scholarly journals Gamma-Enolase

2020 ◽  
Author(s):  
Keyword(s):  
Gamma Enolase

scholarly journals Proteomic Analysis of Hippocampus and Cortex in Streptozotocin-Induced Diabetic Model Mice Showing Dementia

2018 ◽  
Vol 2018 ◽  
pp. 1-11 ◽  
Author(s):  
Kenji Matsuura ◽  
Mieko Otani ◽  
Masaoki Takano ◽  
Keiichi Kadoyama ◽  
Shogo Matsuyama
Keyword(s):  
Calcium Ion ◽  
Proteomic Analysis ◽  
Neurotransmitter Release ◽  
Ion Binding ◽  
Two Dimensional Gel Electrophoresis ◽  
Iron Storage ◽  
Diabetic Model ◽  
The Central Nervous System ◽  
Gtpase Activation ◽  
Gamma Enolase

Aim. Diabetes with its associated hyperglycemia induces various type of peripheral damage and also impairs the central nervous system (CNS). This study is aimed at clarifying the precise mechanism of diabetes-induced dementia as an impairment of CNS. Methods. The proteomic analysis of the hippocampus and cortex in streptozotocin- (STZ-) treated mouse diabetic model showing dementia was performed using two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (n=3/group). Results. Significant changes in the expression of 32 proteins and 7 phosphoproteins were observed in the hippocampus and cortex. These identified proteins and phosphoproteins could be functionally classified as cytoskeletal protein, oxidoreductase, protein deubiquitination, energy metabolism, GTPase activation, heme binding, hydrolase, iron storage, neurotransmitter release, protease inhibitor, transcription, glycolysis, antiapoptosis, calcium ion binding, heme metabolic process, protein degradation, vesicular transport, and unknown in the hippocampus or cortex. Additionally, Western blotting validated the changes in translationally controlled tumor protein, ATP-specific succinyl-CoA synthetase beta subunit, and gamma-enolase isoform 1. Conclusions. These findings showed that STZ-induced diabetes changed the expression of proteins and phosphoproteins in the hippocampus and cortex. We propose that alterations in expression levels of these proteins play an important role in diabetes-induced dementia.

Hippocampal levels of gamma-enolase, C-1-tetrahydrofolate synthase and serotransferrin fluctuate over the estrous cycle in the rat

Neuroscience ◽  
2008 ◽  
Vol 154 (3) ◽  
pp. 1009-1020 ◽  
Author(s):  
W.-F. Diao ◽  
L. Afjehi-Sadat ◽  
W.-Q. Chen ◽  
J. Höger ◽  
H. Höger ◽  
...  
Keyword(s):  
Estrous Cycle ◽  
Tetrahydrofolate Synthase ◽  
Gamma Enolase

Developmental Expression of Alpha- and Gamma-Enolase Subunits and mRNA Sequences in the Mouse Brain

1988 ◽  
Vol 10 (2) ◽  
pp. 91-98 ◽  
Author(s):  
M. Lucas ◽  
N. Lamande ◽  
M. Lazar ◽  
F. Gros ◽  
L. Legault-Demare
Keyword(s):  
Mouse Brain ◽  
Developmental Expression ◽  
Gamma Enolase

Immunoradiometric assay for alpha gamma- and gamma gamma-enolase (neuron-specific enolase), with use of monoclonal antibodies and magnetizable polymer particles.

