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Journal articles on the topic 'Oncogene expression'

Author: Grafiati
Published: 4 June 2021
Last updated: 3 February 2022

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1

Ito, Reina E., Chitose Oneyama, and Kazuhiro Aoki. "Oncogenic mutation or overexpression of oncogenic KRAS or BRAF is not sufficient to confer oncogene addiction." PLOS ONE 16, no. 4 (April 1, 2021): e0249388. http://dx.doi.org/10.1371/journal.pone.0249388.

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Oncogene addiction is a cellular property by which cancer cells become highly dependent on the expression of oncogenes for their survival. Oncogene addiction can be exploited to design molecularly targeted drugs that kill only cancer cells by inhibiting the specific oncogenes. Genes and cell lines exhibiting oncogene addiction, as well as the mechanisms by which cell death is induced when addicted oncogenes are suppressed, have been extensively studied. However, it is still not fully understood how oncogene addiction is acquired in cancer cells. Here, we take a synthetic biology approach to investigate whether oncogenic mutation or oncogene expression suffices to confer the property of oncogene addiction to cancer cells. We employed human mammary epithelium-derived MCF-10A cells expressing the oncogenic KRAS or BRAF. MCF-10A cells harboring an oncogenic mutation in a single-allele of KRAS or BRAF showed weak transformation activity, but no characteristics of oncogene addiction. MCF-10A cells overexpressing oncogenic KRAS demonstrated the transformation activity, but MCF-10A cells overexpressing oncogenic BRAF did not. Neither cell line exhibited any oncogene addiction properties. These results indicate that the introduction of oncogenic mutation or the overexpression of oncogenes is not sufficient for cells to acquire oncogene addiction, and that oncogene addiction is not associated with transformation activity.
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2

Shestakova, E. A. "HOX GENE EXPRESSION IN HUMAN B-CELL PROGENITOR LEUKEMIA CELL LINES EXPRESSING E2A-PBX1 ONCOGENE." Russian Journal of Biotherapy 19, no. 1 (March 22, 2020): 89–95. http://dx.doi.org/10.17650/1726-9784-2019-19-1-89-95.

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Introduction. Acute lymphoblastic leukemia (ALL) is diagnosed mainly in children (2/3 of diseases) making this type of leukemia one of the most common oncological diseases among children. Oncogenes are involved in the development of ALL, in particular the product of chromosomes 1 and 19 translocation, the oncogene E2A-PBX1 that codes for E2A-PBX1 chimeric oncoprotein with strong transcription activation properties as well as oncogenes of HOX family, mainly HOXA and HOXB cluster genes. E2A-PBX1 chimeric oncoprotein and НОХА proteins are associated in vivo with factors participating in epigenetic regulation of gene expression such as chromatin modifying and remodeling enzymes that partially determines their oncogenic properties. In previous studies we obtained data indicating genetic interactions of E2A-PBX1 and НОХ genes participating in leukemia development.The aim of this research was to confirm the role of Е2А – РВХ1 oncogene in the activation of the expression of НОХА cluster genes coding for the proteins with high oncogenic potential.Materials and methods. The objects of the study were four B cell progenitor (pre-B) leukemia cell lines: RCH-ACV, KASUMI-2, 697 and NALM-6. Standard polymerase chain reaction (PCR) was used for the identification of chromosome 1 and 19 translocation product, E2A-PBX1 oncogene and its expression. Method of reverse transcription coupled with quantitative polymerase chain reaction (Q-RT-PCR) was used for the analysis of 11 HOXA cluster genes expression.Results. It is demonstrated that E2A-PBX1 oncogene is present and expressed in three studied human pre-B leukemia cell lines, RCH-ACV, KASUMI-2 and 697, while its expression is absent in NALM-6 cell line. High expression of 7 from 11 HOXА cluster genes is revealed in RCH-ACV, KASUMI-2 and 697 cell lines expressing E2A-PBX1 oncogene, whereas NALM-6 cell line, that does not express E2A-PBX1 oncogene, also does not express HOXA genes except low expression of two genes from this cluster.Conclusions. The data obtained in this study demonstrate that RCH-ACV, KASUMI-2 and 697 human leukemia pre-B cell lines, containing and expressing Е2А-РВХ1 oncogene, also express most of HOXA genes (7 genes of 11 genes) at high level in contrast to control NALM-6 cell line that does not comprise Е2А-РВХ1 oncogene and almost does not express НОХА genes. Therefore, the results of this study suggest the participation of strong transcriptional activator, chimeric oncoprotein Е2А-РВХ1, associated with chromatin modifying and remodeling enzymes, in the expression activation of HOXA cluster genes that also possess high oncogenic potential.
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3

GOFF, BARBARA A., HOWARD G. MUNTZ, BENJAMIN E. GREER, HISHAM K. TAMIMI, and ALLEN M. GOWN. "Oncogene Expression." Obstetrical & Gynecological Survey 92, no. 1 (July 1998): 88–93. http://dx.doi.org/10.1097/00006250-199807000-00018.

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4

TIAN, XIAOBING, MOHAN R. ARUVA, PONUGOTI S. RAO, WENYI QIN, PAUL READ, EDWARD R. SAUTER, MATHEW L. THAKUR, and ERIC WICKSTROM. "Imaging Oncogene Expression." Annals of the New York Academy of Sciences 1002, no. 1 (December 2003): 165–88. http://dx.doi.org/10.1196/annals.1281.015.

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5

Mukherjee, Archana, Eric Wickstrom, and Mathew L. Thakur. "Imaging oncogene expression." European Journal of Radiology 70, no. 2 (May 2009): 265–73. http://dx.doi.org/10.1016/j.ejrad.2009.01.043.

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6

Luna, Adrian J., Rosa T. Sterk, Anastacia M. Griego-Fisher, Joon-Yong Chung, Kiersten L. Berggren, Virginie Bondu, Pamela Barraza-Flores, et al. "MEK/ERK signaling is a critical regulator of high-risk human papillomavirus oncogene expression revealing therapeutic targets for HPV-induced tumors." PLOS Pathogens 17, no. 1 (January 22, 2021): e1009216. http://dx.doi.org/10.1371/journal.ppat.1009216.

