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 -