Structure of the T cell receptor in a Ti alpha V beta 2, alpha V beta 8-positive T cell line
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Structure of the T cell receptor in a Ti alpha V beta 2, alpha V beta 8-positive T cell line. / Hou, X; Dietrich, J; Kuhlmann, J; Wegener, A M; Geisler, C.
In: European Journal of Immunology, Vol. 24, No. 5, 1994, p. 1228-33.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Structure of the T cell receptor in a Ti alpha V beta 2, alpha V beta 8-positive T cell line
AU - Hou, X
AU - Dietrich, J
AU - Kuhlmann, J
AU - Wegener, A M
AU - Geisler, C
N1 - Keywords: Animals; Calcium; Cell Line; Clone Cells; Flow Cytometry; Humans; Mice; Receptors, Antigen, T-Cell, alpha-beta; Signal Transduction
PY - 1994
Y1 - 1994
N2 - The T cell receptor (TcR) is composed of at least six different polypeptide chains consisting of the clonotypic Ti heterodimer (Ti alpha beta or Ti gamma delta) and the noncovalently associated CD3 chains (CD3 gamma delta epsilon zeta). The exact number of subunits constituting the TcR is still not known; however, it has been suggested that each TcR contains two Ti dimers. To gain insight into the structure of the TcR we constructed a Ti alpha V beta 2, alpha V beta 8-positive T cell line which expressed the endogenous human TiV beta 8 and the transfected mouse TiV beta 2 both in association with the endogenous Ti alpha and CD3 chains at the cell surface. Preclearing experiments with radioiodinated cell lysate prepared with digitonin lysis buffer demonstrated that depleting the lysate of Ti alpha V beta 8 by immunoprecipitation with anti V beta 8 monoclonal antibody (mAb) did not reduce the amount of Ti alpha V beta 2 in the lysate, and likewise, depleting the lysate of Ti alpha V beta with anti-V beta 2 mAb did not reduce the amount of Ti alpha V beta 8. Comodulation experiments showed that V beta 8 and V beta 2 did not comodulate with each other. Furthermore, functional tests demonstrated that TcR containing V beta 8 and TcR containing V beta 2 mediated transmembrane activation signals independently of each other. These data demonstrate that mouse V beta 2 and human V beta 8 were not expressed in the same TcR in agreement with a TcR model where each TcR contains only one Ti dimer.
AB - The T cell receptor (TcR) is composed of at least six different polypeptide chains consisting of the clonotypic Ti heterodimer (Ti alpha beta or Ti gamma delta) and the noncovalently associated CD3 chains (CD3 gamma delta epsilon zeta). The exact number of subunits constituting the TcR is still not known; however, it has been suggested that each TcR contains two Ti dimers. To gain insight into the structure of the TcR we constructed a Ti alpha V beta 2, alpha V beta 8-positive T cell line which expressed the endogenous human TiV beta 8 and the transfected mouse TiV beta 2 both in association with the endogenous Ti alpha and CD3 chains at the cell surface. Preclearing experiments with radioiodinated cell lysate prepared with digitonin lysis buffer demonstrated that depleting the lysate of Ti alpha V beta 8 by immunoprecipitation with anti V beta 8 monoclonal antibody (mAb) did not reduce the amount of Ti alpha V beta 2 in the lysate, and likewise, depleting the lysate of Ti alpha V beta with anti-V beta 2 mAb did not reduce the amount of Ti alpha V beta 8. Comodulation experiments showed that V beta 8 and V beta 2 did not comodulate with each other. Furthermore, functional tests demonstrated that TcR containing V beta 8 and TcR containing V beta 2 mediated transmembrane activation signals independently of each other. These data demonstrate that mouse V beta 2 and human V beta 8 were not expressed in the same TcR in agreement with a TcR model where each TcR contains only one Ti dimer.
M3 - Journal article
C2 - 8181534
VL - 24
SP - 1228
EP - 1233
JO - European Journal of Immunology
JF - European Journal of Immunology
SN - 0014-2980
IS - 5
ER -
ID: 8545972