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Gene Review

ENO1  -  enolase 1, (alpha)

Bos taurus

 
 
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Disease relevance of ENO1

 

High impact information on ENO1

  • Northern analyses revealed that NNE mRNA hypoxic up-regulation began at 1-2 h, peaked at 18 h, persisted for 48 h, and returned to base line after return to 21% O2 for 24 h [1].
  • Western analysis of subcellular fractions localized NNE primarily to the cytoplasm and confirmed that it was up-regulated 2.3-fold by hypoxia [1].
  • The presence of single nerve cell bodies and small ganglia in the retractor penis muscle and the penile artery of the bull was demonstrated by using antisera to neurofilament protein and neuron specific enolase [2].
  • Immunohistochemical study on the distribution of neuron-specific enolase- and peptide-containing nerves in the omasum of cattle [3].
  • The expression of alpha-enolase isoform 1 was enhanced after 17beta-oestradiol treatment [4].
 

Biological context of ENO1

 

Anatomical context of ENO1

 

Associations of ENO1 with chemical compounds

 

Other interactions of ENO1

 

Analytical, diagnostic and therapeutic context of ENO1

References

  1. Non-neuronal enolase is an endothelial hypoxic stress protein. Aaronson, R.M., Graven, K.K., Tucci, M., McDonald, R.J., Farber, H.W. J. Biol. Chem. (1995) [Pubmed]
  2. Histochemical demonstration of nerve cell bodies in the retractor penis muscle and the penile artery of the bull. Alaranta, S., Uusitalo, H., Klinge, E., Palkama, A., Sjöstrand, N.O. Neuroscience (1989) [Pubmed]
  3. Immunohistochemical study on the distribution of neuron-specific enolase- and peptide-containing nerves in the omasum of cattle. Kitamura, N., Yamada, J., Yamashita, T. J. Comp. Neurol. (1987) [Pubmed]
  4. Proteomic approach to identify changes in protein expression modified by 17beta-oestradiol in bovine vascular smooth muscle cells. Molero, L., García-Méndez, A., Alonso-Orgaz, S., Carrasco, C., Macaya, C., López Farré, A.J. Clin. Sci. (2005) [Pubmed]
  5. Complex of brain D-phosphoglycerate mutase and gamma enolase and its reactivation by D-glycerate 2,3-bisphosphate. Batke, J., Nazaryan, K.B., Karapetian, N.H. Arch. Biochem. Biophys. (1988) [Pubmed]
  6. Highly sensitive enzyme immunoassay for bovine chromogranin A: application for studies of regional distribution in bovine central nervous system. Kawakubo, A., Takatsuki, K., Yoneda, M., Kurokawa, M., Suzuki, A., Semba, R., Kato, K. J. Mol. Neurosci. (1989) [Pubmed]
  7. Interaction of rabbit muscle enolase and 3-phosphoglycerate mutase studied by ELISA and by batch gel filtration. Nazaryan, K.B., Climent, F., Simonian, S., Tompa, P., Batke, J. Arch. Biochem. Biophys. (1992) [Pubmed]
  8. Immunocytochemical demonstration of hydroxyindole O-methyltransferase (HIOMT), neuron-specific enolase (NSE) and S-100 protein in the bovine pineal gland. Kuwano, R., Iwanaga, T., Nakajima, T., Masuda, T., Takahashi, Y. Brain Res. (1983) [Pubmed]
  9. Comparative evaluation of the performance of two commercial kits for the detection of central nervous system tissue in meat. Hughson, E., Reece, P., Dennis, M.J., Oehlschlager, S. Food additives and contaminants. (2003) [Pubmed]
  10. Enzymes and pathways of glucose utilization in bovine adrenal medulla. Millaruelo, A.I., Sagarra, M.R., Delicado, E., Torres, M., Miras-Portugal, M.T. Mol. Cell. Biochem. (1986) [Pubmed]
  11. Altered erythrocyte enolase ans pyruvate kinase activity and blood magnesium concentration in cattle with industrial fluorosis. Sterkowicz, J., Gumińska, M. Folia biologica. (1977) [Pubmed]
  12. Development of an integrated procedure for the detection of central nervous tissue in meat products using cholesterol and neuron-specific enolase as markers. Lücker, E., Eigenbrodt, E., Wenisch, S., Failing, K., Leiser, R., Bülte, M. J. Food Prot. (1999) [Pubmed]
  13. Effect of acrylamide and related compounds on glycolytic enzymes in mouse brain in vitro. Sakamoto, J., Hashimoto, K. Arch. Toxicol. (1985) [Pubmed]
  14. Large scale preparation and crystallization of neuron-specific enolase. Ishioka, N., Isobe, T., Kadoya, T., Okuyama, T., Nakajima, T. J. Biochem. (1984) [Pubmed]
  15. Glycolytic enzyme interactions with tubulin and microtubules. Walsh, J.L., Keith, T.J., Knull, H.R. Biochim. Biophys. Acta (1989) [Pubmed]
  16. Degenerative axonal swellings in the trigeminal ganglia of cattle. Furuoka, H., Watanabe, T., Matsui, T., Narama, I. Acta Neuropathol. (1996) [Pubmed]
  17. Three cases of carcinoid in the equine nasal cavity and maxillary sinuses: histologic and immunohistochemical features. van Maanen, C., Klein, W.R., Dik, K.J., van den Ingh, T.S. Vet. Pathol. (1996) [Pubmed]
  18. Copurification of selected glycolytic enzymes with retinal S-antigen (arrestin) by hydroxyapatite agarose chromatography of bovine retina. Mirshahi, M., Camoin, L., Nicolas, C., Ghedira, I., Cozette, J., Faure, J.P. Curr. Eye Res. (1999) [Pubmed]
  19. Identification of antigenic proteins from Neospora caninum recognized by bovine immunoglobulins M, E, A and G using immunoproteomics. Shin, Y.S., Lee, E.G., Shin, G.W., Kim, Y.R., Lee, E.Y., Kim, J.H., Jang, H., Gershwin, L.J., Kim, D.Y., Kim, Y.H., Kim, G.S., Suh, M.D., Jung, T.S. Proteomics (2004) [Pubmed]
  20. Triose phosphate isomerase, a novel enzyme-crystallin, and tau-crystallin in crocodile cornea. High accumulation of both proteins during late embryonic development. Kathiresan, T., Krishnan, K., Krishnakumar, V., Agrawal, R., Anand, A., Muralidhar, D., Mishra, A.K., Dhople, V.M., Aggrawal, R.K., Sharma, Y. FEBS J. (2006) [Pubmed]
 
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