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Intracellular pathogens have evolved to utilize normal cellular processes to complete their replicative cycles. Pathogens that interface with proliferative cell signaling pathways risk infections that can lead to cancers, but the factors that influence malignant outcomes are incompletely understood. Human papillomaviruses (HPVs) predominantly cause benign hyperplasia in stratifying epithelial tissues. However, a subset of carcinogenic or “high-risk” HPV (hr-HPV) genotypes are etiologically linked to nearly 5% of all human cancers. Progression of hr-HPV-induced lesions to malignancies is characterized by increased expression of the E6 and E7 oncogenes and the oncogenic functions of these viral proteins have been widely studied. Yet, the mechanisms that regulate hr-HPV oncogene transcription and suppress their expression in benign lesions remain poorly understood. Here, we demonstrate that EGFR/MEK/ERK signaling, influenced by epithelial contact inhibition and tissue differentiation cues, regulates hr-HPV oncogene expression. Using monolayer cells, epithelial organotypic tissue models, and neoplastic tissue biopsy materials, we show that cell-extrinsic activation of ERK overrides cellular control to promote HPV oncogene expression and the neoplastic phenotype. Our data suggest that HPVs are adapted to use the EGFR/MEK/ERK signaling pathway to regulate their productive replicative cycles. Mechanistic studies show that EGFR/MEK/ERK signaling influences AP-1 transcription factor activity and AP-1 factor knockdown reduces oncogene transcription. Furthermore, pharmacological inhibitors of EGFR, MEK, and ERK signaling quash HPV oncogene expression and the neoplastic phenotype, revealing a potential clinical strategy to suppress uncontrolled cell proliferation, reduce oncogene expression and treat HPV neoplasia.
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7

Byun, Eunyoung, Joo Weon Lim, Jung Mogg Kim, and Hyeyoung Kim. "α-Lipoic Acid InhibitsHelicobacter pylori-Induced Oncogene Expression and Hyperproliferation by Suppressing the Activation of NADPH Oxidase in Gastric Epithelial Cells." Mediators of Inflammation 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/380830.

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Hyperproliferation and oncogene expression are observed in the mucosa ofHelicobacter pylori- (H. pylori-)infected patients with gastritis or adenocarcinoma. Expression of oncogenes such asβ-catenin and c-myc is related to oxidative stress.α-Lipoic acid (α-LA), a naturally occurring thiol compound, acts as an antioxidant and has an anticancer effect. The aim of this study is to investigate the effect ofα-LA onH. pylori-induced hyperproliferation and oncogene expression in gastric epithelial AGS cells by determining cell proliferation (viable cell numbers, thymidine incorporation), levels of reactive oxygen species (ROS), NADPH oxidase activation (enzyme activity, subcellular levels of NADPH oxidase subunits), activation of redox-sensitive transcription factors (NF-κB, AP-1), expression of oncogenes (β-catenin, c-myc), and nuclear localization ofβ-catenin. Furthermore, we examined whether NADPH oxidase mediates oncogene expression and hyperproliferation inH. pylori-infected AGS cells using treatment of diphenyleneiodonium (DPI), an inhibitor of NADPH oxidase. As a result,α-LA inhibited the activation of NADPH oxidase and, thus, reduced ROS production, resulting in inhibition on activation of NF-κB and AP-1, induction of oncogenes, nuclear translocation ofβ-catenin, and hyperproliferation inH. pylori-infected AGS cells. DPI inhibitedH. pylori-induced activation of NF-κB and AP-1, oncogene expression and hyperproliferation by reducing ROS levels in AGS cells. In conclusion, we propose that inhibiting NADPH oxidase byα-LA could prevent oncogene expression and hyperproliferation occurring inH. pylori-infected gastric epithelial cells.
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8

Chernov, A. N. "The impact of the nerve growth factor on the number of MYCC, MYCN oncogene copies in human medulloblastoma cells." Malignant tumours 9, no. 1 (April 10, 2019): 22–28. http://dx.doi.org/10.18027/2224-5057-2019-9-1-22-28.

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Introduction: The search for new molecular targets for chemotherapy of malignancies, particularly pediatric brain tumors, is a relevant issue of modern oncology. MYC expression and amplification is often observed in brain tumors, which is an unfavorable prognostic factor. Many oncogenic processes are regulated by some growth factors including the nerve growth factor (NGF).Purpose: To study the changes in the number of MYCCand MYCN‑gene copies in MB cells exposed to the NGF.Material and methods: The impact of the NGF on the number of MYCC‑, MYCN oncogene copies in the primary human medulloblastoma cell culture was assessed using the method of fluorescence in situ hybridization.Results: Exposure to the NGF was shown to decrease the number of MB cells containing 6, 8 copies of MYCN oncogenes and 3, 8 copies of MYCC oncogene. The NGF was also shown to increase the number of tumor cells that contain a double set of copies of both oncogenes. There was a statistically significant (p<0.0001) negative correlation (r=–0.65) between the average number of MYCC oncogene copies and the NGF cytotoxicity index.Conclusion: The increased number of oncogene copies reduces the susceptibility of MB cells to the growth factor.
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9

Rowley, Peter T., and Gary R. Skuse. "Oncogene expression in myelopoiesis." International Journal of Cell Cloning 5, no. 4 (1987): 255–66. http://dx.doi.org/10.1002/stem.5530050402.

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10

ROWLEY, PETER T., BARBARA KOSCIOLEK, and JUDITH L. BADER. "Oncogene Expression in Neurofibromatosis." Annals of the New York Academy of Sciences 486, no. 1 Neurofibromat (December 1986): 327–32. http://dx.doi.org/10.1111/j.1749-6632.1986.tb48085.x.

