Immunologic Cross-Reactivity between Spinal Cord Protein and Myelin Basic Protein

1982 ◽  
Vol 68 (3) ◽  
pp. 196-200 ◽  
Author(s):  
I.A. Ramshaw ◽  
D. Welter ◽  
C.F.C. MacPherson
1984 ◽  
Vol 21 (10) ◽  
pp. 999-1005
Author(s):  
Patricia Prokopchuk ◽  
Barry Ziola ◽  
Ian A. Ramshaw ◽  
Catherine F.C. Macpherson

2010 ◽  
Vol 42 (2) ◽  
pp. 135-139 ◽  
Author(s):  
Marzia Pesaresi ◽  
Silvia Giatti ◽  
Donato Calabrese ◽  
Omar Maschi ◽  
Donatella Caruso ◽  
...  

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 316
Author(s):  
Svetlana V. Baranova ◽  
Pavel S. Dmitrenok ◽  
Valentina N. Buneva ◽  
Sergey E. Sedykh ◽  
Georgy A. Nevinsky

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.


Author(s):  
William E. Grever ◽  
Fung-Chow Chiu ◽  
Marianela Tricoche ◽  
William K. Rashbaum ◽  
Karen M. Weidenheim ◽  
...  

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