An Antigen-Specific Suppressor T Cell Factor Controlled by Two Genes in the Immunoglobulin Heavy Chain Linkage Group and in the I-J Subregion of the H-2 Complex

Author(s):  
M. Taniguchi ◽  
T. Tokuhisa ◽  
M. Kanno ◽  
T. Honjo
1985 ◽  
Vol 82 (20) ◽  
pp. 7063-7067 ◽  
Author(s):  
M. Noguchi ◽  
K. Onoe ◽  
M. Ogasawara ◽  
K. Iwabuchi ◽  
L. Geng ◽  
...  

1983 ◽  
Vol 158 (6) ◽  
pp. 1912-1923 ◽  
Author(s):  
I Takei ◽  
T Sumida ◽  
M Taniguchi

An acceptor hybridoma with a receptor that recognizes the keyhole limpet hemocyanin (KLH)-specific suppressor T cell factor (KLH-TsF) was established after the fusion of C57BL/6 splenic T cells enriched with KLH-coated petri dishes. The cloned hybridoma (34S-281) could be specifically activated by stimulation with the conventional KLH-TsF or monoclonal KLH-TsF from three different hybridomas in the absence of the relevant antigen (KLH) and it started to produce another factor that suppresses the antibody response against DNP-KLH in a KLH-specific fashion. The KLH specificity of the TsF was required for activation. The new factor was found not to bind the KLH but to be absorbed with the KLH-TsF-producing hybridoma. It is thus strongly suggested that the acceptor site has a complementary structure (antiidiotype) for the KLH-TsF. Moreover, the idiotypic determinant on KLH-TsF was found to have a structure similar to that on some of the anti-KLH antibodies, since the acceptor hybridoma was specifically killed by the conventional anti-KLH antibodies and complement. Drawing on the above results, the idiotype-antiidiotype network in the conventional antigen system is discussed.


1981 ◽  
Vol 153 (6) ◽  
pp. 1672-1677 ◽  
Author(s):  
M Taniguchi ◽  
T Saito ◽  
I Takei ◽  
T Tokuhisa

The secreted form of the suppressor T cell factor specific for keyhole limpet hemocyanin derived from the hybridoma 34S-704 was found to consist of the two distinct polypeptide chains, i.e., the antigen-binding and the I-J-encoded chains. They were linked in covalent association with disulfide bonds. The two chains were cleaved by the reduction with dithiothreitol and were easy to reconstitute the active form of TsF. The association of the two distinct chains was suggested to be essential for the expression of the TsF activity.


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