Mechanism of Ribosomal p70S6 Kinase Activation by Granulocyte Macrophage Colony-stimulating Factor in Neutrophils
We report here for the first time the detection of the ribosomal p70S6 kinase (p70S6K) in a hematopoietic cell, the neutrophil, and the stimulation of its enzymatic activity by granulocyte macrophage colony-stimulating factor (GM-CSF). GM-CSF modified the Vmax of the enzyme (from 7.2 to 20.5 pmol/mi...
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Published in | The Journal of biological chemistry Vol. 278; no. 30; pp. 28130 - 28138 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
25.07.2003
American Society for Biochemistry and Molecular Biology |
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Abstract | We report here for the first time the detection of the ribosomal p70S6 kinase (p70S6K) in a hematopoietic cell, the neutrophil, and the stimulation of its enzymatic activity by granulocyte macrophage colony-stimulating factor (GM-CSF). GM-CSF modified the Vmax of the enzyme (from 7.2 to 20.5 pmol/min/mg) and induced a time- and dose-dependent phosphorylation on p70S6K residues Thr389 and Thr421/Ser424. The immunosuppressant macrolide rapamycin caused either a decrease in intensity of phospho-Thr389 bands in Western blots, or as a downshift in the relative mobility of phospho-Thr421/Ser424 bands (consistent with the loss of phosphate), but not both simultaneously. The immunosuppressant FK506 failed to inhibit p70S6K activation, but was able to rescue the rapamycin-induced downshift, pointing to a role for the mammalian target of rapamycin (mTOR) kinase. Rapamycin also caused an inhibition (IC50 0.2 nm) of the in vitro enzymatic activity of p70S6K. However, the inhibition of activity was not complete, but only a 40–50%, indicating that neutrophil p70S6K activity has a rapamycin-resistant component. This component was totally inhibited by pre-incubating the cells with the mitogen-activated protein kinase (MAPK) kinase (MEK) inhibitor PD-98059 prior to treatment with rapamycin. This indicated that a kinase from the MEK/MAPK pathway also plays a role in p70S6K activation. Thus, GM-CSF causes the dual activation of a rapamycin-resistant, MAPK-related kinase, that targets Thr421/Ser424 S6K phosphorylation, and a rapamycin-sensitive, mTOR-related kinase, that targets Thr389, both of which are needed in cooperation to achieve full activation of neutrophil p70S6K. |
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AbstractList | We report here for the first time the detection of the ribosomal p70S6
kinase (p70S6K) in a hematopoietic cell, the neutrophil, and the stimulation
of its enzymatic activity by granulocyte macrophage colony-stimulating factor
(GM-CSF). GM-CSF modified the V max of the enzyme (from 7.2
to 20.5 pmol/min/mg) and induced a time- and dose-dependent phosphorylation on
p70S6K residues Thr 389 and Thr 421 /Ser 424 . The
immunosuppressant macrolide rapamycin caused either a decrease in intensity of
phospho-Thr 389 bands in Western blots, or as a downshift in the
relative mobility of phospho-Thr 421 /Ser 424 bands
(consistent with the loss of phosphate), but not both simultaneously. The
immunosuppressant FK506 failed to inhibit p70S6K activation, but was able to
rescue the rapamycin-induced downshift, pointing to a role for the mammalian
target of rapamycin (mTOR) kinase. Rapamycin also caused an inhibition
(IC 50 0.2 n m ) of the in vitro enzymatic
activity of p70S6K. However, the inhibition of activity was not complete, but
only a 40â50%, indicating that neutrophil p70S6K activity has a
rapamycin-resistant component. This component was totally inhibited by
pre-incubating the cells with the mitogen-activated protein kinase (MAPK)
kinase (MEK) inhibitor PD-98059 prior to treatment with rapamycin. This
indicated that a kinase from the MEK/MAPK pathway also plays a role in p70S6K
activation. Thus, GM-CSF causes the dual activation of a rapamycin-resistant,
MAPK-related kinase, that targets Thr 421 /Ser 424 S6K
phosphorylation, and a rapamycin-sensitive, mTOR-related kinase, that targets
Thr 389 , both of which are needed in cooperation to achieve full
activation of neutrophil p70S6K. We report here for the first time the detection of the ribosomal p70S6 kinase (p70S6K) in a hematopoietic cell, the neutrophil, and the stimulation of its enzymatic activity by granulocyte macrophage colony-stimulating factor (GM-CSF). GM-CSF modified the Vmax of the enzyme (from 7.2 to 20.5 pmol/min/mg) and induced a time- and dose-dependent phosphorylation on p70S6K residues Thr389 and Thr421/Ser424. The immunosuppressant macrolide rapamycin caused either a decrease in intensity of phospho-Thr389 bands in Western blots, or as a downshift in the relative mobility of phospho-Thr421/Ser424 bands (consistent with the loss of phosphate), but not both simultaneously. The immunosuppressant FK506 failed to inhibit p70S6K activation, but was able to rescue the rapamycin-induced downshift, pointing to a role for the mammalian target of rapamycin (mTOR) kinase. Rapamycin also caused an inhibition (IC50 0.2 nm) of the in vitro enzymatic activity of p70S6K. However, the inhibition of activity was not complete, but only a 40–50%, indicating that neutrophil p70S6K activity has a rapamycin-resistant component. This component was totally inhibited by pre-incubating the cells with the mitogen-activated protein kinase (MAPK) kinase (MEK) inhibitor PD-98059 prior to treatment with rapamycin. This indicated that a kinase from the MEK/MAPK pathway also plays a role in p70S6K activation. Thus, GM-CSF causes the dual activation of a rapamycin-resistant, MAPK-related kinase, that targets Thr421/Ser424 S6K phosphorylation, and a rapamycin-sensitive, mTOR-related kinase, that targets Thr389, both of which are needed in cooperation to achieve full activation of neutrophil p70S6K. |
Author | Calvo, Victor Lehman, Jason A. Gomez-Cambronero, Julian |
Author_xml | – sequence: 1 givenname: Jason A. surname: Lehman fullname: Lehman, Jason A. organization: Department of Physiology and Biophysics, Wright State University School of Medicine, Dayton, Ohio 45435 – sequence: 2 givenname: Victor surname: Calvo fullname: Calvo, Victor organization: Instituto de Investigaciones Biomedicas, Consejo Superior de Investigaciones Cientificas, Facultad Medicina Universidad Autonoma de Madrid, Arturo Duperier 4, 28029 Madrid, Spain – sequence: 3 givenname: Julian surname: Gomez-Cambronero fullname: Gomez-Cambronero, Julian email: julian.cambronero@wright.edu organization: Department of Physiology and Biophysics, Wright State University School of Medicine, Dayton, Ohio 45435 |
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Snippet | We report here for the first time the detection of the ribosomal p70S6 kinase (p70S6K) in a hematopoietic cell, the neutrophil, and the stimulation of its... We report here for the first time the detection of the ribosomal p70S6 kinase (p70S6K) in a hematopoietic cell, the neutrophil, and the stimulation of its... |
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Title | Mechanism of Ribosomal p70S6 Kinase Activation by Granulocyte Macrophage Colony-stimulating Factor in Neutrophils |
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