Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-104 |
Sentence |
denotes |
Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells. |
T2 |
105-279 |
Sentence |
denotes |
We have previously found that Raf-1, which is activated by hematopoietic growth factors in association with phosphorylation, is required for hematopoietic cell proliferation. |
T3 |
280-468 |
Sentence |
denotes |
Recently, 12-O-tetradecanoylphorbol 13-acetate has been found to mediate Raf-1 phosphorylation, suggesting that protein kinase C (PKC) may be involved in the Raf-1 activation mechanism(s). |
T4 |
469-704 |
Sentence |
denotes |
Since PKC can be activated by hematopoietic growth factors, it was investigated as a potential "Raf-1 kinase-kinase." Results demonstrate that bryostatin 1, a pharmacologic activator of PKC, induces activation of Raf-1 in FDC-P1 cells. |
T5 |
705-845 |
Sentence |
denotes |
PKC inhibitors H7 and staurosporine block both bryostatin 1- and interleukin-3-mediated Raf-1 phosphorylation and FDC-P1 cell proliferation. |
T6 |
846-1018 |
Sentence |
denotes |
Additionally, an antisense c-raf oligodeoxyribonucleotide specifically inhibits bryostatin 1-mediated proliferation, indicating a necessary role for Raf-1 in PKC signaling. |
T7 |
1019-1103 |
Sentence |
denotes |
Purified PKC can phosphorylate Raf-1 serine residues to high stoichiometry in vitro. |
T8 |
1104-1276 |
Sentence |
denotes |
Comparative phosphopeptide maps localize two PKC phosphorylation sites to Raf-1 phosphopeptides isolated from hematopoietic growth factor- or bryostatin 1-stimulated cells. |
T9 |
1277-1361 |
Sentence |
denotes |
The sites of PKC-mediated Raf-1 phosphorylation are deduced to be Ser497 and Ser619. |
T10 |
1362-1478 |
Sentence |
denotes |
Furthermore, PKC-mediated serine phosphorylation is sufficient to activate the enzymatic function of Raf-1 in vitro. |
T11 |
1479-1647 |
Sentence |
denotes |
These findings demonstrate that activated PKC can promote hematopoietic cell growth by regulating the enzymatic activity of Raf-1 through direct serine phosphorylation. |
T1 |
0-104 |
Sentence |
denotes |
Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells. |
T2 |
105-279 |
Sentence |
denotes |
We have previously found that Raf-1, which is activated by hematopoietic growth factors in association with phosphorylation, is required for hematopoietic cell proliferation. |
T3 |
280-468 |
Sentence |
denotes |
Recently, 12-O-tetradecanoylphorbol 13-acetate has been found to mediate Raf-1 phosphorylation, suggesting that protein kinase C (PKC) may be involved in the Raf-1 activation mechanism(s). |
T4 |
469-704 |
Sentence |
denotes |
Since PKC can be activated by hematopoietic growth factors, it was investigated as a potential "Raf-1 kinase-kinase." Results demonstrate that bryostatin 1, a pharmacologic activator of PKC, induces activation of Raf-1 in FDC-P1 cells. |
T5 |
705-845 |
Sentence |
denotes |
PKC inhibitors H7 and staurosporine block both bryostatin 1- and interleukin-3-mediated Raf-1 phosphorylation and FDC-P1 cell proliferation. |
T6 |
846-1018 |
Sentence |
denotes |
Additionally, an antisense c-raf oligodeoxyribonucleotide specifically inhibits bryostatin 1-mediated proliferation, indicating a necessary role for Raf-1 in PKC signaling. |
T7 |
1019-1103 |
Sentence |
denotes |
Purified PKC can phosphorylate Raf-1 serine residues to high stoichiometry in vitro. |
T8 |
1104-1276 |
Sentence |
denotes |
Comparative phosphopeptide maps localize two PKC phosphorylation sites to Raf-1 phosphopeptides isolated from hematopoietic growth factor- or bryostatin 1-stimulated cells. |
T9 |
1277-1361 |
Sentence |
denotes |
The sites of PKC-mediated Raf-1 phosphorylation are deduced to be Ser497 and Ser619. |
T10 |
1362-1478 |
Sentence |
denotes |
Furthermore, PKC-mediated serine phosphorylation is sufficient to activate the enzymatic function of Raf-1 in vitro. |
T11 |
1479-1647 |
Sentence |
denotes |
These findings demonstrate that activated PKC can promote hematopoietic cell growth by regulating the enzymatic activity of Raf-1 through direct serine phosphorylation. |