Interleukin 2 (IL-2)-induced tyrosine phosphorylation of IL-2 receptor p75.
We have recently established a mAb named TU11 mAb specific for the p75 subunit of human IL-2 receptor (IL-2R). The present study using TU11 mAb demonstrates the IL-2-induced phosphorylation of IL-2Rp75 on tyrosine residues in IL-2-dependent T cells. The tyrosine phosphorylation is mediated by the high affinity IL-2R, correlates with the IL-2-induced cell growth, and rapidly increases during the first 5 min of IL-2 stimulation. Phosphorylation of serine and threonine residues of IL-2Rp75 is also detected, but its IL-2 dependency is not significant during at least the first 5 min. These results suggest some roles of a tyrosine kinase associated with IL-2Rp75 in the IL-2-induced signal-transducing pathway.
Asao
H
H
Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
Takeshita
T
T
Nakamura
M
M
Nagata
K
K
Sugamura
K
K
D006801:Humans; D007376:Interleukin-2 / Q000494:pharmacology*; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000502:physiology; D015375:Receptors, Interleukin-2 / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism*
D007376:Interleukin-2; D015375:Receptors, Interleukin-2; D013912:Threonine; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases