Suppression of experimental allergic encephalomyelitis in lewis rats treated with myelin basic protein-liposome complexes: Clinical, histopathological, and cell-mediated immunity correlates

1984 ◽  
Vol 84 (1) ◽  
pp. 171-184 ◽  
Author(s):  
G.H. Strejan ◽  
D.H. Percy ◽  
J.St. Louis
Keyword(s):  
Myelin Basic Protein ◽  
Experimental Allergic Encephalomyelitis ◽  
Basic Protein ◽  
Cell Mediated Immunity ◽  
Allergic Encephalomyelitis ◽  
Lewis Rats ◽  
Experimental Allergic

scholarly journals Myelin basic protein serum factor. An endogenous neuroantigen influencing development of experimental allergic encephalomyelitis in Lewis rats.

1978 ◽  
Vol 148 (6) ◽  
pp. 1716-1721 ◽  
Author(s):  
R S Fujinami ◽  
P Y Paterson ◽  
E D Day ◽  
V A Varitek
Keyword(s):  
Myelin Basic Protein ◽  
Experimental Allergic Encephalomyelitis ◽  
Basic Protein ◽  
Potential Importance ◽  
Serum Factor ◽  
Allergic Encephalomyelitis ◽  
Lewis Rats ◽  
Age Related ◽  
Protein Serum ◽  
Experimental Allergic

Age-related concentrations of myelin basic protein serum factor (MBP-SF), an endogenous neuroantigen detected and quantitated by inhibition of binding of rat myelin basic protein (RMBP) antibody with 125I-RMBP reagent antigen and immunochemically indistinguishable from native RMBP in this respect, reach peak levels as high as 21 ng/microliter among 2-3-wk-old normal suckling Lewis rats. Levels then progressively decline to low, usually undetectable levels of less than or equal to 0.6 ng/microliter MBP-equivalents in adult animals by 7 wk of age. MBP-SF levels are inversely related to the age-related increasing capacity of maturing Lewis rats to develop experimental allergic encephalomyelitis (EAE) after sensitization to MBP of syngeneic, but not xenogeneic, origin. MBP-SF appears to be an endogenous neuroimmunoregulatory product of potential importance for immunologic tolerance to autologous RMBP in Lewis rats.

scholarly journals Protection from experimental allergic encephalomyelitis conferred by a monoclonal antibody directed against a shared idiotype on rat T cell receptors specific for myelin basic protein.

1988 ◽  
Vol 168 (6) ◽  
pp. 2153-2164 ◽  
Author(s):  
M Owhashi ◽  
E Heber-Katz
Keyword(s):  
T Cell ◽  
Myelin Basic Protein ◽  
Experimental Allergic Encephalomyelitis ◽  
Basic Protein ◽  
Specific Cell ◽  
Allergic Encephalomyelitis ◽  
Two Dimensional Gel Electrophoresis ◽  
Lewis Rats ◽  
T Cell Lines ◽  
Experimental Allergic

Immunizing Lewis rats with guinea pig myelin basic protein (MBP) yielded an encephalitogen specific, Ia-restricted, rat-mouse T cell hybridoma 5.10, which was used to establish a clonotypic mAb (10.18) that binds to and precipitates the rat TCR. By two-dimensional gel electrophoresis, the rat TCR was shown to consist of two disulfide-linked peptide chains with mol wt of 48,000 and 39,000. 10.18 binds the majority of cells in MBP-specific T cell lines that are capable of transferring experimental allergic encephalomyelitis (EAE) to Lewis rat recipients, but does not bind to either a purified protein derivative of tuberculin-specific cell line or an OVA-specific line. Furthermore, soluble 10.18 can block antigen-specific stimulation of hybridoma 5.10 but cannot control hybridomas, while immobilized 10.18 stimulates 5.10, but cannot control the hybrids. Though 10.18+ cells are very rare in normal rats, increase of 10.18+ cells is observed in MBP-primed paralyzed rats. Finally, when 10.18 is injected into MBP-primed Lewis rats, EAE is abrogated. We have thus characterized EAE as a "mono-idiotypic" autoimmune disease.

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