scholarly journals Myelin basic protein demonstrated immunocytochemically in oligodendroglia prior to myelin sheath formation.

1978 ◽  
Vol 75 (5) ◽  
pp. 2521-2524 ◽  
Author(s):  
N. H. Sternberger ◽  
Y. Itoyama ◽  
M. W. Kies ◽  
H. D. Webster
Keyword(s):  
Myelin Basic Protein ◽  
Myelin Sheath ◽  
Basic Protein ◽  
Sheath Formation

scholarly journals Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K

2011 ◽  
Vol 192 (5) ◽  
pp. 797-811 ◽  
Author(s):  
Lisbeth S. Laursen ◽  
Colin W. Chan ◽  
Charles ffrench-Constant
Keyword(s):  
Protein Synthesis ◽  
Myelin Basic Protein ◽  
Myelin Sheath ◽  
Basic Protein ◽  
Inhibitory Effect ◽  
Integrin Activation ◽  
Hnrnp K ◽  
Sheath Formation ◽  
The Central Nervous System ◽  
Mrna Binding

Myelination in the central nervous system provides a unique example of how cells establish asymmetry. The myelinating cell, the oligodendrocyte, extends processes to and wraps multiple axons of different diameter, keeping the number of wraps proportional to the axon diameter. Local regulation of protein synthesis represents one mechanism used to control the different requirements for myelin sheath at each axo–glia interaction. Prior work has established that β1-integrins are involved in the axoglial interactions that initiate myelination. Here, we show that integrin activation regulates translation of a key sheath protein, myelin basic protein (MBP), by reversing the inhibitory effect of the mRNA 3′UTR. During oligodendrocyte differentiation and myelination α6β1-integrin interacts with hnRNP-K, an mRNA-binding protein, which binds to MBP mRNA and translocates from the nucleus to the myelin sheath. Furthermore, knockdown of hnRNP-K inhibits MBP protein synthesis during myelination. Together, these results identify a novel pathway by which axoglial adhesion molecules coordinate MBP synthesis with myelin sheath formation.

Phase separation of myelin sheath in Triton X-114 solution: predominant localization of the 21.5-kDa isoform of myelin basic protein in the lipid raft-associated domain

2014 ◽  
Vol 155 (4) ◽  
pp. 265-271 ◽  
Author(s):  
M. Uruse ◽  
M. Yamamoto ◽  
M. Sugawa ◽  
K. Matsuura ◽  
Y. Sato ◽  
...  
Keyword(s):  
Phase Separation ◽  
Myelin Basic Protein ◽  
Lipid Raft ◽  
Myelin Sheath ◽  
Basic Protein ◽  
Triton X

The structure of myelin basic protein determined by high resolution electron microscopy and molecular modelling

1996 ◽  
Vol 54 ◽  
pp. 60-61
Author(s):  
D.R. Beniac ◽  
R.A. Ridsdale ◽  
M.D. Luckevich ◽  
T.A. Tompkins ◽  
G. Harauz
Keyword(s):  
High Resolution ◽  
Myelin Basic Protein ◽  
Molecular Modelling ◽  
Myelin Sheath ◽  
Basic Protein ◽  
Total Length ◽  
Energy Minimisation ◽  
Resolution Electron ◽  
Electron Microscopical ◽  
Β Sheet

Multiple sclerosis (MS) is characterised by the active degradation of the myelin sheath, and is thought to be precipitated by an autoimmune response to one or more of the sheath’s protein components. Myelin basic protein (MBP) is generally considered to be the antigen responsible for autoimmunity and is one of the most abundant proteins of the sheath. Knowledge of the tertiary structure of MBP, and its organisation on lipid layers and within the compacted myelin multilayers, is essential to understanding the organisation of the myelin membrane and the mechanisms of development of autoimmunity in MS. MBP has hitherto not proved crystallisable for structural studies by X-ray diffractometry despite much effort in this area. We have initiated high-resolution electron microscopical analyses of MBP. When imaged as individual particles, a recurring motif is that of a “C” shape in projection, of approximately 2 nm in thickness and 8 nm in length (Figure a – field of view; Figure b – class averages after single particle analysis; Figure c – 3D reconstruction). The total length of this particle is less than would be expected if the polypeptide chain were fully extended. Crystallisation experiments on MBP using monolayers of lipid mixtures (phosphatidylcholine, phosphatidylserine, dioleoyl phosphatidylethanolamine, galactocerebroside) yielded microcrystalline structures with a repeating pattern of packed protein molecules of size 5 nm, with an arm width of 2 nm and total length of 10-11 nm (Figure d). Molecular modelling of MBP based on the schemes proposed by Stoner and Martenson, and using coordinates of the β sheet backbone of bacteriochlorophyll A protein and energy minimisation of intervening segments, yielded a compact structure of size and appearance consistent with the electron microscopical data (Figure e). The bend of the C shape appears due to a natural curvature in the β sheet. These results are fully congruous with MBP having a regular secondary structure and domains that are potentially flexible with respect to one another. Energy minimisation experiments were performed on this model structure after specific post-translational modifications such as phosphorylation of specific sites (e.g., Ser7, Thr98) and conversion of arginine residues to citrullines. These results are consistent with biochemical data on accessibility of these sites to modification, and provide a framework for hypothesising scenarios of myelin sheath degradation in MS.

