Disease relevance of ENO1

• Analysis of hypoxia response elements in the ENO1 and Ldha gene promoters revealed that each contains two functionally-essential HIF-1 sites arranged as direct and inverted repeats, respectively [1].
• Specifically, the gene ENO1 was amplified in six and the gene PAX7 in five out of 37 cases which included both biopsies and paraffin-embedded tissues of squamous cell lung carcinomas [2].
• Introduction of in vitro transcribed ENO1 mRNA into neuroblastoma cells induces cell death [3].
• Astrocytomas, ependymomas, oligodendrocytomas, meningiomas and acoustic neuromas all contained varying quantities of alpha enolase [4].
• Measurement of tissue-specific enolase isoenzymes may be of assistance in identifying small cell carcinomas of the lung and in distinguishing them from other pulmonary tumors [5].

Psychiatry related information on ENO1

• Brain levels of neuron-specific and nonneuronal enolase in Huntington's disease [6].
• Our results suggest that increased activity of SOD and NSE in blood cells may be related to liver injury mainly in alcoholism while increased NNE activity may also be a marker of alcohol abuse without liver injury [7].
• Neuron-specific enolase (NSE), a glycolytic enzyme enolase found in brain, was examined in the cerebrospinal fluid and serum of 30 patients with presumptive Alzheimer's disease (AD) and of 13 healthy controls and evaluated as a measure of neuronal functional activity associated with AD [8].
• Delirium tremens: some clinico-chemical features. A study of alanine-aminotransferase, alcaline phosphatase, prothrombine and enolase [9].

High impact information on ENO1

• In terms of sequence similarity, size, and other physical characteristics delta-crystallin is closely related to argininosuccinate lyase, tau-crystallin to enolase, and SIII-crystallin to glutathione S-transferase; moreover, it has recently been demonstrated that epsilon-crystallin is an active lactate dehydrogenase [10].
• The activity of pp60c-src from six of nine carcinoma cell lines was higher (on average, fivefold as measured by enolase phosphorylation, or eightfold as measured by autophosphorylation) than that of pp60c-src from normal colonic mucosal cells, or human or rodent fibroblasts [11].
• RESULTS: Activity of Yes in adenomas at greatest risk for cancer was significantly greater (12- or 14-fold as measured by enolase or autophosphorylation, respectively) than activity in adjacent normal mucosa [12].
• Neuron-specific enolase (NSE) is a neuronal form of the glycolytic enzyme enolase, which was first found in extracts of brain tissue, and was later shown to be present in APUD (amine precursor uptake and decarboxylation) cells and neurons of the diffuse neuroendocrine system but not in other peripheral cells [13].
• These procedures are illustrated by applications to proton abstractions catalyzed by enolase and methylamine dehydrogenase and hydride-transfer reactions by alcohol dehydrogenase and xylose isomerase [14].

Chemical compound and disease context of ENO1

• The gamma-subunit of 2-phospho-D-glycerate hydrolyase, E.C. 4.2.1.11 (enolase), neuron-specific enolase (NSE), is present at high concentrations in neurons and neuroendocrine cells and has therefore recently been introduced as a marker for neuroendocrine tumors [15].
• Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas [16].
• Phosphoglycerate mutase, enolase and 2,3-bisphosphoglycerate phosphatase presented greater changes in the oestrogen receptor-negative/progesterone receptor-negative breast carcinomas than in the steroid receptor-positive tumours [17].
• The activities of hexokinase, phosphofructokinase, aldolase, enolase and pyruvate kinase were studied in breast cancer tissues, in comparison to benign breast disease and normal breast tissues [18].
• 80 patients were randomly divided into two subgroups (SMAR(X)T vs. standard PVC control) and analyzed for the kinetic of cerebral ischemia markers neuronspecific enolase, protein S100 and neuropsychologically tested with the Mini-Mental-Status Test (MMST) before and after the operation [19].

Biological context of ENO1

• The finding that a transcriptional repressor of the c-myc oncogene is an alternatively translated product of the ENO1 gene, which maps to a region of human chromosome 1 frequently deleted in human cancers, makes ENO1 a potential candidate for tumor suppressor [20].
• The karyotypic abnormalities in these cell lines were exploited as chromosomal landmarks; we could thus show that the telomere to centromere gene order was PTPRZ2-(MBP-1/ENO1/ENO1L1)-(C1orf1/XBX1)-+ ++FRAP2 [21].
• Gene amplification at chromosome 1pter-p33 including the genes PAX7 and ENO1 in squamous cell lung carcinoma [2].
• The haemolysate of an individual with the heterozygous ENO1/ENO2 genotype had a triple banded pattern replacing band I, a double-banded pattern replacing band II and a single weakly staining band III [22].
• Interestingly, a similar but much stronger dose-dependent reduction of cell growth was observed by transfection of in vitro transcribed ENO1 mRNA into neuroblastoma cells [3].

Anatomical context of ENO1

• Alpha enolase is demonstrable in astrocytes, ependymal cells, capillary endothelial cells [4].
• Levels of the cell-specific brain isoenzymes of enolase were determined in basal ganglia and cerebral cortical tissue of Huntington's disease and age- and sex-matched control brain [6].
• In normal liver, alpha-enolase was positively stained in almost all hepatocytes and bile duct cells. beta- and gamma-enolases were localized in hepatocytes and bile duct cells, respectively [23].
• This is almost the same localization pattern of enolase isozymes as in preexisting bile duct cells. gamma-Enolase was detected in some hepatocytes in eight of 12 cases with chronic active hepatitis and six of 12 cases with cirrhosis [23].
• 1. Four major enolase isozymes have been identified in human tissues and are referred to as L, M, 'intermediate' and 'fast'. The M isozyme is the major form found in skeletal muscle and heart extracts and the L isozyme the major form found in extracts of liver and most other tissues [24].

Associations of ENO1 with chemical compounds

• The differential activation of the ENO1 and ENO2 promoters during tachyzoite to bradyzoite differentiation was investigated by deletion analysis of 5'-flanking regions fused to the chloramphenicol acetyltransferase reporter followed by transient transfection [25].
• Functionally, the neuronal enolase has been demonstrated to be uniquely stable to concentrations of chloride salts that rapidly inactivate the glial enzyme [26].
• The fine structural localization of NSE in neoplastic cells suggests that the conversion of 2-D-glycerophosphate to phosphoenolpyruvate by enolase may occur on the membrane and, in the case of astrocytic tumours, on the cytoplasmic filaments as well as in the cytoplasm [27].
• Enolase (EC 4.2.1.11) is an enzyme of the glycolytic pathway catalyzing the dehydratation reaction of 2-phosphoglycerate [28].
• Expression of the human adenylate kinase isozymes, phosphopyruvate hydratase, 6-phosphogluconate dehydrogenase, and phosphoglucomutase-1 in man-rodent somatic cell hybrids [29].

Physical interactions of ENO1

• Plasminogen binding activity of a molecular weight similar to alpha-enolase also was present in a variety of other cell types [30].
• Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity [31].
• This shorter form of alpha-enolase is able to bind the MBP-1 consensus sequence and to downregulate expression of a luciferase reporter gene under the control of the c-myc P2 promoter [20].
• The Myc promoter-binding protein-1 (MBP-1) is a 37-38 kDa protein that binds to the c-myc P2 promoter and negatively regulates transcription of the protooncogene [20].

Enzymatic interactions of ENO1

• Kinase experiments demonstrated that in the presence of AAP1, the ability of c-ABL to phosphorylate either glutathione S-transferase-CRK or enolase was inhibited [32].

Regulatory relationships of ENO1

• In contrast, levels of NSE in cerebral cortical tissue from Huntington's disease patients remains unchanged in comparison with controls whereas NNE levels are significantly increased [6].
• Together, our results suggested a novel role of MBP-1 for suppression of prostate cancer cell growth by regulating the MEK5-mediated signaling pathway [33].
• Treatment of the responsive human prostate carcinoma cell line PC3 with TGF beta induces a rapid and specific decrease in cellular levels of pp60Src and pp53/56Lyn and a corresponding decrease in their protein kinase activity when the assays were performed in vitro using the exogenous substrate enolase [34].
• Serum samples from 52 patients with RA and 40 healthy controls were tested for presence of antibodies against citrullinated and non-citrullinated alpha-enolase by immunoblotting of the purified antigens [35].

Other interactions of ENO1

• Conserved canonical E boxes in ENO1, HK2, and LDHA occur in 31- to 111-bp islands with high interspecies sequence identity (>65%) [36].
• A specific radioimmunoassay is described for NNE and NSE with the studies reported indicating that neuronal enzyme levels vary considerably when different brain areas are compared, suggesting a relationship between functional activity and levels of NSE [26].
• Variable levels of secretion of enolase and GAPDH proteins as well as of the Plg activation cofactor function were detected in strains representing major taxonomic groups of the genus Lactobacillus [37].
• Comparative gene mapping of man and Cebus capucinus for PGD, ENO1, PGM2, and SOD1 [38].
• Chromosome 1: lods on linkage among eight loci: Do, ENO1 Fy, PGM1, Rh, UMPK, Sc, and PGD [39].

Analytical, diagnostic and therapeutic context of ENO1

• Furthermore, electrophoresis mobility shift assays demonstrated the presence of DNA-binding proteins in tachyzoite and bradyzoite nuclear lysates that bound to stress response elements (STRE), heat shock-like elements (HSE) and other cis-regulatory elements in the upstream regulatory regions of ENO1 and ENO2 [25].
• By flow cytometry and immunofluorescence analyses and using human enolase-specific antibody, human pharyngeal cells (Detroit 562) also were found to express enolase on their surface [40].
• The present study examines the enolase isoenzyme pattern in human cerebral metastases of various primary progeny, using electrophoresis of tumor tissue extracts as well as immunohistochemistry [41].
• Enolase isozymes (alpha, beta and gamma enolases) in the extracts of pediatric tumors (neuroblastoma, ganglioneuroblastoma, rhabdomyosarcoma and Wilms' tumor) were determined by means of enzyme immunoassay systems [42].
• Immunoblotting with a monoclonal antibody to NSE confirmed the identity of the acidic enolase isoform as the gammagamma-isoform in both pituitary and placental samples [43].

References