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The T3/T cell receptor complex: antigenic distinction between the two 20‐kd T3 (T3‐delta and T3‐epsilon) subunits.
Author(s) -
Pessano S.,
Oettgen H.,
Bhan A.K.,
Terhorst C.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb03634.x
Subject(s) - biology , delta , antigen , microbiology and biotechnology , t cell receptor , receptor , genetics , t cell , physics , astronomy , immune system
Clonally distributed (clonotypic) antigen receptors on human T lymphocytes (alpha and beta chains) are associated with three invariable T3 polypeptide chains (T3 gamma, delta and epsilon), together forming the T3/T cell receptor complex. Monoclonal antibodies prepared against the two 20‐kd T3 polypeptide chains demonstrated that T3‐delta and T3‐epsilon are distinct polypeptide chains. Only one monoclonal antibody (anti‐T3‐delta chain) reacted with the T cell surface as judged by indirect immunofluorescence, and by its mitogenicity for quiescent peripheral blood lymphocytes. Immunohistological staining and immunoprecipitation experiments showed that both the T3‐delta and T3‐epsilon chains are T cell‐specific. As seen with the anti‐alpha/beta chain reagent WT‐31, anti‐T3‐delta chain monoclonal antibodies stained medullary thymocytes more intensely than cortical thymocytes, whereas the difference between the staining of cortical and medullary thymocytes was generally not apparent with anti‐T3‐epsilon chain antibodies. Because of this specificity and their ability to react with both the denatured and the native forms of each polypeptide chain, these new monoclonal reagents will be useful tools in studies of the biosynthesis and cell surface expression of the T3/T cell receptor complex during normal and malignant thymic differentiation.