scholarly journals Quantitative Dynamic Analysis of Site-Specific Phosphorylation of Myelin Basic Protein Using Mass Spectrometry and iTRAQ Reagent

2009 ◽  
Vol 57 (4) ◽  
pp. 249-254 ◽  
Author(s):  
Mamoru MATSUBARA ◽  
Fumihiko TSUCHIYA
Keyword(s):  
Mass Spectrometry ◽  
Dynamic Analysis ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Site Specific ◽  
Itraq Reagent

scholarly journals HIV-Infected Patients: Cross Site-Specific Hydrolysis of H3 and H4 Histones and Myelin Basic Protein with Antibodies against These Three Proteins

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 316
Author(s):  
Svetlana V. Baranova ◽  
Pavel S. Dmitrenok ◽  
Valentina N. Buneva ◽  
Sergey E. Sedykh ◽  
Georgy A. Nevinsky
Keyword(s):  
Myelin Basic Protein ◽  
Intercellular Space ◽  
Basic Protein ◽  
Cross Reactivity ◽  
Cleavage Sites ◽  
Site Specific ◽  
Protein Clusters ◽  
Negative Role ◽  
Toxic Responses ◽  
Hydrolysis Of

Histones play important roles in chromatin functioning and gene transcription, but in the intercellular space, they are harmful since they stimulate systemic inflammatory and toxic responses. Electrophoretically homogeneous IgGs against myelin basic protein (MBP), as well as H3 and H4 histones, were isolated from sera of HIV-infected patients. In contrast to known classical proteases, these IgGs split exclusively only histones and MBP but no other control proteins. Among 13 sites of hydrolysis of H3 by IgGs against H3 and 14 sites for anti-MBP IgGs, only two sites of the hydrolysis were the same. Between seven cleavage sites of H4 with IgGs against H4 and 9 sites of this histone hydrolysis by antibodies against MBP, only three sites were the same. The sites of hydrolysis of H3 (and H4) with abzymes against these histones and against MBP were different, but several expended protein clusters containing hydrolysis sites are partially overlapped. The existence of enzymatic cross-reactivity of abzymes against H3 and H4 and MBP represents a great menace to humans since due to cell apoptosis, histones constantly occur in human blood. They can hydrolyze MBP of the myelin sheath of axons and play a negative role in the pathogenesis of HIV-infected patients.

scholarly journals Proteolysis of multiple myelin basic protein isoforms after neurotrauma: characterization by mass spectrometry

2008 ◽  
Vol 104 (5) ◽  
pp. 1404-1414 ◽  
Author(s):  
Andrew K. Ottens ◽  
Erin C. Golden ◽  
Liliana Bustamante ◽  
Ronald L. Hayes ◽  
Nancy D. Denslow ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Isoforms

Primary structure of equine myelin basic protein by mass spectrometry

2002 ◽  
Vol 405 (1) ◽  
pp. 137-146 ◽  
Author(s):  
D.D Wood ◽  
Y.M She ◽  
A.D Freer ◽  
G Harauz ◽  
M.A Moscarello
Keyword(s):  
Mass Spectrometry ◽  
Myelin Basic Protein ◽  
Primary Structure ◽  
Basic Protein

Site-specific degradation of myelin basic protein by the proteasome

2009 ◽  
Vol 425 (1) ◽  
pp. 68-72 ◽  
Author(s):  
A. A. Belogurov ◽  
N. A. Ponomarenko ◽  
V. M. Govorun ◽  
A. G. Gabibov ◽  
A. V. Bacheva
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Site Specific ◽  
Specific Degradation

Autoantibodies in HIV‐infected patients: Cross site‐specific hydrolysis of H1 histone and myelin basic protein

BioFactors ◽  
2018 ◽  
Vol 45 (2) ◽  
pp. 211-222 ◽  
Author(s):  
Svetlana V. Baranova ◽  
Pavel S. Dmitrienok ◽  
Valentina N. Buneva ◽  
Georgy A. Nevinsky
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Site Specific ◽  
H1 Histone ◽  
Hydrolysis Of ◽  
Cross Site

scholarly journals Competition Between Two MHC Binding Registers in a Single Peptide Processed from Myelin Basic Protein Influences Tolerance and Susceptibility to Autoimmunity

2003 ◽  
Vol 197 (10) ◽  
pp. 1391-1397 ◽  
Author(s):  
Audrey Seamons ◽  
Jennifer Sutton ◽  
Dina Bai ◽  
Emily Baird ◽  
Nena Bonn ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Mass Spectrometry ◽  
T Cells ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Allergic Encephalomyelitis ◽  
Tolerance Mechanisms ◽  
High Affinity ◽  
Experimental Allergic ◽  
Single Peptide

Experimental allergic encephalomyelitis (EAE) is an animal model for multiple sclerosis induced by stimulating myelin basic protein (MBP)-specific T cells. The MBP-specific repertoire in B10.PL mice is shaped by tolerance mechanisms that eliminate MBP121–150–specific T cells. In contrast, MBPAc1–11–specific T cells escape tolerance and constitute the encephalitogenic repertoire. To determine if this differential tolerance is caused by differences in the abundance of MBP epitopes generated by processing, MBP peptides were eluted from I-Au complexes and analyzed by mass spectrometry. Peptides were identified from both the NH2-terminal and MBP121–150 regions. Unexpectedly, MBPAc1–18 and Ac1–17, which contain the MBPAc1–11 epitope, were much more abundant than MBP121–150 peptides. The results demonstrate that competition between two I-Au binding registers, a low affinity register defined by MBPAc1–11 and a high affinity register defined by MBP5–16, prevents most of the NH2-terminal naturally processed peptides from binding in the MBPAc1–11 register. The small fraction of MBPAc1–18 bound in the MBPAc1–11 register is not sufficient to induce tolerance but provides a ligand for MBPAc1–11–specific T cells during disease. These results provide a basis for both the lack of tolerance to MBPAc1–11 and the ability of this epitope to become a target during autoimmunity.

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