scholarly journals Immune Profile and Signal Transduction of T-Cell Receptor in Autoimmune Thyroid Diseases

10.5772/35467 ◽  
2012 ◽  
Author(s):  
Adriano Namo
Keyword(s):  
Signal Transduction ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Thyroid Diseases ◽  
Autoimmune Thyroid Diseases ◽  
Immune Profile ◽  
Autoimmune Thyroid

Ig alpha and Ig beta are functionally homologous to the signaling proteins of the T-cell receptor

1994 ◽  
Vol 14 (2) ◽  
pp. 1095-1103
Author(s):  
A L Burkhardt ◽  
T Costa ◽  
Z Misulovin ◽  
B Stealy ◽  
J B Bolen ◽  
...  
Keyword(s):  
Signal Transduction ◽  
T Cells ◽  
T Cell ◽  
B Cell ◽  
T Cell Receptor ◽  
Interleukin 2 ◽  
Antigen Receptor ◽  
Cell Receptor ◽  
Antigen Receptors ◽  
Cell Antigen

Signal transduction by antigen receptors and some Fc receptors requires the activation of a family of receptor-associated transmembrane accessory proteins. One common feature of the cytoplasmic domains of these accessory molecules is the presence is at least two YXXA repeats that are potential sites for interaction with Src homology 2 domain-containing proteins. However, the degree of similarity between the different receptor-associated proteins varies from that of T-cell receptor (TCR) zeta and Fc receptor RIIIA gamma chains, which are homologous, to the distantly related Ig alpha and Ig beta proteins of the B-cell antigen receptor. To determine whether T- and B-cell antigen receptors are in fact functionally homologous, we have studied signal transduction by chimeric immunoglobulins bearing the Ig alpha or Ig beta cytoplasmic domain. We found that Ig alpha and Ig beta cytoplasmic domains were able to activate Ca2+ flux, interleukin-2 secretion, and phosphorylation of the same group of cellular substrates as the TCR in transfected T cells. Chimeric proteins were then used to examine the minimal requirements for activation of the Fyn, Lck, and ZAP kinases in T cells. Both Ig alpha and Ig beta were able to trigger Fyn, Lck, and ZAP directly without involvement of TCR components. Cytoplasmic tyrosine residues in Ig beta were required for recruitment and activation of ZAP-70, but these amino acids were not essential for the activation of Fyn and Lck. We conclude that Fyn and Lck are able to recognize a clustered nonphosphorylated immune recognition receptor, but activation of these kinases is not sufficient to induce cellular responses such as Ca2+ flux and interleukin-2 secretion. In addition, the molecular structures involved in antigen receptor signaling pathways are conserved between T and B cells.

scholarly journals A therapeutic anti-CD4 monoclonal antibody inhibits T cell receptor signal transduction in mouse autoimmune cardiomyopathy

2007 ◽  
Vol 120 (15) ◽  
pp. 1319-1325 ◽  
Author(s):  
Zhao-hui WANG ◽  
Yu-hua LIAO ◽  
Jing YUAN ◽  
Li ZHANG ◽  
Min WANG ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Monoclonal Antibody ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Receptor Signal

scholarly journals How does T cell receptor clustering impact on signal transduction?

2019 ◽  
Vol 132 (4) ◽  
pp. jcs226423 ◽  
Author(s):  
Jesse Goyette ◽  
Daniel J. Nieves ◽  
Yuanqing Ma ◽  
Katharina Gaus
Keyword(s):  
Signal Transduction ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Receptor Clustering

scholarly journals Serine/threonine phosphorylation of the γ-subunit after activation of the high-affinity Fc receptor for immunoglobulin G

1994 ◽  
Vol 299 (2) ◽  
pp. 569-577 ◽  
Author(s):  
D L Durden ◽  
H Rosen ◽  
J A Cooper
Keyword(s):  
Signal Transduction ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Fc Receptor ◽  
U937 Cells ◽  
Mobility Shift ◽  
Gamma Subunit ◽  
High Affinity ◽  
Phosphorylated Form

In this report we show that interferon gamma treatment of U937 cells induces increased expression of the gamma-subunit of the high-affinity Fc receptor for IgG (Fc gamma RI). Interferon treatment results in a 10-fold increased expression of the gamma-subunit and induces expression of a phosphorylated form (gamma 1). The increased expression of the gamma-subunit correlates with its ability to transmit a signal via Fc gamma R, as measured by activation of the respiratory burst using insoluble immune complexes. During Fc gamma R activation, a mobility shift occurs in the phosphorylated form of this gamma 1-subunit. Phosphoamino acid analysis demonstrates that this gamma 1 subunit is threonine phosphorylated in resting differentiated U937 cells and becomes predominantly serine phosphorylated on Fc receptor activation. The mobility shift in the gamma-subunit can be induced by treating U937 cells with phorbol 12-myristate 13-acetate or by monoclonal antibody cross-linking of Fc gamma RI. Hence the gamma-subunit is serine phosphorylated in response to Fc gamma RI and protein kinase C activation. Therefore the gamma-subunit, initially described as a subunit of Fc epsilon RI, now appears to be involved in signal transduction via Fc gamma RI. The data also suggest that the gamma-subunit, in contrast with the zeta-subunit of the T-cell receptor-CD3 complex, is a substrate for serine/threonine kinase(s) in the cell. The serine phosphorylation of the gamma-subunit suggests a divergence of structure and function between the gamma-subunit and its homologue, the zeta-subunit of the T-cell receptor. Phosphorylation of the gamma-subunit on serine may play some regulatory role in Fc gamma RI signal transduction in myeloid cells.

scholarly journals Phase separation of signaling molecules promotes T cell receptor signal transduction

Science ◽  
2016 ◽  
Vol 352 (6285) ◽  
pp. 595-599 ◽  
Author(s):  
Xiaolei Su ◽  
Jonathon A. Ditlev ◽  
Enfu Hui ◽  
Wenmin Xing ◽  
Sudeep Banjade ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Phase Separation ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Signaling Molecules ◽  
Receptor Signal
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