Статті в журналах: "Leukemia inhibitory factor"

1

Nicola, Nicos A., and Jeffrey J. Babon. "Leukemia inhibitory factor (LIF)." Cytokine & Growth Factor Reviews 26, no. 5 (October 2015): 533–44. http://dx.doi.org/10.1016/j.cytogfr.2015.07.001.

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2

Metcalf, Donald. "The leukemia inhibitory factor (LIF)." International Journal of Cell Cloning 9, no. 2 (1991): 95–108. http://dx.doi.org/10.1002/stem.5530090201.

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3

Vanchieri, C. "Leukemia Inhibitory Factor Has Multiple Personalities." JNCI Journal of the National Cancer Institute 86, no. 4 (February 16, 1994): 262. http://dx.doi.org/10.1093/jnci/86.4.262.

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4

Hinds, Mark G., Till Maurer, Jian-Guo Zhang, Nicos A. Nicola, and Raymond S. Norton. "Solution Structure of Leukemia Inhibitory Factor." Journal of Biological Chemistry 273, no. 22 (May 29, 1998): 13738–45. http://dx.doi.org/10.1074/jbc.273.22.13738.

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5

Senturk, Levent M., and Aydin Arici. "Leukemia Inhibitory Factor in Human Reproduction." American Journal of Reproductive Immunology 39, no. 2 (February 1998): 144–51. http://dx.doi.org/10.1111/j.1600-0897.1998.tb00346.x.

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6

RAY, DAVID W., SONG-GUANG REN, and SHLOMO MELMED. "Leukemia Inhibitory Factor Regulates Proopiomelanocortin Transcriptiona." Annals of the New York Academy of Sciences 840, no. 1 (May 1998): 162–73. http://dx.doi.org/10.1111/j.1749-6632.1998.tb09560.x.

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7

Lass, Amir, Weishui Weiser, Alain Munafo, and Ernest Loumaye. "Leukemia inhibitory factor in human reproduction." Fertility and Sterility 76, no. 6 (December 2001): 1091–96. http://dx.doi.org/10.1016/s0015-0282(01)02878-3.

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8

Hilton, Douglas J., and Nicholas M. Gough. "Leukemia inhibitory factor: A biological perspective." Journal of Cellular Biochemistry 46, no. 1 (May 1991): 21–26. http://dx.doi.org/10.1002/jcb.240460105.

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9

Pepper, M. S., N. Ferrara, L. Orci, and R. Montesano. "Leukemia inhibitory factor (LIF) inhibits angiogenesis in vitro." Journal of Cell Science 108, no. 1 (January 1, 1995): 73–83. http://dx.doi.org/10.1242/jcs.108.1.73.

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Using an in vitro model in which endothelial cells can be induced to invade a three-dimensional collagen gel to form capillary-like tubular structures, we demonstrate that leukemia inhibitory factor (LIF) inhibits angiogenesis in vitro. The inhibitory effect was observed on both bovine aortic endothelial (BAE) and bovine microvascular endothelial (BME) cell, and occurred irrespective of the angiogenic stimulus, which included basic fibroblast growth factor (bFGF), vascular endothelial growth factor (VEGF), the synergistic effect of the two in combination, or the tumor promoter phorbol myristate acetate. LIF inhibited bFGF- and VEGF-induced proliferation in BAE and BME cells. In addition, LIF inhibited BAE but not BME cell migration in a conventional two-dimensional assay. Finally, LIF decreased the proteolytic activity of BAE and BME cells and increased their expression of plasminogen activator inhibitor-1. These results demonstrate that LIF inhibits angiogenesis in vitro, an effect that can be correlated with a LIF-mediated decrease in endothelial cell proliferation, migration and extracellular proteolysis.

10

Hanington, Patrick C., Shunmoogum A. Patten, Laura M. Reaume, Andrew J. Waskiewicz, Miodrag Belosevic, and Declan W. Ali. "Analysis of leukemia inhibitory factor and leukemia inhibitory factor receptor in embryonic and adult zebrafish (Danio rerio)." Developmental Biology 314, no. 2 (February 2008): 250–60. http://dx.doi.org/10.1016/j.ydbio.2007.10.012.

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11

Pehlivan, Melek, Ceyda Caliskan, Zeynep Yuce, and Hakkı Ogun Sercan. "Forced expression of Wnt antagonists sFRP1 and WIF1 sensitizes chronic myeloid leukemia cells to tyrosine kinase inhibitors." Tumor Biology 39, no. 5 (May 2017): 101042831770165. http://dx.doi.org/10.1177/1010428317701654.