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11

Fan, Alice C., Debabrita Deb-Basu, Melissa Horoschak, Amy Shirer, David Voehringer, Roger O’Neill, and Dean W. Felsher. "Nano-Fluidic Detection of Oncoprotein Signaling in Preclinical and Patient Lymphoma Samples." Blood 108, no. 11 (November 16, 2006): 2527. http://dx.doi.org/10.1182/blood.v108.11.2527.2527.

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Abstract Inactivation of oncogenes can be an effective cancer therapy. Determining precise levels of oncogene expression is important in the development of drugs to target oncogenes. We have developed a novel automated nano-fluidic Western-blot-like technology to detect and quantify oncogene expression in small numbers of mouse and human hematopoietic tumor cells. To detect different levels of oncogene expression, we generated transgenic mice in which the MYC or BCL2 oncogenes are regulated conditionally via the Tetracycline Regulatory System (Tet-system). Using lymphoma- derived cell lines from these mice, we titrated the level of oncogene expression by adding different concentrations of doxycycline in vitro. We were able to distinguish among different levels of oncogene expression in cell lysates, with high sensitivity in as few as 400 cells by nano-fluidic detection. Next, lymphoma derived cell lines were injected subcutaneously into syngeneic mice. Upon tumor development, MYC or BCL2 oncogenes were inactivated in vivo. Both MYC and BCL2 levels decreased in serial fine needle aspirations (FNAs) of tumor nodules upon parallel analysis with nano-fluidic detection and Western blot. Finally, we used nano-fluidic detection to determine levels of MYC, BCL2, AKT and ERK in lymph node samples from patients with follicular, transformed DLBC, Burkitt’s, and mantle cell lymphomas. BCL2 was overexpressed in mantle cell and follicular lymphoma patients, confirmed by Western analysis, whereas MYC was found to be overexpressed in Burkitt’s lymphoma. These results demonstrate that nano-fluidic detection technology may be used both as a preclinical tool for the assessment of changes in oncoprotein signaling and as a clinical diagnostic modality on microscopic clinical specimens.
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12

Alema, S., F. Tato, and D. Boettiger. "myc and src oncogenes have complementary effects on cell proliferation and expression of specific extracellular matrix components in definitive chondroblasts." Molecular and Cellular Biology 5, no. 3 (March 1985): 538–44. http://dx.doi.org/10.1128/mcb.5.3.538.

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The effects of the avian viral oncogenes src and myc were compared for their ability to alter the differentiated phenotype and the proliferative capacity of definitive chondroblasts. As previously demonstrated, viruses carrying the src oncogene suppressed the synthesis of the chondroblast-specific products, type II collagen and cartilage-specific sulfated proteoglycan. In contrast, infection with MC29 and HB1 viruses, which carry the myc oncogene, did not suppress the synthesis of these normal differentiated cell products, but the infected cells exhibited an increased proliferative potential. The MH2 virus, which carries both the myc and mil oncogenes, both induced the suppression of these chondroblast-specific products and increased cell proliferation. The implications of these results for cooperation between oncogenes and the multi-oncogene models for neoplastic transformation are discussed.
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13

Alema, S., F. Tato, and D. Boettiger. "myc and src oncogenes have complementary effects on cell proliferation and expression of specific extracellular matrix components in definitive chondroblasts." Molecular and Cellular Biology 5, no. 3 (March 1985): 538–44. http://dx.doi.org/10.1128/mcb.5.3.538-544.1985.

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The effects of the avian viral oncogenes src and myc were compared for their ability to alter the differentiated phenotype and the proliferative capacity of definitive chondroblasts. As previously demonstrated, viruses carrying the src oncogene suppressed the synthesis of the chondroblast-specific products, type II collagen and cartilage-specific sulfated proteoglycan. In contrast, infection with MC29 and HB1 viruses, which carry the myc oncogene, did not suppress the synthesis of these normal differentiated cell products, but the infected cells exhibited an increased proliferative potential. The MH2 virus, which carries both the myc and mil oncogenes, both induced the suppression of these chondroblast-specific products and increased cell proliferation. The implications of these results for cooperation between oncogenes and the multi-oncogene models for neoplastic transformation are discussed.
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14

Scheerger and Zempleni. "Expression of Oncogenes Depends on Biotin in Human Small Cell Lung Cancer Cells NCI-H69." International Journal for Vitamin and Nutrition Research 73, no. 6 (December 1, 2003): 461–67. http://dx.doi.org/10.1024/0300-9831.73.6.461.

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Oncogenes play important roles in cell proliferation and biotin status correlates with gene expression and proliferation rates in human cells. In this study we determined whether biotin supply affects biotin homeostasis, expression of oncogenes, and proliferation rates in NCI-H69 small cell lung cancer cells. NCI-H69 cells were cultured in media containing deficient (0.025 nmol/L), physiologic (0.25 nmol/L), or pharmacologic (10 nmol/L) concentrations of biotin for 3 weeks. Biotin concentrations in culture media correlated negatively with biotin transport rates, suggesting that cells responded to marginal biotin supply with increased expression of biotin transporters. Increased biotin uptake was not sufficient to prevent depletion of intracellular biotin in cells cultured in biotin-deficient medium, as judged by decreased activity of biotin-dependent propionyl-CoA carboxylase and decreased biotinylation of histones. The expression of oncogenes N-myc, c-myb, N-ras, and raf correlated with biotin supply in media: oncogene expression increased by up to 20% in cells cultured in pharmacologic medium compared to physiologic controls; oncogene expression decreased by up to 47% in cells cultured in deficient medium. This observation is consistent with a role for biotin in oncogene-dependent metabolic pathways. Cellular uptake of thymidine (marker for proliferation) was not affected by biotin supply, suggesting that effects of biotin-dependent expression of oncogenes on the growth of tumor cells are quantitatively minor. The clinical significance of effects of biotin supply on expression of oncogenes remains to be elaborated.
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15

Kelekar, A., and M. D. Cole. "Immortalization by c-myc, H-ras, and Ela oncogenes induces differential cellular gene expression and growth factor responses." Molecular and Cellular Biology 7, no. 11 (November 1987): 3899–907. http://dx.doi.org/10.1128/mcb.7.11.3899.

