Disease relevance of LOC396016

• In the case of chicken enolase, a peptide was isolated from a Staphylococcus aureus proteinase digest by HPLC and analyzed directly by fast atom bombardment mass spectrometry (FABMS) [1].
• Influence of transformation by Rous sarcoma virus on the amount, phosphorylation and enzyme kinetic properties of enolase [2].
• Interestingly, this group includes the hypoxia-inducible factor-1 alpha (Hif-1alpha) transcription factor and the glycolytic enzyme enolase, suggesting that adaptation to hypoxia could play a role in tumorigenesis by v-Jun [3].
• Under similar conditions, the specific activity of enolase is decreased in neuroblastoma cell line (NG108) [4].

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 4.2.1.11) 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

• The chicken beta-enolase, on the other hand, shares 84-85% amino acid sequence homology with mammalian beta-enolases [6].
• Chicken alpha- and beta-enolase cDNAs have been cloned and analyzed to reveal that alpha- but not beta-enolase has a Src-dependent phosphorylation site [6].
• Northern blot analysis indicated that alpha-enolase mRNA can be expressed in a wide range of chicken tissues, and that the gene expression switch from alpha to beta-enolase occurs just after hatching in developing chicken muscle [6].
• Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis [6].
• Peptides generated from enzymatic hydrolysis of chicken enolase and the alpha- and beta-subunits of bovine F1-ATPase were analyzed by mass spectrometry to determine the nature of their modified N-termini [1].

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

• The amino acid sequence between residues 33 and 50 in chicken alpha-enolase coincided with the reported tryptic peptide sequence of rabbit beta-enolase, the tyrosine residue in which was phosphorylated in vitro by Rous-sarcoma-virus tyrosine kinase [6].
• In chicken beta-enolase, on the other hand, the corresponding tyrosine residue was found to be replaced with a histidine residue, in accordance with the previous observation that chicken beta-enolase was not phosphorylated in vivo or in vitro [6].
• Inactivation of chicken muscle enolase by carbodiimide and glycine methyl ester [12].
• A number of the proteins found in vesicular TT preparations were found to be extractable by a mild Triton-X100 treatment and were identified as aldolase, enolase, creatine kinase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and pyruvate kinase [13].
• Steroid hormones, insulin and serum albumin also modify both enolase activities in pure neurons and in mixed cultures of neurons and glial cells [9].

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

• The localisation and distribution of Neuron-specific enolase is reported in the avian Gallus domesticus retinal development by using immunocytochemistry [19].

References