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Chronic myeloid leukemia is a clonal myeloproliferative disorder that arises from the neoplastic transformation of the hematopoietic stem cell, in which the Wnt/β-catenin signaling pathway has been demonstrated to play an important role in disease progression. However, the role of Wnt signaling antagonists in therapy resistance and disease progression has not been fully investigated. We aimed to study the effects of Wnt/β-catenin pathway antagonists—secreted frizzled-related protein 1 and Wnt inhibitory factor 1—on resistance toward tyrosine kinase inhibitors in chronic myeloid leukemia. Response to tyrosine kinase inhibitors was analyzed in secreted frizzled-related protein 1 and Wnt inhibitory factor 1 stably transfected K562 cells. Experiments were repeated using a tetracycline-inducible expression system, confirming previous results. In addition, response to tyrosine kinase inhibitor treatment was also analyzed using the secreted frizzled-related protein 1 expressing, BCR-ABL positive MEG01 cell line, in the presence and absence of a secreted frizzled-related protein 1 inhibitor. Our data suggests that total cellular β-catenin levels decrease in the presence of secreted frizzled-related protein 1 and Wnt inhibitory factor 1, and a significant increase in cell death after tyrosine kinase inhibitor treatment is observed. On the contrary, when secreted frizzled-related protein 1 is suppressed, total β-catenin levels increase in the cell and the cells become resistant to tyrosine kinase inhibitors. We suggest that Wnt antagonists carry the potential to be exploited in designing new agents and strategies for the advanced and resistant forms of chronic myeloid leukemia.

12

Vernallis, Ann B., Keith R. Hudson, and John K. Heath. "An Antagonist for the Leukemia Inhibitory Factor Receptor Inhibits Leukemia Inhibitory Factor, Cardiotrophin-1, Ciliary Neurotrophic Factor, and Oncostatin M." Journal of Biological Chemistry 272, no. 43 (October 24, 1997): 26947–52. http://dx.doi.org/10.1074/jbc.272.43.26947.

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13

Metcalf, D. "The Unsolved Enigmas of Leukemia Inhibitory Factor." Stem Cells 21, no. 1 (January 1, 2003): 5–14. http://dx.doi.org/10.1634/stemcells.21-1-5.

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14

Gulluoglu, Sukru, Mesut Sahin, Emre Can Tuysuz, Cumhur Kaan Yaltirik, Aysegul Kuskucu, Ferda Ozkan, Fikrettin Sahin, Ugur Ture, and Omer Faruk Bayrak. "Leukemia Inhibitory Factor Promotes Aggressiveness of Chordoma." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 25, no. 7 (August 7, 2017): 1177–88. http://dx.doi.org/10.3727/096504017x14874349473815.

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15

AGHAJANOVA, LUSINE. "Leukemia Inhibitory Factor and Human Embryo Implantation." Annals of the New York Academy of Sciences 1034, no. 1 (December 2004): 176–83. http://dx.doi.org/10.1196/annals.1335.020.

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16

Metcalf, Donald. "Leukemia Inhibitory Factor—A Puzzling Polyfunctional Regulator." Growth Factors 7, no. 3 (January 1992): 169–73. http://dx.doi.org/10.3109/08977199209046921.

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17

GEARING, DAVID P. "Leukemia Inhibitory Factor: Does the Cap Fit?" Annals of the New York Academy of Sciences 628, no. 1 Negative Regu (July 1991): 9–18. http://dx.doi.org/10.1111/j.1749-6632.1991.tb17218.x.

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18

KURZROCK, RAZELLE, ZEEV ESTROV, MEIR WETZLER, JORDAN U. GUTTERMAN, and OSHE MTALPAZ. "LIF: Not Just a Leukemia Inhibitory Factor*." Endocrine Reviews 12, no. 3 (August 1991): 208–17. http://dx.doi.org/10.1210/edrv-12-3-208.

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19

Cornish, J., K. E. Callon, S. G. Edgar, and I. R. Reid. "Leukemia inhibitory factor is mitogenic to osteoblasts." Bone 21, no. 3 (September 1997): 243–47. http://dx.doi.org/10.1016/s8756-3282(97)00144-0.