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Early-passage rat kidney cells were immortalized or rescued from senescence with three different oncogenes: viral promoter-driven c-myc, H-ras (Val-12), and adenovirus type 5 E1a. The normal c-myc and H-ras (Gly-12) were unable to immortalize cells under similar conditions. Quantitation of RNA in the ras-immortalized lines demonstrated that the H-ras oncogene was expressed at a level equivalent to that of the normal H-ras gene in established human or rat cell lines. Cell lines immortalized by different oncogenes were found to have distinct growth responses to individual growth factors in a short-term assay. E1a-immortalized cells were largely independent of serum growth factors, whereas c-myc-immortalized cells responded to serum better than to epidermal growth factor and insulin. H-ras-immortalized cells responded significantly to insulin alone and gave a maximal response to epidermal growth factor and insulin. Several cellular genes associated with platelet-derived growth factor stimulation, including c-myc, were expressed at high levels in the H-ras-immortalized cells, and c-myc expression was deregulated, suggesting that the H-ras oncogene has provided a "competence" function. H-ras-immortalized cells could not be morphologically transformed by secondary transfection with a long terminal repeat-c-myc oncogene, but secondary transfection of the same cells with H-ras (Val-12) produced morphologically transformed colonies that had 20- to 40-fold higher levels of H-ras oncogene expression. Thus, transformation in this system is dependent on high levels of H-ras oncogene expression rather than on the presence of activated H-ras and c-myc oncogenes in the same cell.
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16

Kelekar, A., and M. D. Cole. "Immortalization by c-myc, H-ras, and Ela oncogenes induces differential cellular gene expression and growth factor responses." Molecular and Cellular Biology 7, no. 11 (November 1987): 3899–907. http://dx.doi.org/10.1128/mcb.7.11.3899-3907.1987.

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Early-passage rat kidney cells were immortalized or rescued from senescence with three different oncogenes: viral promoter-driven c-myc, H-ras (Val-12), and adenovirus type 5 E1a. The normal c-myc and H-ras (Gly-12) were unable to immortalize cells under similar conditions. Quantitation of RNA in the ras-immortalized lines demonstrated that the H-ras oncogene was expressed at a level equivalent to that of the normal H-ras gene in established human or rat cell lines. Cell lines immortalized by different oncogenes were found to have distinct growth responses to individual growth factors in a short-term assay. E1a-immortalized cells were largely independent of serum growth factors, whereas c-myc-immortalized cells responded to serum better than to epidermal growth factor and insulin. H-ras-immortalized cells responded significantly to insulin alone and gave a maximal response to epidermal growth factor and insulin. Several cellular genes associated with platelet-derived growth factor stimulation, including c-myc, were expressed at high levels in the H-ras-immortalized cells, and c-myc expression was deregulated, suggesting that the H-ras oncogene has provided a "competence" function. H-ras-immortalized cells could not be morphologically transformed by secondary transfection with a long terminal repeat-c-myc oncogene, but secondary transfection of the same cells with H-ras (Val-12) produced morphologically transformed colonies that had 20- to 40-fold higher levels of H-ras oncogene expression. Thus, transformation in this system is dependent on high levels of H-ras oncogene expression rather than on the presence of activated H-ras and c-myc oncogenes in the same cell.
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17

Land, H., A. C. Chen, J. P. Morgenstern, L. F. Parada, and R. A. Weinberg. "Behavior of myc and ras oncogenes in transformation of rat embryo fibroblasts." Molecular and Cellular Biology 6, no. 6 (June 1986): 1917–25. http://dx.doi.org/10.1128/mcb.6.6.1917.

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The requirements for transformation of rat embryo fibroblasts (REFs) by transfected ras and myc oncogenes were explored. Under conditions of dense monolayer culture, neither oncogene was able to transform REFs on its own. However, the introduction of a ras oncogene together with a selectable neomycin resistance marker into REFs allowed killing of the normal nontransfected cells and the outgrowth of colonies of ras transformants, 10% of which survived crisis and became tumorigenic. These cells expressed greater than 10-fold-higher levels of ras p21 than tumorigenic cells cotransfected with ras and myc oncogenes. The myc oncogene similarly was unable to induce tumorigenic conversion of REFs unless especially refractile colonies of oncogene-bearing cells, produced by use of a cotransfected selectable marker, were picked and subcultured. Tumorigenic conversion of REFs by single transfected oncogenes appears to require special culture conditions and high levels of gene expression.
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18

Land, H., A. C. Chen, J. P. Morgenstern, L. F. Parada, and R. A. Weinberg. "Behavior of myc and ras oncogenes in transformation of rat embryo fibroblasts." Molecular and Cellular Biology 6, no. 6 (June 1986): 1917–25. http://dx.doi.org/10.1128/mcb.6.6.1917-1925.1986.

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The requirements for transformation of rat embryo fibroblasts (REFs) by transfected ras and myc oncogenes were explored. Under conditions of dense monolayer culture, neither oncogene was able to transform REFs on its own. However, the introduction of a ras oncogene together with a selectable neomycin resistance marker into REFs allowed killing of the normal nontransfected cells and the outgrowth of colonies of ras transformants, 10% of which survived crisis and became tumorigenic. These cells expressed greater than 10-fold-higher levels of ras p21 than tumorigenic cells cotransfected with ras and myc oncogenes. The myc oncogene similarly was unable to induce tumorigenic conversion of REFs unless especially refractile colonies of oncogene-bearing cells, produced by use of a cotransfected selectable marker, were picked and subcultured. Tumorigenic conversion of REFs by single transfected oncogenes appears to require special culture conditions and high levels of gene expression.
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19

Klemenz, R., E. Fröhli, A. Aoyama, S. Hoffmann, R. J. Simpson, R. L. Moritz, and R. Schäfer. "Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts." Molecular and Cellular Biology 11, no. 2 (February 1991): 803–12. http://dx.doi.org/10.1128/mcb.11.2.803.

