Role of the p70 S6 kinase cascade in neutrophilic differentiation and proliferation of HL-60 cells—a study of transferrin receptor-positive and -negative cells obtained from dimethyl sulfoxide- or retinoic acid-treated HL-60 cells

Kanayasu-Toyoda, Toshie; Yamaguchi, Teruhide; Oshizawa, Tadashi; Kogi, Mieko; Uchida, Eiji; Hayakawa, Tetsuo

doi:10.1016/s0003-9861(02)00330-2

Cited by 11 publications

(19 citation statements)

References 43 publications

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“…In addition the intensive cytoplasmic and nuclear staining of S6K2 was demonstrated in tumor samples but not in normal tissue. Collectively these data indicate that S6K is involved in the process of cell transformation accompanied by cell dedifferentiation and invasion [36].…”

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confidence: 76%

Subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in primary monolayer culture of rat thyrocytes

2008

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The main aim of this work was to determine subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in the primary monolayer culture of thyrocytes obtained from undamaged follicles. In the thyroid follicles S6K1, S6K2 have been detected predominantly in the cytoplasm of the cells, however, in the monolayer culture of thyrocytes in the course of follicles outspreading S6K1 and S6K2 have been observed in nuclei as well. Such redistribution of S6K was not directly related to the appearance of proliferating Ki-67 positive cells. At the same time there was a correlation between the appearance of S6K1, S6K2 positive nuclei in monolayer thyrocyte culture and decrease in thyroglobulin content in cultured cells. Thus, the obtained results indicated that the down regulation of thyrocyte functional activity caused by the loss of follicle organization was accompanied by subcellular redistribution of S6K1 and S6K2.

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confidence: 76%

Subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in primary monolayer culture of rat thyrocytes

2008

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“…Furthermore, inhibition of mTORC1 by rapamycin alone can promote the differentiation of several myeloid leukemia cell lines, 75 and enhances differentiation in the myeloid leukemia-derived HL-60 cell line in concert with DMSO, G-CSF, 76 or with all-transretinoic acid (ATRA). 77 Subsequently Kanayasu-Toyoda et al showed that rapamycin reduced expression of c-MYC in the HL-60 cells demonstrating enhanced differentiation. 78 Importantly, MPRO cells are immortalized promyelocytes derived from normal murine bone marrow that undergo more complete differentiation in response to retinoids, 79 extending the relevance of mTORC1-dependent regulation of differentiation to nontransformed cells.…”

Section: Discussionmentioning

confidence: 99%

Translational control of c-MYC by rapamycin promotes terminal myeloid differentiation

Wall

Poortinga

Hannan

et al. 2008

Blood

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IntroductionThe bHLH-LZ transcription factor c-MYC acts in a gene-specific manner by binding consensus E-box motifs in target genes to activate transcription 1-6 and generally to influence chromatin structure, 7-9 resulting in master regulation of key biologic processes including differentiation, proliferation, and apoptosis. Unsurprisingly, the consequences of dysregulated c-MYC expression are profound: loss of c-MYC expression in knockout mice is embryonically lethal 10 and overexpression of c-MYC in mouse models results in malignant transformation. [11][12][13][14][15][16] In addition, overexpression of c-MYC is observed in many forms of human cancer as a result of chromosomal translocations, gene amplification, altered protein stability, or other ill-defined mechanisms. [17][18][19] An increasingly recognized function of MYC is the ability to drive cell growth by regulating a subset of genes critical for cellular metabolism, macromolecular (RNA and protein) synthesis, and protein turnover. 20-23 c-MYC has been shown to regulate RNA polymerase II-dependent synthesis of ribosomal proteins 20,23,24 and RNA polymerase III-dependent synthesis of 5S rRNA and tRNAs, 25 and more recently we and others have linked it to RNA polymerase I-dependent transcription, [26][27][28][29] resulting in the coordinate upregulation of ribosome biogenesis that is required for growth. A key feature of the growth-promoting role of c-MYC is its ability to act in concert with the PI3K/AKT/mTORC1 signal transduction pathway not only to coordinate ribosome biogenesis but also via modulation of ribosome function to promote its own expression.The mTORC1 complex represents a vital downstream node in the PI3K/AKT signal transduction pathway for matching rates of protein synthesis to nutrient availability. 30,31 Under favorable energy conditions, signaling through mTORC1 contributes to ribosome biogenesis by improving the efficiency with which mRNAs containing a 5Ј TOP (terminal oligopyrimidine tract) are translated. 32-34 mTORC1 also drives rDNA transcription via phosphorylation of S6 kinase 1 and subsequent downstream signaling to UBF. 35 In addition, phosphorylation of another mTORC1 substrate, 4EBP1, releases eIF4E from inhibitory binding by 4EBP1 allowing eIF4E to participate in a fully competent translation initiation complex. In turn, this permits the cap-dependent translation of a subset of mRNAs containing a complex secondary structure in the 5Ј UTR region that is weakly translated when the activity of the PI3K pathway is suboptimal. 36 This subset of mRNAs with a complex 5Ј UTR includes c-Myc and other growth-and cell cycle-related transcripts such as ornithine decarboxylase (Odc) and cyclin D1. 37 The macrolide antibiotic rapamycin is a potent mTORC1 inhibitor. Rapamycin and its analogues act in complex with the immunophilin FK506-binding protein 12 (FKB12), to bind and selectively inhibit mTORC1 activity and therefore limit ribosome numbers and function. [38][39][40][41] Terminal myeloid differentiation (TMD) is the process b...

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“…The role of S6K in differentiation was studied previously on neural cells, neutrophiles and other types of cells [18,19]. It was shown that suppression of S6K1 delays the differentiation of neural cells.…”

Section: Methodsmentioning

confidence: 99%

Subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in rat thyrocytes under conditions of two- and three-dimensional culture

2008

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The aim of this work was to study the link between activation of processes of migration, proliferation, loss of thyrocyte follicle organization at different culture conditions and subcellular localization of S6K1/2. The subcellular redistribution of S6K1/2 takes place in the rat thyrocyte monolayer culture where S6K1/2 was detected not only in the cytoplasm but in the nuclei of cells as well|. In addition, the content of S6K1/2 in proliferating cells was increased. The subcellular| localization of S6K1/2 in thyrocytes cultivated as follicles was similar to that observed in normal thyroid tissue. Subcellular relocalization of S6K1/2 was detected only in certain cellular population, which for some reasons lost follicle organization and, consequently, functional activity. Thus, the changes in subcellular localization of S6K1/2 in cultivated thyrocytes are directly related to the level of differentiation, unlike proliferation and migration of these cells.

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Role of the p70 S6 kinase cascade in neutrophilic differentiation and proliferation of HL-60 cells—a study of transferrin receptor-positive and -negative cells obtained from dimethyl sulfoxide- or retinoic acid-treated HL-60 cells

Cited by 11 publications

References 43 publications

Subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in primary monolayer culture of rat thyrocytes

Subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in primary monolayer culture of rat thyrocytes

Translational control of c-MYC by rapamycin promotes terminal myeloid differentiation

Subcellular localization of S6K1 and S6K2 forms of ribosomal protein S6 kinase in rat thyrocytes under conditions of two- and three-dimensional culture

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