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PubMed1991

Mutations within the Ddc promoter alter its neuron-specific pattern of expression.

The Drosophila dopa decarboxylase gene (Ddc) is expressed in a reproducible set of approximately 150 neurons, and in a subset of the glia of the third instar larva's central nervous system (CNS). Expression in this pattern requires a cell type-specific neuronal enhancer/glial repressor region located 1000 bp from the transcriptional start site, and specific sequences within the promoter. We have used mutagenesis in vitro and P-element-mediated transformation to examine the role of the promoter, particularly its major CNS activator sequence (element I), in the generation of the wildtype expression pattern. Immunohistological analysis of these transgenic strains demonstrates that particular deletion mutations shift the site of transgene expression to a set of neurons which do not express Ddc at detectable levels in wild-type larvae. Transgene expression in these strains may be driven by a previously undetected activator sequence. Our data also suggest that glial expression may be driven by the same activator sequences that drive expression in the hypoderm.

Animals↗

PubMed1994

Serum neurone-specific enolase concentrations in patients with neurological disorders.

A radioimmunoassay (RIA) has been developed for neurone-specific enolase (NSE) and used to measure serum levels in patients with a range of neurological disorders. Serum NSE levels were within the normal range in 21 patients with multiple sclerosis and 4 patients with Guillain-Barre syndrome. Normal serum NSE levels were also recorded in patients with motor neurone disease, anterior spinal thrombosis, multi-infarct disease, benign intracranial hypertension and peripheral neuropathy. However, two patients in coma, one as a result of encephalitis, the other due to subarachnoid haemorrhage (SAH) had elevated serum NSE. In the former, serum NSE levels appeared to predict a deterioration in clinical state, levels later returning to normal before an improvement in clinical condition. In the patient with SAH, levels were elevated on admission and remained elevated until death. Serum NSE levels may be of use in predicting outcome in patients with acute neurological disease.

Adolescent↗

PubMed1989

Structure of the gene encoding peripherin, an NGF-regulated neuronal-specific type III intermediate filament protein.

We have cloned the rat gene encoding peripherin, a neuronal-specific intermediate filament protein that is NGF-regulated. Determination of the complete sequence, including 821 nucleotides of the 5'-flanking region, allows us to make conclusions about the evolutionary origin of the peripherin gene, its homology with other intermediate filament proteins, and possible mechanisms of regulation of peripherin expression in neurons. The positions of the eight peripherin gene introns correspond to the intron patterns of desmin, vimentin, and GFAP, with one example of intron sliding. Together with protein sequence homologies, this conclusively demonstrates that peripherin is a type III intermediate filament protein. The peripherin promoter contains sequences homologous to regions of other NGF-regulated promoters, which may function in peripherin induction by NGF.

Amino Acid Sequence↗

PubMed1984

Neuron specific enolase: a marker for the early development of nerves and endocrine cells in the human lung.

Neuron specific enolase (NSE), an isoenzyme of the glycolytic enzyme enolase, has been established by immunocytochemical means as a marker of morphological and functional maturation in central neurons and appears late in development. However, little is known about the presence of NSE in developing peripheral neurons and endocrine cells and its relationship to the development of classical neurotransmitters and peptides. We therefore investigated the appearance of NSE immunoreactivity in nerves and mucosal endocrine cells of the human respiratory tract in foetal, neonatal and adult life. NSE was found to be present in neuroblasts, nerve fibres and endocrine cells from the earliest period of gestation examined (8 weeks), before the appearance of acetylcholinesterase activity (10-12 weeks), dopamine-beta-hydroxylase (20 weeks), vasoactive intestinal polypeptide (20 weeks) or calcitonin (20 weeks). Bombesin-like immunoreactivity was found in a small proportion of mucosal endocrine cells as early as eight weeks in the foetal respiratory tract. These findings indicate that unlike central neurons and their processes, peripheral neurons of the lung contain NSE immunoreactivity well before full maturation and establishment of synaptic contact with end organs.

Endocrine Glands↗

PubMed1995

Expression of neuron-specific enolase in the pineal organ of the domestic fowl during post-hatching development.