1989 ◽  
Vol 35 (10) ◽  
pp. 2034-2038 ◽  
Author(s):  
E Paus ◽  
K Nustad
Keyword(s):  
Monoclonal Antibodies ◽  
Lung Carcinoma ◽  
Solid Phase ◽  
Small Cell Lung Carcinoma ◽  
Neuron Specific Enolase ◽  
Small Cell ◽  
Immunoradiometric Assay ◽  
Small Cell Lung ◽  
Cell Lung Carcinoma ◽  
Gamma Enolase

Abstract Monoclonal antibodies were raised against neuron-specific enolase, gamma gamma-enolase, and used in an immunoradiometric assay (IRMA), with mono-disperse magnetizable particles as the solid phase. The assay's sensitivity was 0.4 microgram/L and the interassay coefficient of variation was less than 5% in the working range from 0.4 to 170 micrograms/L. Compared with our radioimmunoassay based on polyclonal antibodies, the incubation time is shorter, and precision and sensitivity are improved. The IRMA also improved detection of neuron-specific enolase in sera from patients with lung cancer without a concomitant change in measured enolase in the reference population. The better sensitivity of the IRMA results from its ability to measure alpha gamma- and gamma gamma-enolase with equal response. Ninety percent of the small-cell lung carcinoma patients (36 of 40) had increased values before treatment, compared with 7% of non-small-cell lung carcinoma patients (8 of 114).

Cloning, expression and sequence homologies of cDNA for human gamma enolase

Gene ◽  
1989 ◽  
Vol 79 (2) ◽  
pp. 355-360 ◽  
Author(s):  
Daniele Oliva ◽  
Giovanna Barba ◽  
Giovanna Barbieri ◽  
Agata Giallongo ◽  
Salvatore Feo
Keyword(s):  
Sequence Homologies ◽  
Gamma Enolase

Coexpression of alpha and gamma enolase genes in neurons of adult rat brain

1994 ◽  
Vol 38 (5) ◽  
pp. 493-504 ◽  
Author(s):  
A. Keller ◽  
A. Bérod ◽  
M. Dussaillant ◽  
N. Lamandé ◽  
F. Gros ◽  
...  
Keyword(s):  
Rat Brain ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Gamma Enolase

Gamma enolase expression as early marker of neuronal differentiation of murine neuroblastoma cells N-115

1993 ◽  
Vol 11 (S1) ◽  
pp. S167-S169
Author(s):  
M. Cervello ◽  
A. Giallongo ◽  
L. D'Amelio ◽  
S. Sciarrino ◽  
V. Matranga
Keyword(s):  
Neuronal Differentiation ◽  
Neuroblastoma Cells ◽  
Murine Neuroblastoma ◽  
Early Marker ◽  
Gamma Enolase

scholarly journals Molecular evolution of enolase.

2005 ◽  
Vol 52 (2) ◽  
pp. 507-513 ◽  
Author(s):  
Michał Piast ◽  
Irena Kustrzeba-Wójcicka ◽  
Małgorzata Matusiewicz ◽  
Teresa Banaś
Keyword(s):  
Amino Acid ◽  
Molecular Evolution ◽  
Functional Diversity ◽  
Phylogenetic Trees ◽  
Amino Acid Sequences ◽  
Evolutionary Relationships ◽  
Sort Intolerant From Tolerant ◽  
Alpha Beta ◽  
Gamma Enolase ◽  
Program Show

Enolase (EC 4.2.1.11) is an enzyme of the glycolytic pathway catalyzing the dehydratation reaction of 2-phosphoglycerate. In vertebrates the enzyme exists in three isoforms: alpha, beta and gamma. The amino-acid and nucleotide sequences deposited in the GenBank and SwissProt databases were subjected to analysis using the following bioinformatic programs: ClustalX, GeneDoc, MEGA2 and S.I.F.T. (sort intolerant from tolerant). Phylogenetic trees of enolases created with the use of the MEGA2 program show evolutionary relationships and functional diversity of the three isoforms of enolase in vertebrates. On the basis of calculations and the phylogenetic trees it can be concluded that vertebrate enolase has evolved according to the "birth and death" model of evolution. An analysis of amino acid sequences of enolases: non-neuronal (NNE), neuron specific (NSE) and muscle specific (MSE) using the S.I.F.T. program indicated non-uniform number of possible substitutions. Tolerated substitutions occur most frequently in alpha-enolase, while the lowest number of substitutions has accumulated in gamma-enolase, which may suggest that it is the most recently evolved isoenzyme of enolase in vertebrates.

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