MHC class I signaling in T cells leads to tyrosine kinase activity and PLC-gamma 1 phosphorylation
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
MHC class I signaling in T cells leads to tyrosine kinase activity and PLC-gamma 1 phosphorylation. / Skov, S; Odum, Niels; Claesson, M H.
In: Journal of Immunology, Vol. 154, No. 3, 1995, p. 1167-76.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - MHC class I signaling in T cells leads to tyrosine kinase activity and PLC-gamma 1 phosphorylation
AU - Skov, S
AU - Odum, Niels
AU - Claesson, M H
N1 - Keywords: Antigens, CD45; Benzoquinones; Calcium; Histocompatibility Antigens Class I; Humans; Isoenzymes; Lactams, Macrocyclic; Phospholipase C gamma; Phosphotyrosine; Precipitin Tests; Protein-Tyrosine Kinases; Quinones; Receptor-CD3 Complex, Antigen, T-Cell; Signal Transduction; T-Lymphocytes; Tumor Cells, Cultured; Type C Phospholipases; Tyrosine
PY - 1995
Y1 - 1995
N2 - We have studied the biochemical signal pathway leading to a rise in intracellular free calcium concentration ([Ca2+]i) following cross-linking of MHC class I (MHC-I) molecules on human T leukemic Jurkat cells. Evidence is presented that MHC-I signaling is dependent on tyrosine kinase activity before the observed increase in [Ca2+]i. Thus, tyrosine phosphorylation was detected within 5 s after MHC-I cross-linking, whereas an increase in [Ca2+]i was observed after a lag period of 30 s. Moreover, an inhibitor of tyrosine kinases, herbimycin A, almost completely blocked MHC-I-induced tyrosine phosphorylation and the subsequent calcium response. The early tyrosine kinase activity was found to be dependent on expression of the TCR/CD3 complex and the CD45 molecule on the surface of the T cells. Furthermore, MHC-I cross-linking was shown to tyrosine phosphorylate PLC-gamma 1 (phospholipase C-gamma 1). Collectively, these results indicate that the MHC-I signaling pathway is linked to activation of tyrosine kinase(s) in Jurkat cells.
AB - We have studied the biochemical signal pathway leading to a rise in intracellular free calcium concentration ([Ca2+]i) following cross-linking of MHC class I (MHC-I) molecules on human T leukemic Jurkat cells. Evidence is presented that MHC-I signaling is dependent on tyrosine kinase activity before the observed increase in [Ca2+]i. Thus, tyrosine phosphorylation was detected within 5 s after MHC-I cross-linking, whereas an increase in [Ca2+]i was observed after a lag period of 30 s. Moreover, an inhibitor of tyrosine kinases, herbimycin A, almost completely blocked MHC-I-induced tyrosine phosphorylation and the subsequent calcium response. The early tyrosine kinase activity was found to be dependent on expression of the TCR/CD3 complex and the CD45 molecule on the surface of the T cells. Furthermore, MHC-I cross-linking was shown to tyrosine phosphorylate PLC-gamma 1 (phospholipase C-gamma 1). Collectively, these results indicate that the MHC-I signaling pathway is linked to activation of tyrosine kinase(s) in Jurkat cells.
M3 - Journal article
C2 - 7529791
VL - 154
SP - 1167
EP - 1176
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 3
ER -
ID: 10635993