Immunohistochemistry for neuron-specific enolase (NSE) revealed that NSE is localized in both a limited number of pinealocytes and intrinsic afferent neurons in the pineal organ of the domestic fowl. Furthermore, a computer-assisted three-dimensional imaging technique allowed to clarify the reverse distributional pattern of both elements: NSE-positive pinealocytes displayed a dense distribution especially in the vesicular portion of the gland, whereas NSE-immunoreactive nerve cells were mainly found in the pineal stalk. The number of NSE-positive intrinsic neurons in the pineal organ of chickens decreased rapidly after hatching, with a concentration of these elements in the basal portion (stalk) of the pineal organ. On the other hand, immunoreactive pinealocytes increased remarkably in the end-vesicle of the organ with age, followed by a gradual expansion toward the proximal portion. Thus, the spectacular increase in NSE-positive pinealocytes and the progressive reduction of reactive neurons occurred in parallel during the course of post-hatching development. NSE-immunoreactive pinealocytes displayed morphological characteristics of bipolar elements, endowed with an apical protrusion into the pineal lumen and a short basal process at younger stages, whereas multipolar types of NSE-positive pinealocytes were predominantly found in the adult domestic fowl. These results indicate that in the pineal organ of the domestic fowl (1) the ontogenetic expansion of NSE-immunoreactive pinealocytes is paralleled by a regressive afferent innervation, (2) the NSE-positive pinealocytes transform from a bipolar (columnar) type to a multipolar type during post-hatching development, and (3) these ontogenetic changes in the NSE-immunoreactivity and morphology of pinealocytes may reflect the development of a neurosecretory-like capacity of the organ.

Animals↗

PubMed1999

Visinin-like protein (VILIP) is a neuron-specific calcium-dependent double-stranded RNA-binding protein.

Double-stranded RNA-binding proteins function in regulating the stability, translation, and localization of specific mRNAs. In this study, we have demonstrated that the neuron-specific, calcium-binding protein, visinin-like protein (VILIP) contains one double-stranded RNA-binding domain, a protein motif conserved among many double-stranded RNA-binding proteins. We showed that VILIP can specifically bind double-stranded RNA, and this interaction specifically requires the presence of calcium. Mobility shift studies indicated that VILIP binds double-stranded RNA as a single protein-RNA complex with an apparent equilibrium dissociation constant of 9.0 x 10(-6) M. To our knowledge, VILIP is the first double-stranded RNA-binding protein shown to be calcium-dependent. Furthermore, VILIP specifically binds the 3'-untranslated region of the neurotrophin receptor, trkB, an mRNA localized to hippocampal dendrites in an activity-dependent manner. Given that VILIP is also expressed in the hippocampus, these data suggest that VILIP may employ a novel, calcium-dependent mechanism to regulate its binding to important localized mRNAs in the central nervous system.

3' Untranslated Regions↗

PubMed1981

Brain levels of neuron-specific and nonneuronal enolase in Huntington's disease.

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. Neuron-specific enolase (NSE) levels are decreased an average of 45% in basal ganglia from patients with Huntington's disease whereas the glial-specific form of enolase, nonneuronal enolase (NNE), is not significantly altered. 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. NNE and NSE levels appear to be specific biochemical indicators of glial and neuronal cell number and viability. Levels of these cell-specific isoenzymes may therefore prove useful in quantitating neuropathological changes in various neurological disorders.

Basal Ganglia↗

PubMed1992

A simple enzyme-linked immunosorbent assay (ELISA) for the neuron-specific gamma isozyme of human enolase (NSE) using monoclonal antibodies raised against synthetic peptides corresponding to isozyme sequence differences.

Monoclonal antibodies specific for the gamma isozyme of human enolase (known as neuron-specific enolase or NSE) have been raised against synthetic peptides after coupling to carrier protein: the selected peptides were those corresponding to regions of amino acid sequence difference between the alpha and gamma subunits of these closely similar isozymes. This technique gave monoclonal antibodies of high specificity and affinity. Two monoclonal antibodies raised against different peptides were used to develop a double-antibody sandwich enzyme-linked immunosorbent assay (ELISA), using one as the solid-phase antibody and the other conjugated to horseradish peroxidase to detect the bound NSE. This assay provides a simple and routine method of detecting NSE in serum samples from patients with small-cell carcinoma of the lung and related tumours.

Amino Acid Sequence↗

PubMed1994

Human taste cells express the G protein alpha-gustducin and neuron-specific enolase.

Expression of the alpha-subunit of the taste-specific G protein alpha-gustducin and the glycolytic enzyme neuron-specific enolase (NSE) was investigated immunohistochemically in human circumvallate and foliate taste papillae. Immunofluorescence for alpha-gustducin was observed in taste cells of both types of papillae and exhibited two patterns of immunofluorescence, plasmalemmal and cytosolic. The plasmalemmal pattern showed intense immunofluorescence localized to the apical region, and was exhibited by most immunoreactive taste cells. In contrast, the cytosolic pattern, observed in one or two immunoreactive cells in a taste bud per section, showed immunofluorescence distributed throughout the cytoplasm. A subpopulation of alpha-gustducin-immunoreactive taste receptor cells, most of which exhibited the cytosolic pattern, also expressed NSE. Optical sectioning, using confocal laser scanning microscopy, demonstrated the highest level of expression of alpha-gustducin in the apical microvillar region of the taste cells in close apposition to the taste pore. These studies indicate conservation of epitopes of alpha-gustducin in humans and rats, and suggest that this G protein is associated with taste transduction in both rats and humans. The patterns of expression of alpha-gustducin, and coexpression with NSE, may correlate with specialized subtypes or developmental stages of taste receptor cells.