P4-288: Influence of GETO extract on myelin sheath structure and myelin basic protein content in the brain with AD model

2006 ◽  
Vol 2 ◽  
pp. S601-S601 ◽  
Author(s):  
Jing Shi ◽  
Jinzhou Tian ◽  
Yi Xu ◽  
Junxiang Yin ◽  
Shuli Sheng ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Protein Content ◽  
Myelin Sheath ◽  
Basic Protein ◽  
The Brain ◽  
Sheath Structure

P4-287: Effect of GETO extract on myelin sheath structure and myelin basic protein content in the brain with AD model

2006 ◽  
Vol 2 ◽  
pp. S601-S601 ◽  
Author(s):  
Jinzhou Tian ◽  
Yi Xu ◽  
Jing Shi ◽  
Junxiang Yin ◽  
Shuli Sheng ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Protein Content ◽  
Myelin Sheath ◽  
Basic Protein ◽  
The Brain ◽  
Sheath Structure

scholarly journals HIV-Infected Patients: Cross Site-Specific Hydrolysis of H2a and H2b Histones and Myelin Basic Protein with Antibodies against These Three Proteins

Biomolecules ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1501
Author(s):  
Svetlana V. Baranova ◽  
Pavel S. Dmitrienok ◽  
Valentina N. Buneva ◽  
Georgy A. Nevinsky
Keyword(s):  
Autoimmune Diseases ◽  
Myelin Basic Protein ◽  
Myelin Sheath ◽  
Cell Apoptosis ◽  
Basic Protein ◽  
Maldi Mass Spectrometry ◽  
Cross Reactivity ◽  
Cleavage Sites ◽  
Negative Role ◽  
Hydrolysis Of

Anti-DNA antibodies are usually produced against histone-DNA complexes appearing during cell apoptosis, while histones are known as damage-associated molecules. A myelin sheath of axons contains myelin basic protein (MBP) playing an important role in the pathogenesis of autoimmune diseases. Antibodies with enzymatic activities (abzymes) are distinctive features of some autoimmune and viral diseases. Abzymes against different proteins can usually only hydrolyze these specific proteins. Using sequential chromatographies of homogeneous IgG preparations from sera of HIV-infected patients on columns with immobilized MBP, H2a, and H2b histones, the anti-MBP, anti-H2a, and anti-H2b antibodies were obtained. It was first shown that IgGs against H2a and H2b effectively hydrolyze these histones and MBP, while anti-MBP split MBP, H2a, and H2b, but no other control proteins. Using the MALDI mass spectrometry, the cleavage sites of H2a, H2b, and MBP by abzymes against these three proteins were found. Among 14 sites of hydrolysis of H2a by IgGs against H2a and 10 sites by anti-MBP IgGs, only one site of hydrolysis was the same for these abzymes. Eleven cleavage sites of H2b with IgGs against H2b and 10 sites of its hydrolysis with antibodies against MBP were different. Anti-H2a, anti-H2b, and anti-MBP abzymes are unpredictable examples of IgGs possessing not only cross-complexation but also catalytic cross-reactivity, which may be a common phenomenon for such abzymes in patients with different autoimmune diseases. The existence of cross-reactivity of abzymes against H2a and H2b histones and MBP represent a great danger to humans since, in contrast with MBP, histones due to cell apoptosis constantly occur in human blood. Anti-H2a, anti-H2b, and anti-MBP can attack and hydrolyze myelin basic protein of the myelin sheath of axons and plays a negative role in the pathogenesis of several pathologies.

Cell-free synthesis of the myelin basic protein: A new approach to define the location of this protein in the myelin sheath

1980 ◽  
Vol 8 (5) ◽  
pp. 601-602
Author(s):  
SALLY A. JENNER ◽  
ELIZABETH A. HIRST ◽  
SIMON J. S. HARDY ◽  
MARTIN G. RUMSBY
Keyword(s):  
Myelin Basic Protein ◽  
Myelin Sheath ◽  
Basic Protein ◽  
Protein A ◽  
New Approach
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