Distribution of nervous system-specific forms of enolase in peripheral tissues

doi:10.1016/0006-8993(82)90455-3

Brain Research

Volume 237, Issue 2, 15 April 1982, Pages 441-448

https://doi.org/10.1016/0006-8993(82)90455-3 Get rights and content

Abstract

The distribution of 3 forms of rat enolase (αα, αγ and γγ forms), including nervous system-specific forms (αγ and γγ), was determined in various tissues with a sensitive enzyme immunoassay system. The brain and spinal cord contained more than 100 pmol/mg protein of the αα, αγ and γγ enolases. Organs such as the lungs, heart, spleen, liver and kidney contained similarly high levels of αα enolase, but these tissues contained αγ and γγ enolases at levels less than 1% of the central nervous tissues. High levels of the αγ (10pmol/mg) and the γγ (1.5pmol/mg) forms were found in rectum, bladder, and uterus. In gut, major portions of the nervous system-specific forms were localized in the muscle layers. Skeletal muscle and diaphragm, which are composed of striated muscle, contained low levels of the 3 forms of enolase. Megakaryocytes separated from the suspension of bone marrow contained 11.3, and 0.53 amol/cell of the αα and γγ enolases, respectively, with little, if any, of the αγ form.

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Cited by (107)

Neuron specific enolase as a marker of seizure related neuronal injury
2019, Neurochemistry International
Citation Excerpt :
Brain derived neurotropic factor (BDNF) (Toro et al., 2007) myelin basic protein (MBP), glial fibrillary acidic protein (GFAP) (Gurnett et al., 2003), microfilament (Lamers et al., 2003), and different enzymes (enolase, aldolase, pyruvate kinase, lactate dehydrogenase, creatine phosphokinase) (Royds et al., 1983) have been studied. Among all, neuron-specific enolase (NSE) is the most widely investigated biochemical markers of nervous tissue damage, as it is present only in low concentrations outside the nervous system (Kato et al., 1982) and found to be relevant and reliable biomarker in assessing the brain injury (El-Maraghib et al., 2013). Its role in differentiating seizure or syncope was evaluated by Lee SY et al. and suggested that increased NSE was associated with seizure activity thus estimating the NSE levels serve as a diagnostic marker (Lee et al., 2010).
and purpose: Neuron specific enolase (NSE) is an established biomarker of neuronal damage. It is not clear how much seizures contribute to the neuronal damage, morbidity or mortality in critically ill neurology patients. The aim of this study is to determine the impact of seizures on neuronal injury in critically ill neurology patients by using neuron specific enolase as a biomarker.
Forty patients with clinical evidence of acute central nervous system disease associated with seizures were included as critically ill neurology patients with seizures [CINPS] (age in years 38.8 ± 17.54, mean ± SD; 22 males) and 43 age and sex-matched acute central nervous system disease without seizures were recruited as critically ill neurology patients [CINP] (age in years 37.84 ± 17.38 years mean ± SD; 24 males) The serum NSE assays were performed in CINPS (within 24 h of last seizure) and in CINP using an enzyme immunoassay kit.
The level of serum neuron specific enolase was significantly higher in CINP with seizures compared to those without seizures. The length of ICU stay was more prolonged in those with seizures. There was a close correlation between the NSE levels and frequency of seizures. There was no significant difference in the mortality between both the groups.
NSE a marker of neuronal injury was elevated in patients with acute central nervous system diseases. It is significantly higher in patients with seizures in comparison to those without seizures. This warrants further studies to document aggressive treatment of seizures in acute neurologically ill patients can reduce neuronal damage.
Effect of carbamazepine and oxcarbazepine on serum neuron-specific enolase in focal seizures: A randomized controlled trial
2017, Epilepsy Research
Citation Excerpt :
NSE originates predominantly from the neuronal cytoplasm and neuroendocrine cells. Neuronal damage and impairment of the integrity of blood brain barrier can be detected by the release of NSE into CSF and eventually into the blood (Kato et al., 1982; Royds et al., 1983). NSE is therefore regarded as a marker of neuronal damage and prognosis in various disorders associated with cell damage in the central or peripheral nervous system.