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20

Tran, Ami, Kalman Kovacs, Lucia Stefaneanu, George Kontogeorgos, Bernd W. Scheithauer, and Shlomo Melmed. "Expression of leukemia inhibitory factor in craniopharyngioma." Endocrine Pathology 10, no. 2 (June 1999): 103–8. http://dx.doi.org/10.1007/bf02739822.

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21

Waring, Paul M., Roberto Romero, Nihay Laham, Ricardo Gomez, and Gregory E. Rice. "Leukemia inhibitory factor: Association with intraamniotic infection." American Journal of Obstetrics and Gynecology 171, no. 5 (November 1994): 1335–41. http://dx.doi.org/10.1016/0002-9378(94)90157-0.

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22

Weber, Marietta A., Silvia Schnyder-Candrian, Bruno Schnyder, Valerie Quesniaux, Valeria Poli, Colin L. Stewart, and Bernhard Ryffel. "Endogenous leukemia inhibitory factor attenuates endotoxin response." Laboratory Investigation 85, no. 2 (December 20, 2004): 276–84. http://dx.doi.org/10.1038/labinvest.3700216.

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23

Lemons, Angela R., and Rajesh K. Naz. "Birth control vaccine targeting leukemia inhibitory factor." Molecular Reproduction and Development 79, no. 2 (December 2, 2011): 97–106. http://dx.doi.org/10.1002/mrd.22002.

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24

Hanson, J. M., J. A. Mol, and B. P. Meij. "Expression of leukemia inhibitory factor and leukemia inhibitory factor receptor in the canine pituitary gland and corticotrope adenomas." Domestic Animal Endocrinology 38, no. 4 (May 2010): 260–71. http://dx.doi.org/10.1016/j.domaniend.2009.11.005.

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25

Na, Bon Hyang, Thi Xoan Hoang та Jae Young Kim. "Hsp90 Inhibition Reduces TLR5 Surface Expression and NF-κB Activation in Human Myeloid Leukemia THP-1 Cells". BioMed Research International 2018 (2018): 1–8. http://dx.doi.org/10.1155/2018/4319369.

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Tumors highly express active heat shock protein 90 (Hsp90), which is involved in tumor survival and progression. Enhanced Toll-like receptor (TLR) 5 expression and signaling were reported to be associated with acute myeloid leukemia. In the present study, we investigated the possible modulatory effects of Hsp90 inhibitors on TLR5 expression and signaling in the human myeloid leukemia cell line THP-1. Cells were pretreated with various concentrations of the Hsp90 inhibitor geldanamycin (GA) or the Hsp70 inhibitor VER155008, followed by stimulation with bacterial flagellin. Flagellin-induced nuclear factor-κB (NF-κB) activation was significantly reduced by treatment with GA or VER155008. To elucidate the underlying mechanism of this effect, mRNA and cell surface expression of TLR5 was examined. TLR5 mRNA expression was enhanced by both GA and VER155008, whereas cell surface expression of TLR5 was reduced by three different Hsp90 inhibitors, including GA, 17-(allylamino)-17-demethoxygeldanamycin, and radicicol, and an Hsp70 inhibitor. The inhibitory effect of Hsp90 inhibitors was much higher than that of Hsp70 inhibitor. Our results suggest that Hsp90 inhibitors suppress TLR5 surface expression and activation of NF-κB in THP-1 cells in response to TLR5 ligand, and these inhibitory effects may be associated with the possible mechanisms by which Hsp90 inhibitors suppress myeloid leukemia.

26

Auernhammer, C. J., and S. Melmed. "Leukemia-Inhibitory Factor—Neuroimmune Modulator of Endocrine Function*." Endocrine Reviews 21, no. 3 (June 1, 2000): 313–45. http://dx.doi.org/10.1210/edrv.21.3.0400.

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Abstract Leukemia-inhibitory factor (LIF) is a pleiotropic cytokine expressed by multiple tissue types. The LIF receptor shares a common gp130 receptor subunit with the IL-6 cytokine superfamily. LIF signaling is mediated mainly by JAK-STAT (janus-kinase-signal transducer and activator of transcription) pathways and is abrogated by the SOCS (suppressor-of cytokine signaling) and PIAS (protein inhibitors of activated STAT) proteins. In addition to classic hematopoietic and neuronal actions, LIF plays a critical role in several endocrine functions including the utero-placental unit, the hypothalamo-pituitary-adrenal axis, bone cell metabolism, energy homeostasis, and hormonally responsive tumors. This paper reviews recent advances in our understanding of molecular mechanisms regulating LIF expression and action and also provides a systemic overview of LIF-mediated endocrine regulation. Local and systemic LIF serve to integrate multiple developmental and functional cell signals, culminating in maintaining appropriate hormonal and metabolic homeostasis. LIF thus functions as a critical molecular interface between the neuroimmune and endocrine systems.

