The Experts below are selected from a list of 114 Experts worldwide ranked by ideXlab platform
Robin Miskimins - One of the best experts on this subject based on the ideXlab platform.
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stage specific expression of Myelin Basic Protein in oligodendrocytes involves nkx2 2 mediated repression that is relieved by the sp1 transcription factor
Journal of Biological Chemistry, 2005Co-Authors: Keith W Miskimins, Robin MiskiminsAbstract:Abstract The homeodomain-containing Protein Nkx2.2 is critical for the development of oligodendrocyte lineage cells, but the target genes of Nkx2.2 regulation have not been identified. In the present study, we found that the Myelin Basic Protein gene is one of the genes that is regulated by Nkx2.2. Expression of Nkx2.2 represses the expression of Myelin Basic Protein in oligodendrocyte progenitors. Two regulatory elements in the Myelin Basic Protein promoter were identified and found to interact with Nkx2.2 in vitro. Despite their sequence divergence, both sites were involved in the Nkx2.2-mediated repression of the Myelin Basic Protein promoter. Binding of Nkx2.2 also blocked and disrupted the binding of the transcriptional activator Purα to the Myelin Basic Protein promoter. Additionally Nkx2.2 recruited a histone deacetylase 1-mSin3A complex to the Myelin Basic Protein promoter. We also found that the transcription factor Sp1 was able to compete off the binding of Nkx2.2 to its consensus binding site in vitro and reversed the repressive effect of Nkx2.2 in vivo. Our data revealed a novel role for Nkx2.2 in preventing the precocious expression of Myelin Basic Protein in immature oligodendrocytes. Based on this study and our previous reports, a model for Myelin Basic Protein gene control is proposed.
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Cloning and characterization of the rat Myelin Basic Protein gene promoter.
Gene, 2003Co-Authors: Qiou Wei, W. Keith Miskimins, Robin MiskiminsAbstract:Expression of Myelin Basic Protein in differentiating oligodendrocytes is mainly regulated at the transcriptional level. To better understand the regulation of Myelin Basic Protein gene expression in mammalian cells, we cloned and characterized the rat Myelin Basic Protein promoter by a genome walking technique. Extensive sequence homology has been found among mouse, rat and human MBP promoters. Alignment of the proximal core promoter of mouse and rat reveals highly conserved cis-elements that are important for regulating Myelin Basic Protein gene transcription. One major transcription start site along with two minor sites have been identified in both mouse and rat Myelin Basic Protein gene promoters using RNA ligase-mediated rapid amplification of 5' cDNA ends. The amplified rat Myelin Basic Protein promoter was cloned into a luciferase reporter construct. Transient transfection experiments show that both mouse and rat Myelin Basic Protein promoters yield increased expression when oligodendrocytes differentiate. The sequence and characterization of the rat MBP promoter provide a useful tool to investigate MBP gene regulation in mammalian cells.
Paolo Riccio - One of the best experts on this subject based on the ideXlab platform.
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Antibodies specific for the lipid-bound form of Myelin Basic Protein during experimental autoimmune encephalomyelitis
Journal of neuroimmunology, 1993Co-Authors: Francesco Lolli, Grazia Maria Liuzzi, Marco Vergelli, Luca Massacesi, Clara Ballerini, Luigi Amaducci, Paolo RiccioAbstract:On the hypothesis that Myelin Basic Protein isolated with surrounding lipids may constitute an autoantigen in deMyelinating diseases, we studied the antibody response to the lipid-free and lipid-bound form of Myelin Basic Protein during the course of experimental autoimmune encephalomyelitis induced in rats with either form of Protein. Immunization with the lipid-bound form of Myelin Basic Protein induced high titres of antibodies directed to the Protein, accompanied by no antibodies to cerebroside 30 days after immunization. Antibodies specifically directed to the lipid-bound form of Myelin Basic Protein were revealed after removal of antibodies recognizing the delipidated Myelin Basic Protein. Anti lipid-bound Myelin Basic Protein antibodies could already be detected at day 10 post-immunization, reaching a maximum at day 20 post-immunization. Demonstrations of antibodies entirely specific for the lipid-bound form of Myelin Basic Protein suggests that this molecule may present epitopes not to be found in its already extensively studied primary structure, possibly the result of conformational changes following lipid binding.
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On the spontaneous adherence of Myelin Basic Protein to T lymphocytes.
Biochemical and Biophysical Research Communications, 1991Co-Authors: A. Bobba, Irene Munno, B. Greco, Paolo Riccio, Emilio Jirillo, Ernesto QuagliarielloAbstract:Summary We have applied a double tagging system in order to study whether purified Myelin Basic Protein is able to adhere to normal human peripheral T lymphocytes without the need to purify cells. Evaluation of Myelin Basic Protein adherence to peripheral blood mononuclear cells was determined with biotinylated Myelin Basic Protein and fluoresceinated avidin, and lymphocyte population was identified by the corresponding phycoerythrinated monoclonal antibody. The observed adherence of Myelin Basic Protein to T lymphocytes was found to depend on Protein conformation.
