Disease relevance of ENO3

• Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis [1].
• In chronic active hepatitis and cirrhosis, proliferated biliary ductular cells had both alpha- and gamma-enolases, but did not express beta-enolase [2].
• Before treatment, a serum sample from a patient with rhabdomyosarcoma contained a high level of beta enolase and serum samples from patients with (ganglio)neuroblastoma contained high levels of gamma enolase [3].
• Hypoxia regulates beta-enolase and pyruvate kinase-M promoters by modulating Sp1/Sp3 binding to a conserved GC element [4].
• This indicates that the immunoreactive epitopes are largely conserved from yeast to human, but are not present in beta-enolase. alpha-Enolase autoantibodies are not specific to pituitary autoimmune disease and have been reported in other autoimmune diseases [5].

Psychiatry related information on ENO3

• Here we report the results of the first extensive study of beta enolase expression during human development [6].
• DESIGN: Cross-sectional study on adults from Western India. SETTING: Rural, semi urban, urban higher/middle/lower socioeconomic regions (HSE/MSE/LSE) having diverse dietary habits and environmental conditions [7].
• OBJECTIVES: Regular access to a multi-sensory environment (MSE or Snoezelen room) was compared with a non-complex sensory environment for individuals with learning disabilities [8].
• Exercise tolerance was assessed objectively by percent predicted cycle power output (%PO), and subjectively by a self-efficacy questionnaire for ambulatory (ASE) and muscular (MSE) items and by a disease-specific, health-related, quality-of-life questionnaire (HRQL) [9].

High impact information on ENO3

• A regulatory element upstream of the human myoglobin gene functions as a muscle-specific enhancer (MSE) in conjunction with core promoter elements of the myoglobin gene, but not in combination with the simian virus 40 (SV40) early promoter [10].
• We conclude that mammalian TATA-box elements are functionally heterogeneous, and suggest that this heterogeneity reflects differential interactions with distinctive TATA box-binding factors, only some of which can act cooperatively with MSE-binding proteins to generate an active transcriptional complex [10].
• In adult human muscle, over 90% of enolase activity is accounted for by the beta-enolase subunit, the protein product of the ENO3 gene [1].
• The ENO3 gene of our patient carries two heterozygous missense mutations affecting highly conserved amino acid residues; a G467A transition changing a glycine residue at position 156 to aspartate, in close proximity to the catalytic site, and a G1121A transition changing a glycine to glutamate at position 374 [1].
• We demonstrated that all five of these proteins specifically activate exon inclusion of cardiac troponin T minigenes in vivo via muscle-specific splicing enhancer (MSE) sequences [11].

Chemical compound and disease context of ENO3

• In this paper, we describe analyses of the muscle-specific pyruvate kinase-M and beta-enolase promoters that implicate additional mechanisms for the regulation of glycolytic enzyme gene transcription by hypoxia [4].
• RECENT FINDINGS: New inherited defects are still being discovered, such as the beta-enolase deficiency in glycogenosis type XIII and mutations in the gene encoding an esterase/lipase/thioesterase protein in Chanarin-Dorfman syndrome, a multisystem triglyceride storage disease [12].
• These data imply that serum beta-enolase may be a more effective marker for early myocardial infarction, particularly in milder cases, than measurement of creatine kinase activity [13].
• Crude ethanolic extract of Indian medicinal plant, Desmodium gangeticum (A001) and its three fractions-hexane (F002), n-butanol (F003) and aqueous (F004) were evaluated chemoprophylactically and chemotherapeutically against experimental visceral leishmaniasis in hamsters [14].

Biological context of ENO3

• The role of tissue-specific methylation events within ENO3 remains to be determined [15].
• Molecular structure of the human muscle-specific enolase gene (ENO3) [16].
• The muscle-specific enolase is an early marker of human myogenesis [6].
• Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE) [17].
• These results show that the determination of beta-enolase in plasma may be useful for estimating myocardial damage during open heart surgery [18].

Anatomical context of ENO3

• Furthermore, beta enolase subunit is expressed in proliferating myoblasts from both embryonic and post-natal muscles [6].
• Melanocytes in benign neoplasms stained moderately strongly for both alpha enolase and gamma enolase but staining for beta enolase was consistently negative [19].
• The enolase isoenzyme composed of the beta subunit (alpha beta or beta beta enolase) is distributed predominantly in the heart and skeletal muscles [18].
• Since plasma carbonic anhydrase III, which is known to be localised only in the skeletal muscle, did not increase during the surgery, we suggest that the major portion of the elevated plasma beta-enolase was derived from heart muscle [18].
• Beta-enolase in blood plasma during open heart surgery [18].

Associations of ENO3 with chemical compounds

• A purified human serum protein previously named "modifying protein," which is responsible for the modification of creatine kinase-M and alpha-enolase subunits, modifies beta beta enolase and also has a pH-activity profile identical to that for serum [20].
• Under acid conditions, ethylene oxide was found to be oxidized on the platinum oxide surface at +550 mV vs MSE, thus enabling its monitoring via the measurement of the associated current [21].
• Diets contained either i) margarine (M), ii) margarine with phytosterol esters (MSE) (1.84 g/d), or iii) margarine with phytostanol esters (MSA) (1.84 g/d) [22].
• Plasma total cholesterol level at d 21/22 was lower (P < 0. 05) for MSE (13.4%) but not MSA (10.2%) versus M (6.0%) diets [22].
• Near-point testing revealed less residual accommodation with cyclopentolate (difference in MSE, OD=-0.27 +/- 0.51 D, t=2.68, P=.006; OS=-0.32 +/- 0.49 D, t=3.46, P=.001) [23].

Other interactions of ENO3

• The beta-enolase protein was dramatically reduced in the muscle of our patient, by both immunohistochemistry and immunoblotting, while alpha-enolase was normally represented [1].
• The differentiation of extraocular muscles was studied immunohistochemically in externally normal human embryos (Carnegie stages 13-23), using antibodies to carbonic anhydrase (CA) III and beta-enolase as the markers of type 1 and type 2 muscle fibers, respectively [24].
• Comparison of beta enolase and myoglobin as histological markers of rhabdomyosarcoma [25].
• Specimens of human thymus and thymoma obtained from 81 patients including 22 with myasthenia gravis (MG), ranging in age from 10 weeks of gestation to 75 years were examine by the indirect immunoperoxidase technique using three different striated muscle markers: myoglobin, CPK-mm and beta-enolase [26].

Analytical, diagnostic and therapeutic context of ENO3

• Muscle beta-enolase deficiency should be considered in the differential diagnosis of metabolic myopathies due to inherited defects of distal glycolysis [1].
• To see whether it may be a useful indicator of myocardial damage, concentrations of beta-enolase (the beta subunit of enolase) were determined in serial blood samples taken from 18 patients who underwent mitral valve replacement, using a highly sensitive enzyme immunoassay method [18].
• Plasma concentrations of beta-enolase increased as quickly as those of CK-MB after reperfusion [18].
• This protein was further isolated from K. pneumoniae cell mass in two ways, namely preparative SDS-polyacrylamide gel electrophoresis and specific affinity chromatography using immobilized affinity-purified rabbit antibody raised against human beta-enolase [27].
• There was a concurrent 7-day self-registration of subjective psychological and somatic symptoms, using a validated visual analogue scale (minor symptom evaluation profile; MSE) [28].

References