27

Okabe, M., Y. Kuni-eda, T. Sugiwura, M. Tanaka, T. Miyagishima, I. Saiki, T. Minagawa, M. Kurosawa, T. Itaya, and T. Miyazaki. "Inhibitory effect of interleukin-4 on the in vitro growth of Ph1- positive acute lymphoblastic leukemia cells." Blood 78, no. 6 (September 15, 1991): 1574–80. http://dx.doi.org/10.1182/blood.v78.6.1574.1574.

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Abstract We investigated the effect of recombinant human interleukin-4 (rhIL-4) on the in vitro growth of human leukemia cells in liquid culture and 3H- thymidine incorporation and found inhibitory effects on the growth of leukemic cells from patients with Ph1-positive acute lymphoblastic leukemia (Ph1 ALL) and three Ph1 ALL cell lines. However, no inhibitory effects were seen in Ph1-positive leukemic cell lines derived from patients with chronic myelogenous leukemia in blast crisis and various types of Ph1-negative leukemia cells, including B-lineage leukemia cells. In a flow cytometry assay of IL-4 receptor (IL-4R), all three Ph1-positive ALL cell lines showed the presence of IL-4R on their cell surfaces, and the IL-4-dependent inhibition on the growth of Ph1- positive ALL cells was abrogated by the addition of either monoclonal or polyclonal antibodies against rhIL-4. Other cytokines, including IL- 2, IL-3, granulocyte-macrophage colony-stimulating factor (CSF), granulocyte-CSF, and IL-6, showed no inhibitory effects on the growth of Ph1-ALL cells, but tumor necrosis factor-alpha (TNF-alpha) and interferon (IFN)-alpha, -beta, and -gamma displayed slight inhibitory effects in a high concentration. The growth inhibition induced by rhIL- 4 in the Ph1-positive ALL cells was not abrogated by the addition of antibodies against either IFN-gamma or TNF-alpha. Furthermore, these cells showed no significant production of IFN-alpha, -beta, or -gamma or TNF-alpha after exposure to rhIL-4, thus indicating that the growth inhibition of Ph1-positive ALL cells by rhIL-4 is not associated with IL-4-stimulating production of these factors. rhIL-4 caused significant inhibition of the tyrosine kinase activity in these Ph1-positive ALL cells, similar to Herbimycin A, an inhibitor of tyrosine kinase that inhibited the tyrosine kinase activity in these cells. Our finding suggests that the clinical evaluation of rhIL-4 may offer promising therapeutic possibilities for patients with Ph1-positive ALL.

28

Okabe, M., Y. Kuni-eda, T. Sugiwura, M. Tanaka, T. Miyagishima, I. Saiki, T. Minagawa, M. Kurosawa, T. Itaya, and T. Miyazaki. "Inhibitory effect of interleukin-4 on the in vitro growth of Ph1- positive acute lymphoblastic leukemia cells." Blood 78, no. 6 (September 15, 1991): 1574–80. http://dx.doi.org/10.1182/blood.v78.6.1574.bloodjournal7861574.

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We investigated the effect of recombinant human interleukin-4 (rhIL-4) on the in vitro growth of human leukemia cells in liquid culture and 3H- thymidine incorporation and found inhibitory effects on the growth of leukemic cells from patients with Ph1-positive acute lymphoblastic leukemia (Ph1 ALL) and three Ph1 ALL cell lines. However, no inhibitory effects were seen in Ph1-positive leukemic cell lines derived from patients with chronic myelogenous leukemia in blast crisis and various types of Ph1-negative leukemia cells, including B-lineage leukemia cells. In a flow cytometry assay of IL-4 receptor (IL-4R), all three Ph1-positive ALL cell lines showed the presence of IL-4R on their cell surfaces, and the IL-4-dependent inhibition on the growth of Ph1- positive ALL cells was abrogated by the addition of either monoclonal or polyclonal antibodies against rhIL-4. Other cytokines, including IL- 2, IL-3, granulocyte-macrophage colony-stimulating factor (CSF), granulocyte-CSF, and IL-6, showed no inhibitory effects on the growth of Ph1-ALL cells, but tumor necrosis factor-alpha (TNF-alpha) and interferon (IFN)-alpha, -beta, and -gamma displayed slight inhibitory effects in a high concentration. The growth inhibition induced by rhIL- 4 in the Ph1-positive ALL cells was not abrogated by the addition of antibodies against either IFN-gamma or TNF-alpha. Furthermore, these cells showed no significant production of IFN-alpha, -beta, or -gamma or TNF-alpha after exposure to rhIL-4, thus indicating that the growth inhibition of Ph1-positive ALL cells by rhIL-4 is not associated with IL-4-stimulating production of these factors. rhIL-4 caused significant inhibition of the tyrosine kinase activity in these Ph1-positive ALL cells, similar to Herbimycin A, an inhibitor of tyrosine kinase that inhibited the tyrosine kinase activity in these cells. Our finding suggests that the clinical evaluation of rhIL-4 may offer promising therapeutic possibilities for patients with Ph1-positive ALL.

