Search results for "enolase"

A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Act…

2009

Cytosine-5 methyltransferases of the Dnmt2 family function as DNA and tRNA methyltransferases. Insight into the role and biological significance of Dnmt2 is greatly hampered by a lack of knowledge about its protein interactions. In this report, we address the subject of protein interaction by identifying enolase through a yeast two-hybrid screen as a Dnmt2-binding protein. Enolase, which is known to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), was shown to have both a cytoplasmatic and a nuclear localization in the parasite Entamoeba histolytica. We discovered that enolase acts as a Dnmt2 inhibitor. This unexpected inhibitory activity was antagonized by…

Influence of temperature on the calibration curves in IRMA for neuron specific enolase and its physicochemical interpretation

2009

Abstract Background immunoradiometric assay (IRMA) is one of the principal methods used for the analytical determination of neuron specific enolase (NSE) concentration. We studied the influence of temperature on the calibration curves obtained by this method, and a physicochemical justification based on two theoretical models is proposed. Material and methods we used a commercially available RIA kit for NSE and a gamma counter. Data was analysed using Statistical software. Results and discussion activity bound to the antibody increases with temperature, producing results that are consistent with two modifications to the four parameter and Langmuir equations. Conclusions the two models used …

Role of Enolase/MBP-1 in non-tumorigenic and cancer cells

The glycolytic enzyme α-enolase is a highly conserved protein involved in multiple functions (Díaz-Ramos A et al 2012). Besides the mainly cytoplasmic localization, the protein has been detected on the surface of prokaryotic and eukaryotic cells where it functions as a plasminogen receptor, while a shorter variant, called Myc promoter-binding protein-1 (MBP-1), is mainly located in the nucleus. Several lines of evidence indicate that MBP-1 acts as a tumor suppressor, negatively regulating cell proliferation or promoting apoptosis of cancer cells. Although a few reports indicate that stressful conditions, such as glucose deprivation or hypoxia, may modulate MBP-1 expression in mammalian cell…

Identification of enolase as a plasminogen-binding protein in excretory-secretory products ofFasciola hepatica

2004

AbstractWe have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host–parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an apparent molecular weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.

Enzyme Promiscuity in Enolase Superfamily. Theoretical Study of o-Succinylbenzoate Synthase Using QM/MM Methods

2015

The promiscuous activity of the enzyme o-succinylbenzoate synthase (OSBS) from the actinobacteria Amycolatopsis is investigated by means of QM/MM methods, using both density functional theory and semiempirical Hamiltonians. This enzyme catalyzes not only the dehydration of 2-succinyl-6R-hydroxy-2,4-cyclohexadiene-1R-carboxylate but also catalyzes racemization of different acylamino acids, with N-succinyl-R-phenylglycine being the best substrate. We investigated the molecular mechanisms for both reactions exploring the potential energy surface. Then, molecular dynamics simulations were performed to obtain the free energy profiles and the averaged interaction energies of enzymatic residues wi…

From molecular analysis to histopathology: alpha-enolase/MBP1 isoforms expression in breast cancer

2008

MULTIOMIC ANALYSIS OF TRANSCRIPTIONAL REPRESSOR MBP-1 FUNCTIONS IN GYNECOLOGICAL TUMORS

2014

The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control

2007

Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, a…

Natural bioactive molecules induce a reduction of surface alpha-enolase in breast cancer cells

Cell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to cancer cell invasion and metastasis formation. Although the functional role of surface alpha-enolase in cancer spreading has been clearly linked to the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation, the cellular pathways underlying cell surface transport remain largely elusive. We have previously demonstrated that pro-invasive stimuli promote the surface expression of alpha-enolase in breast cancer cells. To further investigate alpha-enolase translocation to the plasma membrane and to identify the signaling involved in this…

Identification and characterization of autoantibodies against catalase and α-enolase in patients with primary sclerosing cholangitis

1998

SUMMARY Primary sclerosing cholangitis (PSC) is a chronic cholestatic liver disease of unknown aetiology. Recent studies have shown that genetic factors and both cellular and humoral immunological abnormalities are important in the pathogenesis of PSC. The most prominent autoantibodies in PSC are anti-neutrophil cytoplasmic antibodies (ANCA). The autoepitopes of ANCA in PSC are not well defined. The aim of this study was to identify corresponding ANCA autoantigens in patients with PSC. A biochemical approach with enrichment and partial purification of soluble neutrophil proteins, detection of autoantibodies by Western blot and partial amino acid sequencing were used. Two new autoantigen/aut…