, glucose uptake, glycogen utilization and carbon dioxide fixation in Hymenolepis microstoma (Cestoda). Rahman, M.S., Mettrick, D.F., Podesta, R.B. Comp. Biochem. Physiol., B (1982) [Pubmed]
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