29

LI, Yong, Lizhou SUN, Denmei ZHAO, Jun OUYANG, and Mei XIANG. "Aberrant expression of leukemia inhibitory factor receptor (LIFR) and leukemia inhibitory factor (LIF) is associated with tubal pregnancy occurrence." TURKISH JOURNAL OF MEDICAL SCIENCES 45 (2015): 214–20. http://dx.doi.org/10.3906/sag-1307-103.

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30

Wysoczynski, Marcin, Katarzyna Miekus, Kacper Jankowski, Jens Wanzeck, Salvatore Bertolone, Anna Janowska-Wieczorek, Janina Ratajczak, and Mariusz Z. Ratajczak. "Leukemia Inhibitory Factor: A Newly Identified Metastatic Factor in Rhabdomyosarcomas." Cancer Research 67, no. 5 (March 1, 2007): 2131–40. http://dx.doi.org/10.1158/0008-5472.can-06-1021.

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31

Reinart, Nina, Malgorzata Ciesla, Cornelia Rudolph, Astrid Stein, Guenter Krause, Brigitte Schlegelberger, Michael Hallek, and Guenter Fingerle-Rowson. "Macrophage Migration Inhibitory Factor (MIF) Promotes the Development of Murine Chronic Lymphocytic Leukemia (CLL)." Blood 112, no. 11 (November 16, 2008): 27. http://dx.doi.org/10.1182/blood.v112.11.27.27.

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Abstract Introduction: Tumor formation results from a complex interplay between genetic/epigenetic alterations, cell cycle dysregulation and promotion by the tumor environment. Stimulation by extracellular survival factors is important for chronic lymphocytic leukemia (CLL), since the leukemic cells undergo spontaneous apoptosis when removed from their normal milieu. Since preliminary experiments demonstrated that macrophage migration inhibitory factor (MIF), a chemokine-like proinflammatory mediator and an intracellular regulator of growth and apoptosis, is overexpressed in human CLL, we investigated whether MIF participates in the pathogenesis of murine CLL. Methods: We studied the role of MIF in CLL by crossing the Eμ-TCL1-transgenic mouse model with MIF knockout (MIF−/−) mice. B-cell-specific overexpression of T cell leukemia-1 (TCL1) leads to accumulation and proliferation of IgM+/CD5+ mature B-cells via activation of AKT. This results in a CLL-like disease with peripheral lymphocytic leukemia, lymphadenopathy, splenomegaly, BM infiltration and premature death after 8–15 months. TCL1+/wtMIF−/− and TCL1+/wtMIF+/+ mice were compared with respect to leukemia development, tumor burden, cytogenetics and survival. Results: The MIF receptors CD74/CD44 and CXCR2 are expressed on murine B-cells. TCL1+/wtMIF+/+ mice exhibited increased numbers of IgM+/CD5+ B-cells already in the preleukemic phase at month 3 and developed overt leukemia (WBC > 20G/l) 3 months earlier than their MIF−/− counterparts (p = 0.02). Leukemia load at 12 months of age as measured by hepatosplenomegaly was increased in TCL1+/wtMIF+/+ animals and lymphatic organs were densely infiltrated by small, mature lymphocytes. The accelerated disease progression in the presence of MIF translated into a median survival which was 60 days shorter than in the absence of MIF (TCL1+/wtMIF+/+ 400 days, TCL1+/wtMIF−/− 460 days, p = 0.04). SKY analysis in leukemic splenocytes yielded various complex genetic aberrations with trisomies (e.g. +15), tetraploidy, translocations and deletions. Overexpression of tp53 due to the presence of an inactivating mutation in the p53 gene was found more frequently in TCL1+/wtMIF+/+ than in TCL1+/wtMIF−/− animals. Although the rates of DNA-damage-induced apoptosis in pre-leukemic and leukemic mice ex vivo were not significantly different between the genotypes, this defect in the p53-dependent apoptosis pathway corresponded with a reduced rate of spontaneous apoptosis in spleens of leukemic TCL1+/wtMIF+/+ animals. Conclusions: Our experience with the Eμ-TCL-1-transgenic mice shows that this model is suitable for the identification of novel regulators of CLL-like disease. We provide genetic proof that MIF acts to promote the early preleukemic and the leukemic phase of TCL1-induced CLL and thereby identify MIF as a novel regulator of CLL pathogenesis. Ongoing efforts are focussing on further characterizing the differences in pathology, the activation of the AKT pathway and cell cycle control between TCL1+/wtMIF−/− and TCL1+/wtMIF+/+ mice.