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The conditional expression of the v-mos and Ha-ras(EJ) oncogenes in NIH 3T3 cells leads to the accumulation of a 23-kDa protein (p23) (R. Klemenz, S. Hoffmann, R. Jaggi, and A.-K. Werenskiold, Oncogene 4:799-803, 1989). We purified p23 to homogeneity and determined part of the amino acid sequence. The obtained sequence is identical with that of the eye lens protein alpha B crystallin. Northern (RNA) blot and Western immunoblot experiments were performed to demonstrate that alpha B crystallin mRNA and protein do indeed accumulate as a consequence of v-mos and Ha-ras oncogene expression. Comparison of cDNA clones obtained from the mRNA of eye lenses and of oncogene-expressing fibroblasts revealed identity between them. The major transcription initiation site of the alpha B crystallin gene in our experimental system was shown by primer extension experiments to be identical with the one used in eye epithelial cells. In addition, we identified a second minor initiation site 49 nucleotides further upstream. Serum growth factors did not stimulate alpha B crystallin expression in growth-arrested cells.
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20

Klemenz, R., E. Fröhli, A. Aoyama, S. Hoffmann, R. J. Simpson, R. L. Moritz, and R. Schäfer. "Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts." Molecular and Cellular Biology 11, no. 2 (February 1991): 803–12. http://dx.doi.org/10.1128/mcb.11.2.803-812.1991.

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The conditional expression of the v-mos and Ha-ras(EJ) oncogenes in NIH 3T3 cells leads to the accumulation of a 23-kDa protein (p23) (R. Klemenz, S. Hoffmann, R. Jaggi, and A.-K. Werenskiold, Oncogene 4:799-803, 1989). We purified p23 to homogeneity and determined part of the amino acid sequence. The obtained sequence is identical with that of the eye lens protein alpha B crystallin. Northern (RNA) blot and Western immunoblot experiments were performed to demonstrate that alpha B crystallin mRNA and protein do indeed accumulate as a consequence of v-mos and Ha-ras oncogene expression. Comparison of cDNA clones obtained from the mRNA of eye lenses and of oncogene-expressing fibroblasts revealed identity between them. The major transcription initiation site of the alpha B crystallin gene in our experimental system was shown by primer extension experiments to be identical with the one used in eye epithelial cells. In addition, we identified a second minor initiation site 49 nucleotides further upstream. Serum growth factors did not stimulate alpha B crystallin expression in growth-arrested cells.
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21

OLÁH, EDITH, REZSO EZER, WALTER GIARETTI, and JOHN EBLE. "Metabolic control of oncogene expression." Biochemical Society Transactions 18, no. 1 (February 1, 1990): 72–74. http://dx.doi.org/10.1042/bst0180072.

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22

Tatosyan, A. G., S. A. Galetzki, N. P. Kisseljova, A. A. Asanova, I. B. Zborovskaya, D. D. Spitkovsky, E. S. Revasova, P. Martin, and F. L. Kisseljov. "Oncogene expression in human tumors." International Journal of Cancer 35, no. 6 (June 15, 1985): 731–36. http://dx.doi.org/10.1002/ijc.2910350606.

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23

Pillai, Radhakrishna, Kannan Sankara Reddiar, and Prabha Balaram. "Oncogene expression and oral cancer." Journal of Surgical Oncology 47, no. 2 (June 1991): 102–8. http://dx.doi.org/10.1002/jso.2930470209.

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24

Groner, B. "Hormonal regulation of oncogene expression." Journal of Cancer Research and Clinical Oncology 111, S1 (February 1986): S42. http://dx.doi.org/10.1007/bf02579937.

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25

Groner, Bernd. "Hormonal regulation of oncogene expression." Fresenius' Zeitschrift für analytische Chemie 324, no. 3-4 (January 1986): 220. http://dx.doi.org/10.1007/bf00487863.

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26

Bussemakers, M. J. G., J. T. Isaacs, F. M. J. Debruyne, W. J. M. Van de Ven, and J. A. Schalken. "Oncogene expression in prostate cancer." World Journal of Urology 9, no. 2 (June 1991): 58–63. http://dx.doi.org/10.1007/bf00184034.

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27

Xu, Liangzhong, Tingqiu Zhang, Xiaojuan Hu, and Jie Zhang. "Expression of oncogene and anti-oncogene in male breast carcinoma." Chinese Journal of Cancer Research 7, no. 1 (March 1995): 38–43. http://dx.doi.org/10.1007/bf02954705.

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28

Xu, Mai, Qing Yu, Ramesh Subrahmanyam, Michael J. Difilippantonio, Thomas Ried, and Jyoti Misra Sen. "β-Catenin Expression Results in p53-Independent DNA Damage and Oncogene-Induced Senescence in Prelymphomagenic Thymocytes In Vivo." Molecular and Cellular Biology 28, no. 5 (December 26, 2007): 1713–23. http://dx.doi.org/10.1128/mcb.01360-07.

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ABSTRACT The expression of β-catenin, a potent oncogene, is causally linked to tumorigenesis. Therefore, it was surprising that the transgenic expression of oncogenic β-catenin in thymocytes resulted in thymic involution instead of lymphomagenesis. In this report, we demonstrate that this is because the expression of oncogenic β-catenin induces DNA damage, growth arrest, oncogene-induced senescence (OIS), and apoptosis of immature thymocytes. In p53-deficient mice, the expression of oncogenic β-catenin still results in DNA damage and OIS, but the thymocytes survive and eventually progress to thymic lymphoma. β-Catenin-induced thymic lymphomas are distinct from lymphomas that arise in p53−/− mice. They are CD4− CD8−, while p53-dependent lymphomas are largely CD4+ CD8+, and they develop at an earlier age and in the absence of c-Myc expression or Notch1 signaling. Thus, we report that oncogenic β-catenin-induced, p53-independent growth arrest and OIS and p53-dependent apoptosis protect developing thymocytes from transformation by oncogenic β-catenin.
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29

Wickstrom, Eric, Edward Sauter, Xianben Tian, Sampath Rao, Weyng Quin, and Mathew Thakur. "Radiolabeled PNAs for imaging gene expression." Brazilian Archives of Biology and Technology 45, spe (September 2002): 57–59. http://dx.doi.org/10.1590/s1516-89132002000500008.

