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Activation of Ras and formation of GAP complex during TPA-induced monocytic
differentiation of HL-60 cells
K Katagiri, S Hattori, S Nakamura, T Yamamoto, T Yoshida and T Katagiri
Tokyo Institute for Immunopharmacology, Inc., Toshima-kur, Japan.
In this study, it was shown that the proportion of guanosine triphosphate
(GTP)-bound active Ras increased in TPA (12-o- tetradecanoyl
phorbol-13-acetate)-induced monocytic differentiation of HL-60 cells. The
increase of active Ras was observed at 24 hours after TPA stimulation and
attained to threefold (15%) over the proportion in nontreated HL-60 cells.
Herbimycin A, an inhibitor of tyrosine kinase, prevented the activation of
Ras, as well as the induction of monocytic differentiation. In parallel
with the activation of Ras, the proteins with molecular weights of 52, 56,
62, and 190 kD were tyrosine- phosphorylated and formed a complex with
GTPase-activating protein (GAP) for Ras. In addition to the 116-kD GAP
(type I GAP), the 100-kD GAP (type II GAP) molecule was markedly induced at
24 hours after TPA stimulation of HL-60 cells. These phenomena sustained
for a further 24 hours during monocytic differentiation. However, they were
not observed during retinoic acid-induced granulocytic differentiation of
the cells. The HL-60 transfectants, which expressed a dominant inhibitory
Ha-ras Asn17, showed a low level of tyrosine-phosphorylated GAP-associated
proteins and did not undergo full differentiation in response to TPA. Taken
together, these data indicate that the activation of Ras and GAP complex
formation mutually correlate and function downstream of protein- tyrosine
kinases in the signaling pathway for monocytic differentiation of HL-60
cells.
Volume 84,
Issue 6,
pp. 1780-1789,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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