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Uno, Kanako, Takeshi Inukai, Nobuhiko Kayagaki, Kumiko Goi, Hiroki Sato, Atsushi Nemoto, Kazuya Takahashi, et al. "TNF-related apoptosis-inducing ligand (TRAIL) frequently induces apoptosis in Philadelphia chromosome–positive leukemia cells." Blood 101, no. 9 (May 1, 2003): 3658–67. http://dx.doi.org/10.1182/blood-2002-06-1770.

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Tumor necrosis factor (TNF)–related apoptosis-inducing ligand (TRAIL) and Fas ligand (FasL) have been implicated in antitumor immunity and therapy. In the present study, we investigated the sensitivity of Philadelphia chromosome (Ph1)–positive leukemia cell lines to TRAIL- or FasL-induced cell death to explore the possible contribution of these molecules to immunotherapy against Ph1-positive leukemias. TRAIL, but not FasL, effectively induced apoptotic cell death in most of 5 chronic myelogenous leukemia–derived and 7 acute leukemia–derived Ph1-positive cell lines. The sensitivity to TRAIL was correlated with cell-surface expression of death-inducing receptors DR4 and/or DR5. The TRAIL-induced cell death was caspase-dependent and enhanced by nuclear factor κB inhibitors. Moreover, primary leukemia cells from Ph1-positive acute lymphoblastic leukemia patients were also sensitive to TRAIL, but not to FasL, depending on DR4/DR5 expression. Fas-associated death domain protein (FADD) and caspase-8, components of death-inducing signaling complex (DISC), as well as FLIP (FLICE [Fas-associating protein with death domain–like interleukin-1–converting enzyme]/caspase-8 inhibitory protein), a negative regulator of caspase-8, were expressed ubiquitously in Ph1-positive leukemia cell lines irrespective of their differential sensitivities to TRAIL and FasL. Notably, TRAIL could induce cell death in the Ph1-positive leukemia cell lines that were refractory to a BCR-ABL–specific tyrosine kinase inhibitor imatinib mesylate (STI571; Novartis Pharma, Basel, Switzerland). These results suggested the potential utility of recombinant TRAIL as a novel therapeutic agent and the possible contribution of endogenously expressed TRAIL to immunotherapy against Ph1-positive leukemias.

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Yokoyama, A., J. Okabe-Kado, A. Sakashita, N. Maseki, Y. Kaneko, K. Hino, S. Tomoyasu, N. Tsuruoka, T. Kasukabe, and Y. Honma. "Differentiation inhibitory factor nm23 as a new prognostic factor in acute monocytic leukemia." Blood 88, no. 9 (November 1, 1996): 3555–61. http://dx.doi.org/10.1182/blood.v88.9.3555.bloodjournal8893555.

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Differentiation inhibitory factor (nm23 protein) inhibited the induction of differentiation of mouse myeloid leukemia M1 and WEHI-3BD+ and human erythroleukemia HEL, KU812, and K562 cells. Block of differentiation may be associated with the aggressive behavior of leukemia. To examine the role of nm23 in human myeloid leukemia, we investigated the relative levels of nm23-H1, nm23-H2, and c-myc transcripts in 42 patients with acute myelogenous leukemia (AML), and in 5 with chronic myelogenous leukemia at chronic phase by reverse transcriptase polymerase chain reaction. The expression of nm23-H1 and -H2 but not of c-myc in AML was significantly higher than that in normal blood cells. Among AMLs, acute monocytic leukemia (presentation with AML-M5 morphology) was especially associated with elevated nm23-H1 and -H2 mRNA levels. On the other hand, the elevated levels of c-myc expression in AML-M5 were less evident. An analysis of correlation between nm23 expression and clinicopathological parameters showed that resistance to initial chemotherapy is associated with increased nm23-H1 mRNA levels and that a high initial white blood cell count is associated with increased nm23-H2 mRNA levels. Elevated nm23-H1 mRNA levels were associated with significantly reduced the overall survival of AML, especially of AML-M5 patients. The present results indicate that nm23-H1 and -H2 are overexpressed in AML and especially nm23-H1 gene expression predicts the prognosis of AML, especially of AML-M5.