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Scintigraphic imaging of gene expression in vivo by non-invasive means could precisely direct physicians to appropriate intervention at the onset of disease and could contribute extensively to the management of patients. However, no method is currently available to image specific overexpressed oncogene mRNAs in vivo by scintigraphic imaging. Nevertheless, we have observed that Tc-99m-peptides can delineate tumors, and that PNA-peptides are specific for receptors on malignant cells and are taken up specifically and concentrated in nuclei. We hypothesize that antisense Tc-99m-PNA-peptides will be taken up by human breast cancer cells, hybridize to complementary mRNA targets, and permit imaging of oncogene mRNAs in human breast cancer xenografts in a mouse model, providing a proof-of-principle for non-invasive detection of precancerous and invasive breast cancer. Oncogenes cyclin D1, erbB-2, c-MYC, and tumor suppressor p53 will be probed. If successful, this technique will be useful for diagnostic imaging of other solid tumors as well.
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30

Stacey, Dennis W., Masahiro Hitomi, and Guan Chen. "Influence of Cell Cycle and Oncogene Activity upon Topoisomerase IIα Expression and Drug Toxicity." Molecular and Cellular Biology 20, no. 24 (December 15, 2000): 9127–37. http://dx.doi.org/10.1128/mcb.20.24.9127-9137.2000.

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ABSTRACT The cell cycle, oncogenic signaling, and topoisomerase (topo) IIα levels all influence sensitivity to anti-topo II drugs. Because the cell cycle and oncogenic signaling influence each other as well as topo IIα levels, it is difficult to assess the importance of any one of these factors independently of the others during drug treatment. Such information, however, is vital to an understanding of the cellular basis of drug toxicity. We, therefore, developed a series of analytical procedures to individually assess the role of each of these factors during treatment with the anti-topo II drug etoposide. All studies were performed with asynchronously proliferating cultures by the use of time-lapse and quantitative fluorescence staining procedures. To our surprise, we found that neither oncogene action nor the cell cycle altered topo IIα protein levels in actively cycling cells. Only a minor population of slowly cycling cells within these cultures responded to constitutively active oncogenes by elevating topo IIα production. Thus, it was possible to study the effects of the cell cycle and oncogene action on drug-treated cells while topo IIα levels remained constant. Toxicity analyses were performed with two consecutive time-lapse observations separated by a brief drug treatment. The cell cycle phase was determined from the first observation, and cell fate was determined from the second. Cells were most sensitive to drug treatment from mid-S phase through G2 phase, with G1 phase cells nearly threefold less sensitive. In addition, the presence of an oncogenicsrc gene or microinjected Ras protein increased drug toxicity by approximately threefold in actively cycling cells and by at least this level in the small population of slowly cycling cells. We conclude that both cell cycle phase and oncogenic signaling influence drug toxicity independently of alterations in topo IIα levels.
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31

Clark, SS, Y. Liang, CK Reedstrom, and SQ Wu. "Nonrandom cytogenetic changes accompany malignant progression in clonal lines abelson virus-infected lymphocytes." Blood 84, no. 12 (December 15, 1994): 4301–9. http://dx.doi.org/10.1182/blood.v84.12.4301.bloodjournal84124301.

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Initially, lymphoid cells transformed by v-abl or BCR/ABL oncogenes are poorly oncogenic but progress to full transformation over time. Although expression of the oncogene is necessary to initiate and maintain transformation, other molecular mechanisms are thought to be required for full transformation. To determine whether tumor progression in ABL oncogene-transformed lymphoid cells has a genetic basis, we examined whether progression of the malignant phenotype of transformed clones correlates with particular cytogenetic abnormalities. A modified in vitro bone marrow transformation model was used to obtain clonal Abelson murine leukemia virus-transformed B lymphoid cells that were poorly oncogenic. Multiple subclones were then derived from each clone and maintained over a marrow-derived stromal cell line for several weeks. Over time, clonally related Abelson murine leukemia virus-transformed subclones progressed asynchronously to full transformation. The data show that tumor progression can occur in the absence of detectable cytogenetic changes but, more importantly, that certain cytogenetic abnormalities appear reproducibly in highly malignant subclones. Therefore, three independent subclones showed deletion in a common region of chromosome 13. Other highly malignant cells carried a common breakpoint in the X chromosome, and, finally, two subclones carried an additional chromosome 5. These results are consistent with the hypothesis that ABL oncogenes are sufficient for the initial transformation of cells but that additional genetic events can drive oncogenic progression. These observations further suggest that diverse genetic mechanisms may be able to drive tumor progression in cells transformed with ABL oncogenes.
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32

Gabai, Vladimir L., Julia A. Yaglom, Todd Waldman, and Michael Y. Sherman. "Heat Shock Protein Hsp72 Controls Oncogene-Induced Senescence Pathways in Cancer Cells." Molecular and Cellular Biology 29, no. 2 (November 10, 2008): 559–69. http://dx.doi.org/10.1128/mcb.01041-08.