Neuron-specific enolase (NSE) is the most investigated biomarker in the context of epilepsy and brain damage. The present study was conducted to investigate the change in serum NSE in patients with focal seizure and the effect of carbamazepine and oxcarbazepine on serum NSE. The present study is a randomized, open-label, parallel design clinical trial (ClinicalTrials.gov Identifier: NCT02705768) conducted on 60 patients of focal seizure. After recruitment, detailed history, clinical evaluations including Chalfont-National Hospital seizure severity scale (NHS3), Quality of Life in Epilepsy Inventory (QOLIE-31) and serum NSE estimation were done at baseline. Thirty healthy volunteers were recruited for a baseline evaluation of serum NSE. After randomization, one group received tablet oxcarbazepine and another group received tablet carbamazepine. At 4 weeks follow-up, all the parameter were reassessed. Serum NSE level was found to be significantly increased in patients with focal seizure in comparison to healthy volunteers. In both drug groups, serum NSE decreased significantly but the reduction in carbamazepine group (1.43; 95%CI: 0.18–2.67; p = 0.025) was significantly higher than oxcarbazepine group.NHS3 score, score in all seven domains of QOLIE-31 and final QOLIE-31 score improved significantly in both the groups. In conclusion, serum NSE increases in the patients with focal seizure within 48 h of a seizure episode. Therapy with carbamazepine and oxcarbazepine can decrease serum NSE level but the reduction is significantly higher with carbamazepine. Therapy with both the drugs can decrease the severity of epilepsy and improve the quality of life but adverse events were more with carbamazepine.
Measurement of enolase activity in cell lysates
2014, Methods in Enzymology
Citation Excerpt :
The tissues (0.1–0.3 g wet weight) are homogenized in 1 or 2 ml of 15 mM Tris–acetate (pH 6.5), 5 mM MgSO4, and 1 mM EDTA. The homogenate is centrifuged at 100,000 × g for 1 h at 4 °C, and the supernatant is used for the assay of enolase activity (Kato, Ishiguro, Suzuki, Ito, & Semba, 1982). Mammalian cells in culture are washed once with the buffer containing 250 mM sucrose, 20 mM HEPES (pH 7.5), 10 mM KCl, 1 mM MgCl2, 1 mM EGTA, 1 mM EDTA, 1 mM dithiothreitol, and 1 mM phenylmethanesulfonylfluoride and homogenized in 1 ml of the buffer.
Enolase (EC 4.2.1.11) is a cytosolic metalloenzyme responsible for the conversion of 2-phosphoglycerate into phosphoenolpyruvate, the second to last step in glycolysis. In mammals, enolase is encoded by three homologous genes. These gene products not only possess distinct biochemical and immunological properties but also show different tissue distribution. Besides its glycolytic function, α-enolase plays a variety of roles in pathophysiological settings including oncogenesis, tumor progression, ischemia, and bacterial infection. The expression levels of α-enolase have been attributed diagnostic and prognostic value in a number of tumors. Furthermore, neuron-specific α-enolase is released into the cerebrospinal fluid as well as in the systemic circulation upon traumatic brain injury and ischemic episodes. Thus, the measurement of the enzymatic activity of enolase is relevant for diverse fields of investigation, including oncometabolism. Here, we described simple and rapid protocols to measure the activity of enolase in lysates from mammalian cells and tissues.
Serum concentration of NSE and S-100b during LVAD in non-resuscitated patients
2008, Resuscitation
Citation Excerpt :
The distribution of NSE within the various human organs and tissues has been known for more than 20 years. The subtypes αγ- and the γγ-enolase are found in high concentrations in the central nervous system, in axons of the peripheral nerves, and in neuro-endocrine tumours; several other organs and blood cells show lower NSE concentrations.10,12,23,24. An association between haemolysis rate and an increase in NSE serum levels was first described by Pahlmann et al.8,9 In our study, we found a significant decrease in the platelet count and haemoglobin levels, suggesting a mechanical destruction of blood cells during LVAD support, as significant bleeding did not occur.
Increased serum concentrations of brain-derived proteins neuron-specific enolase (NSE) and protein S-100β (S-100b) are used as early predictors of long-term outcome in unconscious survivors after cardiopulmonary resuscitation (CPR). We investigated whether use of short-term Left Ventricular Assist Devices (LVAD) in patients undergoing percutaneous coronary intervention (PCI) effect serum concentrations of NSE and S-100b, because use of such devices in resuscitated cardiogenic shock patients increased during the last years.
We analysed data from 80 consecutive non-resuscitated patients who received LVAD support. 43 patients with uncomplicated myocardial infarction (AMI) without LVAD support after PCI formed the reference group.
69 patients (86%) with LVAD support survived and were discharged from hospital. We observed an increase in NSE serum levels in 93.6% and in S-100b serum levels in 58.6% of these patients during LVAD support. This increase was significant in comparison to the upper limit of normal (ULN) of both biomarkers and to the reference group. Cardiogenic shock patients showed significantly higher serum concentrations of both neuroproteins than patients after high-risk PCI, and after AMI during LVAD support. The use of axial flow pumps led to significantly higher serum concentrations of NSE compared to patients on IABP, but not of S-100b. Thrombocytes and haemoglobin (Hb) concentrations declined significantly during LVAD support. Surprisingly, we also observed a significant increase in NSE in the reference group.
