Modulation of monocytic differentiation of HL-60 cells by inhibitors of protein tyrosine kinases

Katagiri, Koko; Katagiri, Takuya; Kajiyama, Kazuko; Uehara, Yoshimasa; Yamamoto, Tadashi; Yoshida, Takeshi

doi:10.1016/0008-8749(92)90196-v

Cited by 20 publications

(8 citation statements)

References 17 publications

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“…We reported that herbimycin A, an inhibitor of PTK, prevented HL-60 cells from acquiring macrophage-like features such as plastic and cellular adherence after stimulation ( Fig 2A). 4 In addition, herbimycin A completely inhibited TPAinduced activity of nonspecific esterase, a marker enzyme for monocytes (Fig 2A).38 As shown in Fig 2B, Hours after TPA stimulation Recently, the GAP-associated tyrosine phosphoproteins, p62 and p190, were supposed to function as the effectors downstream of signals emitted by R~S.".. '~ Figure 3A showed that in nontreated HL-60 cells, phosphotyrosine-containing proteins were not detected, and TPA and RA induced a tyrosine phosphorylation of various kinds of proteins.…”

Section: Resultsmentioning

confidence: 99%

Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells

Katagiri¹,

Hattori²,

Nakamura³

et al. 1994

Blood

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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.

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Section: Resultsmentioning

confidence: 99%

Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells

Katagiri¹,

Hattori²,

Nakamura³

et al. 1994

Blood

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“…␣-Tubulin can be cleaved by caspases in various circumstances (44 -47), and its cleavage could account for microtubule reorganization described in human monocytes (48) and U937 cells (49) undergoing macrophagic differentiation, which was reported also to involve post-translational modifications of the protein, such as phosphorylation of tyrosine residues (50). Vinculin is a highly conserved intracellular protein with a crucial role in cell adhesion and migration (51).…”

Section: Discussionmentioning

confidence: 99%

Identification of Proteins Cleaved Downstream of Caspase Activation in Monocytes Undergoing Macrophage Differentiation

Cathelin

Rébé

Haddaoui

et al. 2006

Journal of Biological Chemistry

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We have shown previously that caspases were specifically involved in the differentiation of peripheral blood monocytes into macrophages while not required for monocyte differentiation into dendritic cells. To identify caspase targets in monocytes undergoing macrophagic differentiation, we used the human monocytic leukemic cell line U937, whose macrophagic differentiation induced by exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) can be prevented by expression of the baculovirus caspase-inhibitory protein p35. A comparative two-dimensional gel proteomic analysis of empty vector-and p35-transfected cells after 12 h of exposure to 20 nM TPA, followed by mass spectrometry analysis, identified 38 differentially expressed proteins. Those overexpressed in p35-expressing cells (n ‫؍‬ 16) were all full-length, whereas half of those overexpressed in control cells (n ‫؍‬ 22) were N-or C-terminal cleavage fragments. The cleavage or degradation of seven of these proteins was confirmed in peripheral blood monocytes undergoing macrophage colony-stimulating factor-induced macrophagic differentiation. In U937 cells exposed to TPA, these proteolytic events can be inhibited by expression of a caspase-8 dominant negative mutant or the cowpox virus CrmA caspase inhibitor. These cleavages provide new insights to analyze the role of caspases in this specific differentiation program.

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“…In addition, genistein inhibits topoisomerase II and ribosomal S6 kinase by stabilizing a cleavable enzyme-DNA complex and modulating mRNA translation in vitro, which may lead to protein-linked DNA strand breaks and growth suppression of several malignant cell lines (19)(20)(21)(22). Genistein is also found to suppress the proliferation of a variety of human gastrointestinal cancer cell lines (23), induce differentiation of leukemia cells (24) and inhibit endothelial cell angiogenesis relevant to tumor metastasis (25). Recently, Uckun et al (26) reported that the biotherapy potencies of B-cell precursor leukemia are tremendously increased by targeting genistein to CD 19-associated tyrosine kinases.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of ultraviolet B (UVB)-induced c-fos and c-jun expression in vivo by a tyrosine kinase inhibitor genistein

Wang

Zhang²,

Lebwohl

et al. 1998

Carcinogenesis

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We reported the inhibitory effects of genistein, an inhibitor of tyrosine protein kinase (TPK), on ultraviolet B (UVB)-induced expression of c-fos and c-jun in SENCAR mouse skin. UVB irradiation substantially increased transcript levels of c-fos and c-jun mRNA in mouse skin. Topical application of genistein 60 min before UVB radiation reduced c-fos and c-jun expression in the mouse skin in dose-dependent manner. Inhibition was more pronounced in skin exposed to the low dose (5 kJ/m 2 ) than to the high dose (15 kJ/m 2 ) of UVB radiation. In addition, genistein exhibited more inhibition of c-fos than that of c-jun. Post-application of genistein after UVB exposure down-regulated the expressions of c-fos and c-jun, but to a lesser extent compared with pre-application. A431 human epidermoid carcinoma cells, which excessively express epidermal growth factor receptors (EGF-R), were used to investigate the possible mechanism of genistein's action. The results showed that genistein down-regulated the UVB-mediated phosphorylation of TPK-dependent EGF-R in a dose-dependent manner. We concluded that inhibition of UVB-induced c-fos and c-jun expression in mouse skin by genistein may, at least in part, result from the inhibition of TPK activities and down-regulation of EGF-R phosphorylation. Suppression of UVB-induced proto-oncogene expression in mouse skin suggests that genistein may serve as a potential preventative agent against photodamage and photocarcinogenesis.

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Modulation of monocytic differentiation of HL-60 cells by inhibitors of protein tyrosine kinases

Cited by 20 publications

References 17 publications

Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells

Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells

Identification of Proteins Cleaved Downstream of Caspase Activation in Monocytes Undergoing Macrophage Differentiation

Inhibition of ultraviolet B (UVB)-induced c-fos and c-jun expression in vivo by a tyrosine kinase inhibitor genistein

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