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Gene Review

ENO3  -  enolase

Gallus gallus

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Disease relevance of LOC396016


High impact information on LOC396016

  • The phosphorylation of enolase in tyrosine occurred slowly after shift to the permissive temperature, rising from undetectable levels in phenotypically normal cells, to < 10% of the total phosphoamino acid after 3 h, and reaching 30-50% of the total phosphoamino acid by 16 h [2].
  • Two enolase (EC isoenzymes were separated by isoelectric focussing revealing that it was the gammagamma form (pI 5.2-6.7) which had become phosphorylated at tyrosine residues after transformation [2].
  • Although transformation had no apparent effect on the K0.5 of enolase (26 +/- 4 microM for 2-phosphoglycerate), its specific activity was reduced by about one third [2].
  • Using chicken embryo fibroblasts infected with the NY68 transformation-defective temperature-sensitive mutant of Rous sarcoma virus, the phosphorylation and enzyme kinetic properties of enolase have been studied before, and at different stages after, the onset of transformation [2].
  • We observed that pp60c-src activity in crypt cytoskeleton was higher (on average, fourfold as measured by enolase phosphorylation or sevenfold as measured by autophosphorylation) than that in cytoskeletons from differentiated enterocytes [5].

Biological context of LOC396016


Anatomical context of LOC396016

  • The complete amino acid sequence of chicken skeletal-muscle enolase [7].
  • Enolase of the chicken lens epithelium was found to be an enzymatically active dimeric protein of molecular weight 100,000 daltons and representing alpha-enolase [8].
  • In mixed cultures of neurons and glial cells both enolase activities were raised in absence of serum [9].
  • Developmental changes in the levels of translatable mRNAs for alpha and beta enolase subunits in chicken muscle were determined using the rabbit reticulocyte cell-free translation system [10].
  • Immunofluorescent double staining experiments with antibodies against Neuron-specific enolase and with a neural crest marker (HNK-1) indicated no demonstrable overlap between the CgA-positive cells and either of the above cell populations, demonstrating the existence of three distinct neuronal/neuroendocrine cell populations in the avian thymus [11].

Associations of LOC396016 with chemical compounds


Other interactions of LOC396016

  • The cells are immunoreactive with antibodies to MAP2 and neuron specific enolase, two proteins characteristic of neurons [14].
  • Though no general pattern of enzyme activities in different species is discernible, high activities of TPI followed, in decreasing order, by GAPDH, enolase, PK, LDH and aldolase appear to be more common [15].
  • In contrast, the use of cellular promoters such as the neuron-specific enolase promoter or hybrid promoters such as the chicken beta-actin/CMV promoter resulted in sustained transgene expression [16].
  • Cultures active in production of the growth regulator also produced nonneuronal-type enolase and glutamine synthetase [17].
  • In the third pattern (proprotein convertase 3, somatostatin, dopamine-beta-hydroxylase, neuron-specific enolase, vasoactive intestinal polypeptide, and met-enkephalin), differences in immunoreactivity were observed between the medullary and thoracolumbar sympathetic ganglion cells [18].

