scholarly journals Lack of gene rearrangement and mRNA expression of the beta chain of the T cell receptor in spontaneous rat large granular lymphocyte leukemia lines.

1985 ◽  
Vol 161 (5) ◽  
pp. 1249-1254 ◽  
Author(s):  
C W Reynolds ◽  
M Bonyhadi ◽  
R B Herberman ◽  
H A Young ◽  
S M Hedrick
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Antigen Receptor ◽  
Cell Receptor ◽  
Large Granular Lymphocyte ◽  
Beta Chain ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Lgl Leukemia

Using the murine cDNA clone for the beta chain of the T cell antigen receptor, we have examined four highly cytotoxic rat large granular lymphocyte (LGL) leukemia lines for the expression of unique rearrangements and mRNA transcription of the genes coding for the T cell antigen receptor. In contrast to normal rat T cells and nine rat T cell lines, the LGL leukemia lines exhibited no detectable gene rearrangements in the beta chain locus after digestion of LGL DNA by four restriction enzymes. Northern blots containing RNA from these LGL tumor lines demonstrated a low level of aberrant or nonrearranged beta chain transcription (less than 10 copies per cell) but virtually no translatable 1.3 kilobase message. These results demonstrate that LGL leukemia lines which mediate both natural killer (NK) and antibody-dependent cell-mediated cytotoxicity (ADCC) activities do not express the beta chain of the T cell receptor. The nature of the NK cell receptor for antigen remains elusive.

scholarly journals Identification of Inhibitors of the Association of ZAP-70 with the T Cell Receptor by High-Throughput Screen

2016 ◽  
Vol 22 (3) ◽  
pp. 324-331 ◽  
Author(s):  
Patrick R. Visperas ◽  
Christopher G. Wilson ◽  
Jonathan A. Winger ◽  
Qingrong Yan ◽  
Kevin Lin ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Peptide Binding ◽  
Antigen Receptor ◽  
Cell Receptor ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Antigen Receptor Signaling ◽  
Fluorescence Polarization Assay

ZAP-70 is a critical molecule in the transduction of T cell antigen receptor signaling and the activation of T cells. Upon activation of the T cell antigen receptor, ZAP-70 is recruited to the intracellular ζ-chains of the T cell receptor, where ZAP-70 is activated and colocalized with its substrates. Inhibitors of ZAP-70 could potentially function as treatments for autoimmune diseases or organ transplantation. In this work, we present the design, optimization, and implementation of a screen for inhibitors that would disrupt the interaction between ZAP-70 and the T cell antigen receptor. The screen is based on a fluorescence polarization assay for peptide binding to ZAP-70.

scholarly journals Two independently regulated Ca2+ entry mechanisms coexist in Jurkat T cells during T cell receptor antigen activation

1993 ◽  
Vol 293 (2) ◽  
pp. 395-398 ◽  
Author(s):  
S C Chow ◽  
G E Kass ◽  
S Orrenius
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Antigen Receptor ◽  
Cell Receptor ◽  
Jurkat Cells ◽  
Receptor Complex ◽  
T Cell Antigen Receptor ◽  
Bivalent Cation ◽  
Cell Antigen Receptor ◽  
Cell Antigen

Receptor-mediated Ca2+ influx was studied in the human leukaemic T cell line, Jurkat. Stimulation of these cells through the T cell antigen-receptor complex with OKT3 (an antibody against the CD3 molecules of the T cell antigen-receptor complex), or inhibition of the endoplasmic reticular Ca(2+)-ATPase with thapsigargin, resulted in Ca2+ mobilization from intracellular stores and the activation of Ca2+ and Mn2+ entry. The rates of thapsigargin-induced Ca2+ and Mn2+ entry in Jurkat cells were 76% and 64% respectively of those observed after treatment of these cells with OKT3. The combined addition of thapsigargin plus OKT3 to Jurkat cells produced an enhanced effect on the sustained increase in the cytosolic free Ca2+ concentration that was greater than that obtained by addition of thapsigargin or OKT3 alone. The rates of Ca2+ and Mn2+ entry were increased to 119% and 112% respectively of the OKT3-induced rates. Taken together, these results suggest that the inositol 1,4,5-trisphosphate-sensitive Ca(2+)-pool-dependent bivalent cation entry only accounts for 57% and 52% respectively of the total OKT3-dependent Ca2+ and Mn2+ entry, and that the rest is mediated by second messenger(s). Thus two separate pathways coexist in regulating Ca2+ entry in Jurkat cells during activation mediated through the T cell receptor.

scholarly journals Conserved structure of amphibian T-cell antigen receptor beta chain.

1993 ◽  
Vol 90 (14) ◽  
pp. 6811-6814 ◽  
Author(s):  
J. S. Fellah ◽  
F. Kerfourn ◽  
F. Guillet ◽  
J. Charlemagne
Keyword(s):  
T Cell ◽  
Antigen Receptor ◽  
Beta Chain ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Receptor Beta

scholarly journals Stoichiometry of the T cell antigen receptor (TCR) complex: each TCR/CD3 complex contains one TCR alpha, one TCR beta, and two CD3 epsilon chains.

1994 ◽  
Vol 180 (2) ◽  
pp. 587-593 ◽  
Author(s):  
J A Punt ◽  
J L Roberts ◽  
K P Kearse ◽  
A Singer
Keyword(s):  
T Cells ◽  
T Cell ◽  
Antigen Receptor ◽  
Beta Chain ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Quantitative Immunofluorescence ◽  
Beta Proteins ◽  
The Individual

The stoichiometry of the subunits that comprise the T cell antigen receptor (TCR) complex is not completely known. In particular, it is uncertain whether TCR alpha and TCR beta proteins are present in the TCR complex as one or multiple heterodimeric pairs. In this study we have used mice transgenic for two different TCR alpha and two different TCR beta proteins to determine the number of TCR alpha and TCR beta chains in a single TCR complex. Individual thymocytes and splenic T cells from double TCR transgenic mice simultaneously expressed all four transgenic TCR proteins on their surfaces. Because the individual TCR alpha and individual TCR beta proteins were biochemically distinguishable, we were able to examine association among the transgenic TCR products. We found that each TCR alpha chain paired with each TCR beta chain, but that each TCR complex contained only one TCR alpha and one TCR beta protein. Furthermore, quantitative immunofluorescence revealed that T cells expressed twice as many CD3 epsilon as TCR beta proteins. These findings demonstrate that there are precisely one TCR alpha, one TCR beta, and two CD3 epsilon chains in each TCR/CD3 complex expressed on the surfaces of both thymocytes and mature T cells.

Crystal structure of the beta chain of a T cell antigen receptor

Science ◽  
1995 ◽  
Vol 267 (5206) ◽  
pp. 1984-1987 ◽  
Author(s):  
G. Bentley ◽  
G Boulot ◽  
K Karjalainen ◽  
R. Mariuzza
Keyword(s):  
Crystal Structure ◽  
T Cell ◽  
Antigen Receptor ◽  
Beta Chain ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

Selection of amino acid sequences in the beta chain of the T cell antigen receptor

Science ◽  
1988 ◽  
Vol 239 (4847) ◽  
pp. 1541-1544 ◽  
Author(s):  
S. Hedrick ◽  
I Engel ◽  
D. McElligott ◽  
P. Fink ◽  
M. Hsu ◽  
...  
Keyword(s):  
Amino Acid ◽  
T Cell ◽  
Antigen Receptor ◽  
Amino Acid Sequences ◽  
Beta Chain ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Selection Of
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