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Blood, 1 September 2000, Vol. 96, No. 5, pp. 1733-1739
HEMATOPOIESIS
Pyk2 and Syk participate in functional activation of
granulocytic HL-60 cells in a different manner
Yasuo Miura,
Yumi Tohyama,
Terutoshi Hishita,
Amitabha Lala,
Ernesto De Nardin,
Yataro Yoshida,
Hirohei Yamamura,
Takashi Uchiyama, and
Kaoru Tohyama
From the Department of Hematology and Oncology and the
Department of Laboratory Medicine and Clinical Sciences, Graduate
School of Medicine, Kyoto University, Kyoto, Japan; the Department of
Biochemistry, Kobe University School of Medicine, Kobe, Japan; and the
Departments of Oral Biology and Microbiology, State University of New
York at Buffalo, Buffalo, NY.
The roles of the protein tyrosine kinases Pyk2 (also called RAFTK
or CAK  ) and Syk in the process of functional activation of human
myeloid cells were examined. During granulocytic differentiation of
HL-60 cells with dimethyl sulfoxide (DMSO), the amounts of Pyk2 and
2 integrin increased, whereas the amount of Syk was abundant before
differentiation and did not change during differentiation. When the
granulocytic cells were stimulated with
N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP),
tyrosine phosphorylation of Pyk2 occurred promptly and subsequent association of Pyk2 with 2 integrin was detected. In
contrast, Syk was not tyrosine phosphorylated by fMLP stimulation but
constitutively associated with 2 integrin. Stimulation with fMLP
also caused the alteration of 2 integrin to an activated form, a
finding that was confirmed by the observation of fMLP-induced cell
attachment on fibrinogen-coated dishes and inhibition of this
attachment by pretreatment with anti-2 integrin antibody. Cell
attachment to fibrinogen caused the enhanced tyrosine phosphorylation of Pyk2 and the initial tyrosine phosphorylation of Syk, which was also
inhibited by pretreatment with anti-2 integrin antibody. In vitro
kinase assays revealed that Pyk2 and Syk represented kinase activities
to induce tyrosine phosphorylation of several molecules in the
anti-2 integrin immunoprecipitates of the attached cells. These
results showed that Pyk2 is involved in the functional activation of
granulocytic cells in 2 signaling pathways: an fMLP receptor-mediated
"inside-out" signaling pathway that might cause 2
integrin activation and a subsequent 2 integrin-mediated
"outside-in" signaling pathway. Syk was activated in relation to
cell attachment to fibrinogen as a result of "outside-in"
signaling, although it was already associated with 2 integrin before
fMLP stimulation.
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