Control of HL-60 monocytic differentiation

Yen, Andrew; Brown, D G; Fishbaugh, Justin

doi:10.1016/0014-4827(87)90432-0

Cited by 38 publications

(7 citation statements)

References 21 publications

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“…The heterogeneity of pRB bands began to disappear between 10 and 24 h after treatment of the cells with TPA, suggesting a reduction in the phosphorylation of pRB. This coincides with the onset of morphological differentiation and time of cell cycle arrest (Rovera et al 1979;Yen et al 1987; data not shown). By 48 h, all of the slower migrating forms of pRB were no longer present and pRB migrated as a single species.…”

Section: Resultssupporting

confidence: 57%

Dephosphorylation of the retinoblastoma protein during differentiation of HL60 cells

Whyte¹,

Eisenman²

1992

Biochem. Cell Biol.

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Immunoprecipitated retinoblastoma protein from HL60 cells migrated as a series of bands during electrophoresis. The heterogeneity appeared to be generated by phosphorylation of the retinoblastoma protein. Treatment of the cells with the phorbol ester, tetradecanoyl phorbol acetate (TPA), resulted in both a loss of the heterogeneity of the pRB species and a significant decrease in the level of pRB phosphorylation. These changes accompanied differentiation of the HL60 cells into macrophages. Treatment of the cells with dibutyryl cAMP also resulted in dephosphorylation of pRB as well as cell cycle arrest, although no recognizable differentiation occurred. These results are consistent with a model in which TPA and dibutyryl cAMP dependent pathways can activate pRB by altering its phosphorylation.

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Section: Resultssupporting

confidence: 57%

Dephosphorylation of the retinoblastoma protein during differentiation of HL60 cells

Whyte¹,

Eisenman²

1992

Biochem. Cell Biol.

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“…This process involves changes in cell-substrate adherence, growth arrest in late G 1 , and increased expression of monocyte markers (3,4). Similarly, treatment of U937 cells with okadaic acid, a natural product isolated from the black sponge and a potent inhibitor of protein phosphatases 1 and 2A, also induces differentiation of these cells (5), cell cycle arrest, and eventual (72-h) apoptosis (6).…”

mentioning

confidence: 98%

The Role of the Transcription Factor Sp1 in Regulating the Expression of the WAF1/CIP1 Gene in U937 Leukemic Cells

Biggs

Kudlow

Kraft

1996

Journal of Biological Chemistry

208

183

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The Waf1/Cip1 protein induces cell cycle arrest through inhibition of the activity of cyclin-dependent kinases and proliferating cell nuclear antigen. Expression of the WAF1/CIP1 gene is induced in a p53-dependent manner in response to DNA damage but can also be induced in the absence of p53 by agents such as growth factors, phorbol esters, and okadaic acid. WAF1/CIP1 expression in U937 human leukemic cells is induced by both phorbol ester, a protein kinase C activator, and by okadaic acid, an inhibitor of phosphatases 1 and 2A. Both of these agents induce the differentiation of these leukemic cells toward macrophages. We demonstrate that phorbol esters and okadaic acid stimulate transcription from the WAF1/CIP1 promoter in U937 cells. This transcription is mediated by a region of the promoter between ؊154 and ؉16, which contains two binding sites for the transcription factor Sp1. Deletion or mutation of these Sp1 sites reduces WAF1/CIP1 promoter response to phorbol ester and okadaic acid, while a reporter gene under the control of a promoter containing only multiple Sp1 binding sites and a TATA box is induced by phorbol ester and okadaic acid. The WAF1/ CIP1 promoter is also highly induced by exogenous Sp1 in the Sp1-deficient Drosophila Schnieder SL 2 cell line. These results suggest that phorbol ester and okadaic acid activate transcription of the WAF1/CIP1 promoter through a complex of proteins that includes Sp1 and basal transcription factors.Treatment of the human myeloid leukemic cell line U937 with phorbol esters such as phorbol myristate acetate (PMA), 1 an activator of protein kinase C, leads to macrophage/monocyte-like differentiation over a 72-h period (1, 2). This process involves changes in cell-substrate adherence, growth arrest in late G 1 , and increased expression of monocyte markers (3, 4). Similarly, treatment of U937 cells with okadaic acid, a natural product isolated from the black sponge and a potent inhibitor of protein phosphatases 1 and 2A, also induces differentiation of these cells (5), cell cycle arrest, and eventual (72-h) apoptosis (6). Both PMA and okadaic acid induce expression of the cyclindependent kinase inhibitor, WAF1/CIP1 (7,8).WAF1/CIP1 expression is induced by the p53 protein following irradiation of cells (9, 10), but p53-independent expression of WAF1/CIP1 is associated with differentiation of myocytes (11, 12), of HL 60 leukemic cells (13), and of a number of other cells. WAF1/CIP1 is expressed in a number of tissues over the course of murine development, and expression in most tissues is not dependent on the presence of p53 (14). p53-independent expression of the WAF1/CIP1 gene can be induced in cultured cells by a number of agents, including, besides PMA and okadaic acid, platelet-derived growth factor, fibroblast growth factor, and transforming growth factor ␤ (15, 16). Preliminary analysis of the WAF1/CIP1 promoter suggests that the elements mediating response to serum in fibroblasts are located at least 1.9 kb upstream from the transcription start site (14), while...