Aged↗

PubMed1989

Synapsin I, a neuron-specific phosphoprotein interacting with small synaptic vesicles and F-actin.

Synapsin I is a neuron-specific phosphoprotein which is a substrate for cAMP- and Ca2+/calmodulin-dependent protein kinases. It is specifically localized to the cytoplasmic side of small synaptic vesicles. The interaction of synapsin I with the synaptic vesicle membrane is complex in nature, since it is modulated by phosphorylation and involves binding of different domains of the molecule to phospholipid and protein components of synaptic vesicles. Synapsin I is also able to interact with actin filaments in a phosphorylation-dependent manner. Because of these properties, it has been hypothesized that synapsin I acts as a dynamic link between synaptic vesicles an the actin meshwork of the nerve terminal, thereby modulating the release of neurotransmitter.

Actins↗

PubMed2004

Modulation of the stathmin-like microtubule destabilizing activity of RB3, a neuron-specific member of the SCG10 family, by its N-terminal domain.

RB3 is a neuron-specific homologue of the SCG10/stathmin family proteins, possessing a unique N-terminal membrane-associated domain and the stathmin-like domain at the C terminus, which promotes microtubule (MT) catastrophe and/or tubulin sequestering. We examined herein the contribution of the N-terminal subdomain of RB3 to the regulation of MT dynamics. To begin with, we determined the effects of full-length (RB3-f) and short truncated (RB3-s) forms of RB3 on the polymerization of MT in vitro. RB3-s had a deletion of amino acids 1-75 from the N terminus, leaving the so-called stathmin-like domain, consisting of residues 76-217. Although both RB3-f and RB3-s exhibited MT-depolymerizing activity, RB3-f was less effective. The binding affinity for tubulin was also lower in RB3-f. Direct observation of the dynamics of individual MTs using dark field microscopy revealed that RB3-s slowed MT elongation velocity, increased catastrophes, and reduced rescues. This effect is almost identical to that by stathmin/oncoprotein 18. On the other hand, the MT elongation rate increased at lower concentrations of RB3-f. In addition, RB3-f, indicated higher rescue frequency than control as well as the catastrophe in a dose-dependent manner. The functionality of RB3-f indicated that full-length RB3 has not only stathmin-like MT destabilizing activity but also MT-associated protein-like MT stabilizing activity. Possibly, the balance of these activities is altered in a concentration-dependent manner in vitro. This interesting regulatory role of the unique N-terminal domain of RB3 in MT dynamics would contribute to the physiological regulation of neuronal morphogenesis.

Animals↗

PubMed1993

Immunohistochemical localization of a neuron-specific beta-tubulin isotype in the developing chicken ultimobranchial glands.

The localization of a neuron-specific beta-tubulin isotype in the ultimobranchial glands from chickens at various stages of development was studied by means of light- and electron microscopic immunohistochemistry with a monoclonal antibody (TuJ1) against the beta-tubulin isotype, c beta 4. At 8 days of incubation, many C cells in the ultimobranchial glands showed immunoreactivity for TuJ1 invariable degrees, weak to intense. At 12 days of incubation, a vast majority of C cells were intensely immunoreactive for TuJ1, and further TuJ1-immunoreactive nerve fibers were distributed in the ultimobranchial glands. At 14 and 16 days of incubation, intense immunoreactivity for TuJ1 was sustained in the C cells. Electron microscopic analyses revealed that TuJ1 immunoreactivity was diffusely distributed throughout the cytoplasm and also localized on the secretory granules of C cells at these stages. TuJ1 immunoreactivity in the C cells started to decrease at late stages of embryonic development. At the hatching period, dense distributions of TuJ1-immunoreactive nerve fibers were observed in the ultimobranchial glands, whereas TuJ1 immunoreactivity of the C cells became very weak. In 10-day-old chickens, TuJ1 immunoreactivity was restricted to the nerve fibers.

Animals↗

PubMed2002

Diagnostic value of tumor markers Cyfra 21-1 and neuron-specific enolase in analysis of pleural fluid.

The diagnostic value of tumor markers Cyfra 21-1 and neuron-specific enolase in blood serum and pleural fluid in differential diagnosis of pleural exudation in cancer patients and patients with nontumor pleurisy was evaluated. The most pronounced changes were characteristic of Cyfra 21-1. In patients with pleurisy caused by malignant tumors the degree and incidence of increased Cyfra 21-1 concentrations in the serum and pleural fluid were higher than in patients with pleural exudation of nontumor origin. These data attest to high diagnostic sensitivity and specificity of Cyfra 21-1. Complex measurements of the marker in the serum and pleural fluid will improve diagnosis of pleural exudation of tumorous etiology.