LVAD support after PCI is associated with a significant increase in NSE serum concentration as well as in S-100b. We therefore postulate an overestimation of the extent of hypoxic brain damage in unconscious survivors after CPR if treatment include LVAD support or PCI or both procedures. The increase in NSE can be partly explained by alteration of thrombocytes and other blood cells. However, the increase in S-100b remains unexplained since S-100b does not occur in peripheral blood cells. An additional release of both biomarkers from ischemic myocardium or cerebral microembolism should be drawn into consideration.
Central Nervous System Tissue in Meat Products: An Evaluation of Risk, Prevention Strategies, and Testing Procedures
2007, Advances in Food and Nutrition Research
Citation Excerpt :
Finally, Lucker et al. (1998) evaluated immunochemical detection of NSE tissue by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) and Western blotting. NSE is a dimeric protein composed of three immunologically distinct subunits (γγ and αγ) which are present in CNS tissue in greater concentrations than in non‐CNS tissues (Kato et al., 1982). Results indicated that brain was detected at a 1% concentration using the Western blotting method in emulsion‐type sausages, and at a <4% concentration in liver‐type sausages.
Since the outbreak of bovine spongiform encephalopathy (BSE) in the United Kingdom in 1986 and its subsequent link to the human neurological disorder variant Creutzfeldt–Jakob disease (vCJD), presence of tissues from the central nervous system (CNS) in meat products has been considered a public health concern and, thus, has been banned from entering the human food chain in many countries. Despite this, potential can exist during harvesting to contaminate or cross‐contaminate edible meat products with CNS tissue that is designated as a specified risk material (SRM) in many countries. Methods used to detect CNS tissue in meat products vary greatly in their sensitivity, specificity, cost, labor and expertise needed, ease of completion, and type of results given (qualitative vs quantitative) and, within these constraints, appropriate testing methods must be selected to monitor or verify that meat products system controls are effective in removing CNS tissue from the human food chain. The extent to which monitoring procedures are needed should be based on the public health risk of CNS tissue in meat products as determined by each sovereign nation and/or third‐party international organizations such as the World Organization for Animal Health (OIE). Risk associated with consumption of CNS tissue should be estimated by sovereign nations by establishing prevalence of BSE within their borders. Using this information, science‐based decisions may guide international policy and trade. Using available scientific information, appropriate testing methods for monitoring or verification, and prevalence information, nations can estimate and reduce, to the extent deemed necessary, the public health risk of vCJD.
The increase of neuron-specific enolase in cerebrospinal fluid and plasma as a marker of neuronal damage in patients with acute brain infarction
2005, Journal of Clinical Neuroscience
Our goal was to determine the neuron-specific enolase (NSE) concentration in cerebrospinal fluid (CSF) and plasma in patients with the acute brain infarction (BI) and analyze the correlation between the measured NSE concentration and infarct volume and the degree of neurological and functional deficit. The study included 55 patients aged 56–68 with BI in the acute phase. The control group consisted of 16 patients subjected to diagnostic radiculography. The results showed a significant increase of NSE concentration within the first seven days in patients compared to the controls (2.838 ± 0.504 ng/ml CSF and 4.479 ± 0.893 ng/ml plasma). A significant correlation was found between NSE concentration and infarction volume and the degree of neurological and functional deficit both in the CSF (r = 0.828, r = 0.735, r = 0.796; p < 0.001) and in plasma (r = 0.810, r = 0.681, r = 0.783; p < 0.001). The results suggest that an early determination of this marker in CSF and plasma in patients with BI could be a valuable diagnostic factor.

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Distribution of nervous system-specific forms of enolase in peripheral tissues

Abstract

Anal. Biochem.

Biochim. Biophys. Acta

Arch. Biochem. Biophys.

Biochem. Biophys. Res. Commun.

Biochim. Biophys. Acta

Brain Research

Demonstration of enolase activity connected to the brain specific protein 14-3-2

Scand. J. Immunol.

The nature of the two proteins of brain specific antigens 14-3-2

J. Neurochem.