Keith W Miskimins - One of the best experts on this subject based on the ideXlab platform.
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stage specific expression of Myelin Basic Protein in oligodendrocytes involves nkx2 2 mediated repression that is relieved by the sp1 transcription factor
Journal of Biological Chemistry, 2005Co-Authors: Keith W Miskimins, Robin MiskiminsAbstract:Abstract The homeodomain-containing Protein Nkx2.2 is critical for the development of oligodendrocyte lineage cells, but the target genes of Nkx2.2 regulation have not been identified. In the present study, we found that the Myelin Basic Protein gene is one of the genes that is regulated by Nkx2.2. Expression of Nkx2.2 represses the expression of Myelin Basic Protein in oligodendrocyte progenitors. Two regulatory elements in the Myelin Basic Protein promoter were identified and found to interact with Nkx2.2 in vitro. Despite their sequence divergence, both sites were involved in the Nkx2.2-mediated repression of the Myelin Basic Protein promoter. Binding of Nkx2.2 also blocked and disrupted the binding of the transcriptional activator Purα to the Myelin Basic Protein promoter. Additionally Nkx2.2 recruited a histone deacetylase 1-mSin3A complex to the Myelin Basic Protein promoter. We also found that the transcription factor Sp1 was able to compete off the binding of Nkx2.2 to its consensus binding site in vitro and reversed the repressive effect of Nkx2.2 in vivo. Our data revealed a novel role for Nkx2.2 in preventing the precocious expression of Myelin Basic Protein in immature oligodendrocytes. Based on this study and our previous reports, a model for Myelin Basic Protein gene control is proposed.
Marcello Brunelli - One of the best experts on this subject based on the ideXlab platform.
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Modulation of Myelin Basic Protein Gene Expression by Acetyl-l-Carnitine
Molecular Neurobiology, 2011Co-Authors: Giovanna Traina, Giuseppe Federighi, Monica Macchi, Rodolfo Bernardi, Mauro Durante, Marcello BrunelliAbstract:Acetyl- l -carnitine (ALC), the acetyl ester of l -carnitine, is a naturally occurring molecule which plays an essential role in intermediary and mitochondrial metabolism. It has also neurotrophic and antioxidant actions, demonstrating efficacy and high tolerability in the treatment of neuropathies of various etiologies. ALC is a molecule of considerable interest for its clinical application in various neural disorders, although little is known regarding its effects on gene expression. Suppression subtractive hybridization methodology was used for the generation of subtracted complementary DNA libraries and the subsequent identification of differentially expressed transcripts in the rat brain after chronic ALC treatments. We provided evidence for a downregulation of the expression of all of the isoforms of Myelin Basic Protein gene following prolonged ALC treatment, indicating a possible role in the modulation of Myelin Basic Protein turnover, stabilizing and maintaining Myelin integrity.
Joseph J Volpe - One of the best experts on this subject based on the ideXlab platform.
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mature Myelin Basic Protein expressing oligodendrocytes are insensitive to kainate toxicity
Journal of Neuroscience Research, 2003Co-Authors: Paul A Rosenberg, Weimin Dai, Xiao Dong Gan, Sanjida Ali, Stephen A Back, Russell M Sanchez, Michael M Segal, Pamela L Follett, Frances E Jensen, Joseph J VolpeAbstract:We examined the vulnerability to excitotoxicity of rat oligodendrocytes in dissociated cell culture at different developmental stages. Mature oligodendrocytes that express Myelin Basic Protein were resistant to excitotoxic injury produced by kainate, whereas earlier stages in the oligodendrocyte lineage were vulnerable to this insult. To test the hypothesis that the sensitivity of immature oligodendrocytes and the resistance of mature oligodendrocytes to kainate toxicity were due to differences in membrane responsiveness to kainate, we used whole-cell patch-clamp recording. Oligodendrocyte precursors in cultures vulnerable to kainate toxicity responded to 500 μM kainate with large inward currents, whereas mature Myelin Basic Protein-expressing oligodendrocytes in cultures resistant to kainate toxicity showed no clear response to application of this agonist. We assayed expression of glutamate receptor subunits (GluR) -2, -4, -6, -7, and KA2 using immunoblot analysis and found that expression of all of these glutamate receptors was significantly down-regulated in mature oligodendrocytes. These results suggest a striking developmental regulation of glutamate receptors in oligodendrocytes and suggest that the vulnerability of oligodendrocytes to non- N-methyl-D-aspartate receptor-mediated excitotoxicity might be much greater in developing oligodendrocytes than after the completion of Myelination. © 2002 Wiley-Liss, Inc.