Adult↗

PubMedDate not supplied

Detection of paraneoplastic anti-neuronal-specific antibodies: comparison of different immunohistochemical techniques.

Different immunohistochemical techniques have been employed to identify the anti-neuronal antibodies in patients with paraneoplastic neurological syndromes. The finding of anti-neuronal-specific autoantibodies in serum or cerebrospinal fluid well correlates with particular types of tumors, thus leading, in many cases, to an early cancer identification. In this work, we have compared three immunohistochemical methods (immunofluorescence, indirect immunoperoxidase and avidin-biotin immunoperoxidase) on frozen and paraffin-embedded sections of rat cerebellum in order to set up a reliable and simple technique for the diagnosis of these syndromes. Our study demonstrates that the best result was obtained by using frozen sections of rat cerebellum and the avidin-biotin immunoperoxidase method that also allowed the identification of anti-GAD antibodies not detected in paraffin-embedded tissues.

Animals↗

PubMedDate not supplied

Neuron-specific enolase and S-100 protein levels in cerebrospinal fluid of patients with various neurological diseases.

Neuron-specific enolase (NSE) and S-100 protein (S-100) levels in cerebrospinal fluid (CSF) were determined in 129 patients with various neurological diseases. The chronological changes of these nervous system-specific proteins in CSF were also examined in 3 patients with acute disorders. NSE and S-100 levels were elevated in many cases with acute conditions. These specific proteins did not increase simultaneously but independently. These results suggested that NSE and S-100 in CSF would be useful markers for damage of the nervous system and that measurement of both NSE and S-100 might positively indicate whether the damage was neuronal, glial or mixed in origin. Moreover, from the serial determination of these substances, they would be better markers than cell counts and total protein in CSF for the active injury for the nervous tissues.

Adult↗

PubMed1987

Neuron-specific enolase in medullary thyroid carcinoma: immunohistochemical demonstration, but no significance as serum tumor marker.

Neuron-specific enolase (NSE) is an enzyme detectable in nervous and neuroendocrine tissue. Increased serum levels of NSE are found in small cell lung cancer and in patients with neuroblastoma, in whom NSE is used as a serum tumor marker. We have investigated 32 patients with histologically proven medullary thyroid carcinoma, a tumor of neuroendocrine origin, in which the classical tumor marker calcitonin (CT) was pathologically elevated. Positive immunocytochemistry for NSE and CT in C-cells was obtained in all cases. Increased serum NSE levels were found in only 5 of 32 patients, there was no correlation between NSE and CT concentrations. We also compared NSE and CT serum levels during long-term follow-up and again found no correlation between NSE and CT. After i.v. stimulation tests with pentagastrin and calcium, no correlation was found between NSE and CT serum levels. We conclude, therefore, that in medullary thyroid carcinoma NSE is useful for immunocytochemistry but not a reliable serum tumor marker.

Calcitonin↗

PubMed1988

An enzyme antigen immunoassay for the determination of neuron-specific enolase in serum samples.

A method is presented for the detection and quantification of neuron-specific enolase (NSE) in serum samples. It is an enzyme antigen immunoassay (EAIA), relying on specific antibodies to 'catch' the enzyme on a solid support (ELISA-plate) whereafter the enzymatic activity of the immunocaptured enzyme is determined, by coupling the reaction to lactate dehydrogenase. The oxidation of NADH to NAD is followed at 340 nm in an ELISA photometer. The method is proven to work well and is able to measure the low amounts of NSE present in serum samples from normal individuals. It does not require labelling of neither antigen nor antibody, and is therefore superior to the commercially available radioimmunoassay (RIA). The method will also work with monoclonal antibodies towards the enzyme as demonstrated by preliminary observations.

Animals↗

PubMed1992

Serum neurone-specific enolase levels in patients with neuroendocrine and carcinoid tumours.

We have examined concentrations of neurone-specific enolase (NSE) in sera from 18 patients with various neuroendocrine tumours, 26 patients with carcinoid tumours, 21 patients with non-neuroendocrine tumours and 37 control individuals. No statistically significant difference between the concentrations in patients with neuroendocrine tumours and patients with carcinoid tumours was found. However the NSE concentrations in patients with carcinoid and neuroendocrine tumours, when these two groups were combined, were significantly different from the patients with non-neuroendocrine tumours or the control individuals (P < or = 0.01). 38.5% of the patients with carcinoid tumours had raised NSE concentrations in serum; 55.5% of those with non carcinoid neuroendocrine tumours had raised concentrations. There appeared to be no correlation between the NSE concentrations and the extent of metastases.

Adult↗