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Conover, J. C., N. Y. Ip, W. T. Poueymirou, B. Bates, M. P. Goldfarb, T. M. DeChiara, and G. D. Yancopoulos. "Ciliary neurotrophic factor maintains the pluripotentiality of embryonic stem cells." Development 119, no. 3 (November 1, 1993): 559–65. http://dx.doi.org/10.1242/dev.119.3.559.

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Ciliary neurotrophic factor was discovered based on its ability to support the survival of ciliary neurons, and is now known to act on a variety of neuronal and glial populations. Two distant relatives of ciliary neurotrophic factor, leukemia inhibitory factor and oncostatin M, mimic ciliary neurotrophic factor with respect to its actions on cells of the nervous system. In contrast to ciliary neurotrophic factor, leukemia inhibitory factor and oncostatin M also display a broad array of actions on cells outside of the nervous system. The overlapping activities of leukemia inhibitory factor, oncostatin M and ciliary neurotrophic factor can be attributed to shared receptor components. The specificity of ciliary neurotrophic factor for cells of the nervous system results from the restricted expression of the alpha component of the ciliary neurotrophic factor receptor complex, which is required to convert a functional leukemia inhibitory factor/oncostatin M receptor complex into a ciliary neurotrophic factor receptor complex. The recent observation that the alpha component of the ciliary neurotrophic factor receptor complex is expressed by very early neuronal precursors suggested that ciliary neurotrophic factor may act on even earlier precursors, particularly on cells previously thought to be targets for leukemia inhibitory factor action. Here we show the first example of ciliary neurotrophic factor responsiveness in cells residing outside of the nervous system by demonstrating that embryonic stem cells express a functional ciliary neurotrophic factor receptor complex, and that ciliary neurotrophic factor is similar to leukemia inhibitory factor in its ability to maintain the pluripotentiality of these cells.

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Park, Hye-Rin, Hee-Jung Choi, Bo-Sung Kim, Tae-Wook Chung, Keuk-Jun Kim, Jong-Kil Joo, Dongryeol Ryu, Sung-Jin Bae, and Ki-Tae Ha. "Paeoniflorin Enhances Endometrial Receptivity through Leukemia Inhibitory Factor." Biomolecules 11, no. 3 (March 16, 2021): 439. http://dx.doi.org/10.3390/biom11030439.

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Despite advances in assisted reproductive technology, treatment for deficient endometrial receptivity is a major clinical unmet need. In our previous study, the water extract of Paeonia lactiflora Pall. enhanced endometrial receptivity in vitro and in vivo via induction of leukemia inhibitory factor (LIF), an interleukin (IL)-6 family cytokine. In the present study, we found that paeoniflorin, a monoterpene glycoside, is the major active compound of P. lactiflora. Paeoniflorin significantly improved the embryo implantation rate in a murine model of mifepristone (RU486)-induced implantation failure. In addition, paeoniflorin increased the adhesion of human trophectoderm-derived JAr cells to endometrial Ishikawa cells through the expression of LIF in vitro. Moreover, using the National Center for Biotechnology Information (NCBI) Gene Expression Omnibus (GEO) database of the human endometrium, we confirmed that LIF signaling is a key regulator for improving human endometrial receptivity. Therefore, these results suggest that paeoniflorin might be a potent drug candidate for the treatment of endometrial implantation failure by enhancing endometrial receptivity.

36

Estrov, Zeev, Moshe Talpaz, Meir Wetzler, and Razelle Kurzrock. "The Modulatory Hematopoietic Activities of Leukemia Inhibitory Factor." Leukemia & Lymphoma 8, no. 1-2 (January 1992): 1–7. http://dx.doi.org/10.3109/10428199209049811.

