Basic Protein - Explore the Science & Experts | ideXlab

Scan Science and Technology

Contact Leading Edge Experts & Companies

Basic Protein

The Experts below are selected from a list of 153 Experts worldwide ranked by ideXlab platform

Joan M Boggs – One of the best experts on this subject based on the ideXlab platform.

  • Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin Basic Protein.
    Biochemistry, 2010
    Co-Authors: Lopamudra Homchaudhuri, George Harauz, Miguel De Avila, Stina B. Nilsson, Kyrylo Bessonov, Graham S.t. Smith, Vladimir V. Bamm, Abdiwahab A. Musse, Joan M Boggs

    Abstract:

    Myelin Basic Protein (MBP), specifically the 18.5 kDa isoform, is a peripheral membrane Protein and a major component of mammalian central nervous system myelin. It is an intrinsically disordered a…

  • structural polymorphism and multifunctionality of myelin Basic Protein
    Biochemistry, 2009
    Co-Authors: George Harauz, Vladimir Ladizhansky, Joan M Boggs

    Abstract:

    Central nervous system myelin is a dynamic entity arising from membrane processes extended from oligodendrocytes, which form a tightly wrapped multilamellar structure around neurons enabling rapid and efficient signal propagation. The gene of oligodendrocyte lineage (golli) gives rise to a variety of developmentally regulated splice isoforms of myelin Basic Protein (MBP), denoted golli for early forms and classic for later ones. In mature myelin, the predominant splice isoform of classic MBP is 18.5 kDa; its central role is to maintain the structural integrity of the myelin sheath, by holding together the apposing cytoplasmic leaflets of the oligodendrocyte membrane in a tight, spiral, multilamellar arrangement. This Protein’s extreme physicochemical properties, net charge of +19 at neutral pH, low proportion of hydrophobic residues, alternating regions of predicted intrinsic disorder and order, induced folding upon association with membranes and other Proteins, and diversification via combinatorial post-…

  • myelin Basic Protein a multifunctional Protein
    Cellular and Molecular Life Sciences, 2006
    Co-Authors: Joan M Boggs

    Abstract:

    Myelin Basic Protein (MBP), the second most abundant Protein in central nervous system myelin, is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. A member of the ‘intrinsically disordered’ or conformationally adaptable Protein family, it also appears to have several other functions. It can interact with a number of polyanionic Proteins including actin, tubulin, Ca(2+)-calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding Protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. Some size isoforms of MBP are transported into the nucleus and thus they may also bind polynucleotides. Extracellular signals received by myelin or cultured oligodendrocytes cause changes in phosphorylation of MBP, suggesting that MBP is also involved in signaling. Further study of this very abundant Protein will reveal how it is utilized by the oligodendrocyte and myelin for different purposes.

Nicholas J Shaheen – One of the best experts on this subject based on the ideXlab platform.

  • diagnostic utility of major Basic Protein eotaxin 3 and leukotriene enzyme staining in eosinophilic esophagitis
    The American Journal of Gastroenterology, 2012
    Co-Authors: Evan S Dellon, Xiaoxin Chen, Ryan C Miller, John T Woosley, Nicholas J Shaheen

    Abstract:

    Diagnostic Utility of Major Basic Protein, Eotaxin-3, and Leukotriene Enzyme Staining in Eosinophilic Esophagitis

  • diagnostic utility of major Basic Protein eotaxin 3 and leukotriene enzyme staining in eosinophilic esophagitis
    The American Journal of Gastroenterology, 2012
    Co-Authors: Evan S Dellon, Xiaoxin Chen, Ryan C Miller, John T Woosley, Nicholas J Shaheen

    Abstract:

    Diagnostic Utility of Major Basic Protein, Eotaxin-3, and Leukotriene Enzyme Staining in Eosinophilic Esophagitis

Robin Miskimins – One of the best experts on this subject based on the ideXlab platform.

  • 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, 2005
    Co-Authors: Keith W Miskimins, Robin Miskimins

    Abstract:

    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.

  • Cloning and characterization of the rat myelin Basic Protein gene promoter.
    Gene, 2003
    Co-Authors: Qiou Wei, W. Keith Miskimins, Robin Miskimins

    Abstract:

    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.