Analytical, diagnostic and therapeutic context of LOC396016


  1. Structural elucidation of N-terminal post-translational modifications by mass spectrometry: application to chicken enolase and the alpha- and beta-subunits of bovine mitochondrial F1-ATPase. Gibson, B.W., Daley, D.J., Williams, D.H. Anal. Biochem. (1988) [Pubmed]
  2. Influence of transformation by Rous sarcoma virus on the amount, phosphorylation and enzyme kinetic properties of enolase. Eigenbrodt, E., Fister, P., Rübsamen, H., Friis, R.R. EMBO J. (1983) [Pubmed]
  3. Microarray analysis identifies Autotaxin, a tumour cell motility and angiogenic factor with lysophospholipase D activity, as a specific target of cell transformation by v-Jun. Black, E.J., Clair, T., Delrow, J., Neiman, P., Gillespie, D.A. Oncogene (2004) [Pubmed]
  4. Enolase activity in chicken embryo primary retina cells is not affected by exposure to a 60-Hz electric field. Dutta, S.K., Nazar, A.S., Verma, M. Cancer Biochem. Biophys. (1998) [Pubmed]
  5. Intestinal crypt cells contain higher levels of cytoskeletal-associated pp60c-src protein tyrosine kinase activity than do differentiated enterocytes. Cartwright, C.A., Mamajiwalla, S., Skolnick, S.A., Eckhart, W., Burgess, D.R. Oncogene (1993) [Pubmed]
  6. Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis. Tanaka, M., Maeda, K., Nakashima, K. J. Biochem. (1995) [Pubmed]
  7. The complete amino acid sequence of chicken skeletal-muscle enolase. Russell, G.A., Dunbar, B., Fothergill-Gilmore, L.A. Biochem. J. (1986) [Pubmed]
  8. Enolase in the avian and turtle lens. Rudner, G., Katar, M., Maisel, H. Curr. Eye Res. (1990) [Pubmed]
  9. Factors involved in expression of neuron-specific and non-neuronal enolase activity in developing chick brain and in primary cultures of chick neurons. Ledig, M., Tholey, G., Mandel, P. Brain Res. (1985) [Pubmed]
  10. Switching in levels of translatable mRNAs for enolase isozymes during development of chicken skeletal muscle. Tanaka, M., Sugisaki, K., Nakashima, K. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  11. Immunohistochemical assessment of the neurosecretory cells of the chicken thymus using a novel monoclonal antibody against avian chromogranin A. Oubre, C.M., Zhang, X., Clements, K.E., Porter, T.E., Berghman, L.R. Dev. Comp. Immunol. (2004) [Pubmed]
  12. Inactivation of chicken muscle enolase by carbodiimide and glycine methyl ester. Russell, G.A., Fothergill, L.A. FEBS Lett. (1982) [Pubmed]
  13. Characterization of transverse tubule membrane proteins: tentative identification of the Mg-ATPase. Okamoto, V.R., Moulton, M.P., Runte, E.M., Kent, C.D., Lebherz, H.G., Dahms, A.S., Sabbadini, R.A. Arch. Biochem. Biophys. (1985) [Pubmed]
  14. Chicken optic tract cells showing GABA-like immunoreactivity: morphological and immunocytochemical studies. Granda, R.H., Ten Eyck, G.R., Crossland, W.J. J. Comp. Neurol. (1991) [Pubmed]
  15. Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order. Mathur, R.L., Reddy, M.C., Yee, S., Imbesi, R., Groth-Vasselli, B., Farnsworth, P.N. Exp. Eye Res. (1992) [Pubmed]
  16. Recombinant AAV-mediated gene delivery to the central nervous system. Tenenbaum, L., Chtarto, A., Lehtonen, E., Velu, T., Brotchi, J., Levivier, M. The journal of gene medicine. (2004) [Pubmed]
  17. Growth regulator from spinal cord: produced in cultures of glial cells. Kagen, L.J., Miller, S.L., Labissiere, A. Brain Res. (1981) [Pubmed]
  18. Immunocytochemical developmental patterns of the thoracolumbar sympathetic chain in the chick and a comparison with its adrenal counterpart. Sánchez-Montesinos, I., Mérida-Velasco, J.R., Hita-Contreras, F., Espín-Ferra, J., Rodríguez-Vázquez, J.F., De La Cuadra, C., Pasini, B., Mérida-Velasco, J.A. Histol. Histopathol. (2005) [Pubmed]
  19. The neural marker neuron-specific enolase in the development of embryo chicken retina: a morphological description. Prada Oliveira, A., Verástegui Escolano, C., González Moreno, M., Perez Rios, N., Fernández-Trujillo, F.J. Italian journal of anatomy and embryology = Archivio italiano di anatomia ed embriologia. (1997) [Pubmed]
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