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37

REID, I. R., C. LOWE, J. CORNISH, S. J. M. SKINNER, D. J. HILTON, T. A. WILLSON, D. P. GEARING, and T. J. MARTIN. "Leukemia Inhibitory Factor: A Novel Bone-Active Cytokine*." Endocrinology 126, no. 3 (March 1990): 1416–20. http://dx.doi.org/10.1210/endo-126-3-1416.

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38

Knight, D., and T. Bai. "Roles for leukemia inhibitory factor in lung biology." Drug News & Perspectives 12, no. 5 (1999): 261. http://dx.doi.org/10.1358/dnp.1999.12.5.863620.

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39

Auernhammer, C. J. "Leukemia-Inhibitory Factor--Neuroimmune Modulator of Endocrine Function." Endocrine Reviews 21, no. 3 (June 1, 2000): 313–45. http://dx.doi.org/10.1210/er.21.3.313.

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40

van den Bent, Martin J. "Prevention of Chemotherapy-Induced Neuropathy: Leukemia Inhibitory Factor." Clinical Cancer Research 11, no. 5 (March 1, 2005): 1691–93. http://dx.doi.org/10.1158/1078-0432.ccr-05-0079.

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41

Ishizaki, Seiji, Takashi Murase, Yoshihisa Sugimura, Ryoichi Banno, Hiroshi Arima, Yoshitaka Miura, and Yutaka Oiso. "Leukemia inhibitory factor stimulates vasopressin release in rats." Neuroscience Letters 359, no. 1-2 (April 2004): 77–80. http://dx.doi.org/10.1016/j.neulet.2004.02.019.

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42

McCoy, A. J., V. Staton, A. Van Donkelaar, J. N. Varghese, and P. M. Colman. "X-ray crystallographic studies of leukemia inhibitory factor." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (August 21, 1993): c113. http://dx.doi.org/10.1107/s0108767378096750.

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43

Gearing, David P. "Molecular characterization of the leukemia inhibitory factor receptor." Fresenius' Journal of Analytical Chemistry 343, no. 1 (1992): 14–15. http://dx.doi.org/10.1007/bf00331947.

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44

Cornish, J., C. Lowe, S. J. M. Skinner, D. J. Hilton, T. A. Willson, D. P. Gearing, T. J. Martin, and I. R. Reid. "Leukemia inhibitory factor: A novel bone-active cytokine." Bone and Mineral 10, no. 3 (September 1990): S290. http://dx.doi.org/10.1016/0169-6009(90)90322-7.

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45

Liu, Shu-Chen, and Yu-Sun Chang. "Role of leukemia inhibitory factor in nasopharyngeal carcinogenesis." Molecular & Cellular Oncology 1, no. 1 (January 2014): e29900. http://dx.doi.org/10.4161/mco.29900.

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46

Villiger, P. M., Y. Geng, and M. Lotz. "Induction of cytokine expression by leukemia inhibitory factor." Journal of Clinical Investigation 91, no. 4 (April 1, 1993): 1575–81. http://dx.doi.org/10.1172/jci116363.

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47

Marshall, Jean S., Jack Gauldie, Laurie Nielsen, and John Bienenstock. "Leukemia inhibitory factor production by rat mast cells." European Journal of Immunology 23, no. 9 (September 1993): 2116–20. http://dx.doi.org/10.1002/eji.1830230911.

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48

Lowe, Carolyn, Jill Cornish, Karon Callon, John T. Martin, and Ian R. Reid. "Regulation of osteoblast proliferation by leukemia inhibitory factor." Journal of Bone and Mineral Research 6, no. 12 (December 3, 2009): 1277–83. http://dx.doi.org/10.1002/jbmr.5650061203.

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49

Yue, Zhan-Peng, Zeng-Ming Yang, Peng Wei, Shi-Jie Li, Hong-Bin Wang, Jing-He Tan, and Michael J. K. Harper. "Leukemia Inhibitory Factor, Leukemia Inhibitory Factor Receptor, and Glycoprotein 130 in Rhesus Monkey Uterus During Menstrual Cycle and Early Pregnancy1." Biology of Reproduction 63, no. 2 (August 1, 2000): 508–12. http://dx.doi.org/10.1095/biolreprod63.2.508.

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50

Patterson, B., A. Tjernlund, and J. Andersson. "Endogenous Inhibitors of HIV: Potent Anti-HIV Activity of Leukemia Inhibitory Factor." Current Molecular Medicine 2, no. 8 (December 1, 2002): 713–22. http://dx.doi.org/10.2174/1566524023361817.

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