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ABSTRACT The heat shock protein Hsp72 is expressed at the elevated levels in various human tumors, and its levels often correlate with poor prognosis. Previously we reported that knockdown of Hsp72 in certain cancer cells, but not in untransformed breast epithelial cells, triggers senescence via p53-dependent and p53-independent mechanisms. Here we demonstrate that the p53-dependent pathway controlled by Hsp72 depends on the oncogenic form of phosphatidylinositol 3-kinase (PI3K). Indeed, upon expression of the oncogenic PI3K, epithelial cells began responding to Hsp72 depletion by activating the p53 pathway. Moreover, in cancer cell lines, activation of the p53 pathway caused by depletion of Hsp72 was dependent on oncogenes that activate the PI3K pathway. On the other hand, the p53-independent senescence pathway controlled by Hsp72 was associated with the Ras oncogene. In this pathway, extracellular signal-regulated kinases (ERKs) were critical for senescence, and Hsp72 controlled the ERK-activating kinase cascade at the level of Raf-1. Importantly, upon Ras expression, untransformed cells started responding to knockdown of Hsp72 by constitutive activation of ERKs, culminating in senescence. Therefore, Hsp72 is intimately involved in suppression of at least two separate senescence signaling pathways that are regulated by distinct oncogenes in transformed cells, which explains why cancer cells become “addicted” to this heat shock protein.
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33

Kazumoto, Kiyoshi, Masaru Tamura, Hiroo Hoshino, and Yasuhito Yuasa. "Enhanced expression of the sis and c-myc oncogenes in human meningiomas." Journal of Neurosurgery 72, no. 5 (May 1990): 786–91. http://dx.doi.org/10.3171/jns.1990.72.5.0786.

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✓ In 19 human meningiomas (14 primary and four recurrent tumors and one tumor transplanted into athymic nude mice), oncogene expression, amplification, and rearrangement, and loss of heterozygosity on chromosome 22 were examined. Compared to nontumor brain tissue, there was greater than a fivefold expression of the sis oncogene in six (40%) of 15 tumors studied and of the c-myc oncogene in 12 (63%) of the total 19 tumors. Expression of the sis gene was lower in the recurrent tumors than in the primary cases, and there was no detectable expression in anaplastic meningioma cells. Rearrangement of the sis gene was found in one meningioma. Loss of heterozygosity on chromosome 22 was detected in two of the five informative heterozygous cases. Expression of the c-myc gene was higher in cases with loss of heterozygosity than in those without. These results suggest that the sis and c-myc oncogenes are associated with tumorigenicity and that c-myc may induce meningiomas through loss of the putative tumor suppressor gene.
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34

Jetten, A. M., J. C. Barrett, and T. M. Gilmer. "Differential response to retinoic acid of Syrian hamster embryo fibroblasts expressing v-src or v-Ha-ras oncogenes." Molecular and Cellular Biology 6, no. 10 (October 1986): 3341–48. http://dx.doi.org/10.1128/mcb.6.10.3341.

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It has been shown that treatment of many but not all tumor cell lines with retinoids affects cell proliferation and expression of the transformed phenotype. To determine whether the response of the tumor cell to retinoids is influenced by specific oncogenes activated in the cell, we studied the action of these agents in the immortal, nontumorigenic Syrian hamster embryo cell lines DES-4 and 10W transfected with either v-Ha-ras or v-src oncogenes. In this paper we show that in transformed DES-4 cells expressing v-src, retinoic acid inhibited anchorage-independent growth, reduced saturation density, and inhibited the induction of ornithine decarboxylase by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate. In contrast, retinoic acid enhances the expression of the transformed phenotype in DES-4-derived cells that express v-Ha-ras. In these cells retinoic acid increases the number and the average size of colonies formed in soft agar. Moreover, retinoic acid enhances ornithine decarboxylase activity and acts in a synergistic fashion with 12-O-tetradecanoylphorbol-13-acetate. These results indicate that oncogenes activated in cells can indeed influence the response of cells to retinoids. Retinoic acid does not appear to alter the levels of pp60src or p21ras proteins in these cells, suggesting that retinoic acid does not affect the synthesis of these oncogene products. Furthermore, retinoic acid does not affect the protein kinase activity of pp60src. Transformed cell lines derived from 10W cells responded differently, indicating that the presence of a specific oncogene is not the only factor determining the response to retinoids. Possible mechanisms by which retinoic acid may interfere with the expression of the oncogene products are discussed.
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35

Jetten, A. M., J. C. Barrett, and T. M. Gilmer. "Differential response to retinoic acid of Syrian hamster embryo fibroblasts expressing v-src or v-Ha-ras oncogenes." Molecular and Cellular Biology 6, no. 10 (October 1986): 3341–48. http://dx.doi.org/10.1128/mcb.6.10.3341-3348.1986.

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It has been shown that treatment of many but not all tumor cell lines with retinoids affects cell proliferation and expression of the transformed phenotype. To determine whether the response of the tumor cell to retinoids is influenced by specific oncogenes activated in the cell, we studied the action of these agents in the immortal, nontumorigenic Syrian hamster embryo cell lines DES-4 and 10W transfected with either v-Ha-ras or v-src oncogenes. In this paper we show that in transformed DES-4 cells expressing v-src, retinoic acid inhibited anchorage-independent growth, reduced saturation density, and inhibited the induction of ornithine decarboxylase by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate. In contrast, retinoic acid enhances the expression of the transformed phenotype in DES-4-derived cells that express v-Ha-ras. In these cells retinoic acid increases the number and the average size of colonies formed in soft agar. Moreover, retinoic acid enhances ornithine decarboxylase activity and acts in a synergistic fashion with 12-O-tetradecanoylphorbol-13-acetate. These results indicate that oncogenes activated in cells can indeed influence the response of cells to retinoids. Retinoic acid does not appear to alter the levels of pp60src or p21ras proteins in these cells, suggesting that retinoic acid does not affect the synthesis of these oncogene products. Furthermore, retinoic acid does not affect the protein kinase activity of pp60src. Transformed cell lines derived from 10W cells responded differently, indicating that the presence of a specific oncogene is not the only factor determining the response to retinoids. Possible mechanisms by which retinoic acid may interfere with the expression of the oncogene products are discussed.
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36

Rak, Janusz W., Nathalie Magnus, Delphine Garnier, Esterina D’Asti, Maryam Hashemi, Brian Meehan, Chloe Milsom, and Joanne L. Yu. "Oncogenic Regulation of Tissue Factor Expression." Blood 118, no. 21 (November 18, 2011): SCI—16—SCI—16. http://dx.doi.org/10.1182/blood.v118.21.sci-16.sci-16.