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“…RA or D3 are known to induce HL-60 myeloblastic leukemia cells to undergo G0 cell cycle arrest and myeloid or monocytic differentiation [15]. Our previous studies have indicated that in HL-60 cells RA and D3 cause ERK phosphorylation and activation of MAPK signaling leading to myeloid or monocytic differentiation and G0 cell cycle arrest [16].…”

Section: Introductionmentioning

confidence: 99%

Nicotinamide Cooperates with Retinoic Acid and 1,25-Dihydroxyvitamin D<sub>3</sub> to Regulate Cell Differentiation and Cell Cycle Arrest of Human Myeloblastic Leukemia Cells

Shen

Yen

2009

Oncology

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Nicotinamide, the amide derivative of vitamin B₃, cooperates with retinoic acid (RA), a form of vitamin A, and 1,25-dihydroxyvitamin D₃ (D3), to regulate cell differentiation and proliferation of human myeloblastic leukemia cells. In human myeloblastic leukemia cells, RA or D3 are known to cause MAPK signaling leading to myeloid or monocytic differentiation and G0 cell cycle arrest. In this process, RA or D3 induces the early expression of CD38, a receptor that causes ERK signaling and propels further differentiation. Our study demonstrates that nicotinamide in combination with RA or D3 affected induced expression levels of CD38, CD11b and CD14, suggesting a cooperative function of nicotinamide and RA or D3. Nicotinamide transiently retarded the initial RA- or D3-induced expression of CD38, which subsequently reached the same nearly 100% expression. Nicotinamide induced ERK activation and further enhanced the RA-induced ERK activation, but the D3-induced ERK activation was diminished by nicotinamide, although levels still exceeded those induced by RA, suggesting lineage-specific nicotinamide responses. Nicotinamide enhanced both RA- and D3-induced CD11b expression, inducible oxidative metabolism, and G0 cell cycle arrest, accelerating their induced occurrence in all instances. Consistent with this, the RA- or D3-induced downregulation of PARP was enhanced by nicotinamide. Nicotinamide thus regulated RA- or D3-induced differentiation and G0 arrest, causing a transient delay in certain early aspects of the progression to terminal differentiation but ultimately accelerating the occurrence of terminally, functionally differentiated G0 cells.

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Control of HL-60 monocytic differentiation

Cited by 38 publications

References 21 publications

Dephosphorylation of the retinoblastoma protein during differentiation of HL60 cells

Dephosphorylation of the retinoblastoma protein during differentiation of HL60 cells

The Role of the Transcription Factor Sp1 in Regulating the Expression of the WAF1/CIP1 Gene in U937 Leukemic Cells

Nicotinamide Cooperates with Retinoic Acid and 1,25-Dihydroxyvitamin D<sub>3</sub> to Regulate Cell Differentiation and Cell Cycle Arrest of Human Myeloblastic Leukemia Cells

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