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Hk2  -  hexokinase 2

Rattus norvegicus

Synonyms: HK II, Hexokinase type II, Hexokinase-2
 
 
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Disease relevance of Hk2

  • Under basal conditions, the fraction of HK I that was mitochondrial bound was five times greater than for HK II; insulin and ischemia caused a fourfold increase in HK II binding but only a doubling in HK I binding [1].
  • Therefore, overexpression of hexokinase type II in AS-30D hepatoma cells may be based, at least in part, on a stable gene amplification [2].
 

High impact information on Hk2

  • Hexokinase type II is highly overexpressed in many cancer cells, where it plays a pivotal role in the high glycolytic phenotype [2].
  • The expression levels of Glut-1, Glut-3, and HK-II were determined by immunostaining and semiquantitative evaluation [3].
  • These events are isoform specific, suggesting that HK I and HK II are independently regulated and implying that they perform different roles in cardiac glucose regulation [1].
  • Immunoblots detected a decrease in hypothyroid hearts for muscle carnitine palmitoyltransferase I (CPT I) and a marked increase in pyruvate dehydrogenase kinase (PDK)-2 with no changes in liver CPT I, PDK-4, or hexokinase 2 [4].
  • The diastereomers of adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) in the presence of Mg2+, Co2+ and Cd2+ have been used to determine the stereospecificity of the metal-nucleotide binding site of rat muscle hexokinase type II and rat liver glucokinase by the method developed by Jaffe and Cohn [J. Biol. Chem. 254, 10839-10845 (1979)] [5].
 

Biological context of Hk2

 

Anatomical context of Hk2

 

Associations of Hk2 with chemical compounds

 

Other interactions of Hk2

References

  1. A reevaluation of the roles of hexokinase I and II in the heart. Southworth, R., Davey, K.A., Warley, A., Garlick, P.B. Am. J. Physiol. Heart Circ. Physiol. (2007) [Pubmed]
  2. Glucose catabolism in cancer cells: amplification of the gene encoding type II hexokinase. Rempel, A., Mathupala, S.P., Griffin, C.A., Hawkins, A.L., Pedersen, P.L. Cancer Res. (1996) [Pubmed]
  3. Biologic correlates of intratumoral heterogeneity in 18F-FDG distribution with regional expression of glucose transporters and hexokinase-II in experimental tumor. Zhao, S., Kuge, Y., Mochizuki, T., Takahashi, T., Nakada, K., Sato, M., Takei, T., Tamaki, N. J. Nucl. Med. (2005) [Pubmed]
  4. Thyroid hormone controls myocardial substrate metabolism through nuclear receptor-mediated and rapid posttranscriptional mechanisms. Hyyti, O.M., Ning, X.H., Buroker, N.E., Ge, M., Portman, M.A. Am. J. Physiol. Endocrinol. Metab. (2006) [Pubmed]
  5. Metal-nucleotide structure at the active sites of the mammalian hexokinases. Darby, M.K., Trayer, I.P. Eur. J. Biochem. (1983) [Pubmed]
  6. Regulation of glucose transporter and hexokinase II expression in tissues of diabetic rats. Burcelin, R., Printz, R.L., Kande, J., Assan, R., Granner, D.K., Girard, J. Am. J. Physiol. (1993) [Pubmed]
  7. Activity and isoenzyme patterns of glycolytic enzymes during perinatal development of rat lung. Rijksen, G., Staal, G.E., Streefkerk, M., de Vries, A.C., Batenburg, J.J., Heesbeen, E.C., van Golde, L.M. Biochim. Biophys. Acta (1985) [Pubmed]
  8. Hexokinase type II from rat skeletal muscle. Easterby, J.S., Qadri, S.S. Meth. Enzymol. (1982) [Pubmed]
  9. Short-term endurance training results in a muscle-specific decrease of myostatin mRNA content in the rat. Matsakas, A., Friedel, A., Hertrampf, T., Diel, P. Acta Physiol. Scand. (2005) [Pubmed]
  10. Affinity labelling of rat-muscle hexokinase type II by a glucose-derived alkylating agent. Connolly, B.A., Trayer, I.P. Eur. J. Biochem. (1979) [Pubmed]
  11. Changes in pulmonary expression of hexokinase and glucose transporter mRNAs in rats adapted to hyperoxia. Allen, C.B., Guo, X.L., White, C.W. Am. J. Physiol. (1998) [Pubmed]
 
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