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Abstract Abstract SCI-16 Coagulation system plays a long-recognized role in cancer progression and in the related morbidity and mortality (1, 2). Once regarded as an unspecific epiphenomenon of the underlying disease, this involvement is now viewed as a direct consequence of oncogenic mutations and the resulting acquisition of the procoagulant phenotype by cancer cells followed by local and systemic vascular consequences (Trousseau syndrome) (3). Tissue factor (TF) represents an illuminating molecular paradigm of these changes, acting as both the central regulator of the coagulation system circuitry and an emerging regulatory target of several oncogenic lesions. Thus, oncogene-driven TF upregulation has been documented in a wide spectrum of human cancer cells, including: colorectal (CRC), lung, breast, and skin cancer, as well as glioblastoma (GBM), medulloblastoma (MB), and hematopoietic malignancies. This is linked to activation of several dominant acting oncogenes, such as: K-ras, epidermal growth factor receptor (EGFR), mutant EGFR (EGFRvIII), HER-2, MET, retinoid acid receptor (RAR), and several others (4). These effects are also enabled and amplified by losses of tumor suppressor genes, such as p53 and PTEN, and modulated by microRNA (miR) networks, as well as microenvironmental and regulatory factors, such as hypoxia, inflammation, differentiation, and epithelial-to-mesenchymal transition (EMT) (5). In addition, oncogenic mutations activate several mechanisms that may sensitize cancer cells to extracellular stimuli, including the exposure to circulating coagulation factors that may access cancer cells through leaky tumor blood vessels. For instance, the expression of EGFRvIII in human GBM cells leads not only to a dramatic increase in TF levels, but also to the ectopic expression of coagulation factor VII, the main TF ligand. Simultaneously, oncogenic events (e.g., EGFRvIII or K-ras) induce marked upregulation of protease activated receptors 1 and 2 (PAR1/2), which further enhance the transmission of intracellular signals from the TF/FVIIa complex (6). Furthermore, oncogenes provoke cellular vesiculation whereby TF and other signaling proteins (including oncoproteins themselves) are released into the extracellular space and to the systemic circulation. As a result, these signaling proteins may be transferred to other cells, and modify their properties locally, regionally, and systemically (4, 7). These changes are a part of the signaling network that affects tumor growth, invasion, and metastasis, and acts through generation of a procoagulant, proinflammatory, and pro-angiogenic microenvironment, which contain niches for tumor-initiating cells (TICs). TICs (cancer stem cells) are key targets for oncogenic transformation and essential drivers of the malignant process. Their responses to the coagulation system may be altered by changes in TF and PAR status. TF targeting through genetic and pharmacological approaches results in impaired tumor initiation and growth in various experimental settings, including in transgenic models of GBM. In some instances host cell-associated TF may also play a role in disease progression, while in other cases tumor stroma and inflammatory cells are modulated indirectly by TF-expressing cancer cells (7). Collectively, oncogene-dependent deregulation of TF and activation of the coagulation system circuitry represents a unique biological effector mechanism, which likely promotes progression of human cancers, and thereby may serve as a potential therapeutic target. Disclosures: No relevant conflicts of interest to declare.
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37

Zullo, J. N., and D. V. Faller. "P21 v-ras inhibits induction of c-myc and c-fos expression by platelet-derived growth factor." Molecular and Cellular Biology 8, no. 12 (December 1988): 5080–85. http://dx.doi.org/10.1128/mcb.8.12.5080.

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The viral oncogene v-ras inhibited the platelet-derived growth factor (PDGF)-induced upregulation of c-myc and c-fos proto-oncogene expression in fibroblast monolayers. These v-ras-containing cells proliferated in the absence of c-myc induction and no longer required PDGF to support growth. Fibroblasts expressing v-ras continued to express the same number of functional PDGF receptors on their surface as uninfected cells, yet the usual induction of transcription of the genes c-myc, c-fos, and JE in response to PDGF stimulation did not occur in the presence of newly introduced v-ras or chronic v-ras gene expression, and synthesis of c-myc protein did not occur. This inhibitory effect on growth factor-mediated induction of cellular proto-oncogenes was specific for PDGF in that induction of the c-myc and c-fos genes by certain other factors was not impaired.
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38

Zullo, J. N., and D. V. Faller. "P21 v-ras inhibits induction of c-myc and c-fos expression by platelet-derived growth factor." Molecular and Cellular Biology 8, no. 12 (December 1988): 5080–85. http://dx.doi.org/10.1128/mcb.8.12.5080-5085.1988.

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The viral oncogene v-ras inhibited the platelet-derived growth factor (PDGF)-induced upregulation of c-myc and c-fos proto-oncogene expression in fibroblast monolayers. These v-ras-containing cells proliferated in the absence of c-myc induction and no longer required PDGF to support growth. Fibroblasts expressing v-ras continued to express the same number of functional PDGF receptors on their surface as uninfected cells, yet the usual induction of transcription of the genes c-myc, c-fos, and JE in response to PDGF stimulation did not occur in the presence of newly introduced v-ras or chronic v-ras gene expression, and synthesis of c-myc protein did not occur. This inhibitory effect on growth factor-mediated induction of cellular proto-oncogenes was specific for PDGF in that induction of the c-myc and c-fos genes by certain other factors was not impaired.
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39

Baron-Delage, S., L. Mahraoui, A. Cadoret, D. Veissiere, J. L. Taillemite, E. Chastre, C. Gespach, et al. "Deregulation of hexose transporter expression in Caco-2 cells by ras and polyoma middle T oncogenes." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 2 (February 1, 1996): G314—G323. http://dx.doi.org/10.1152/ajpgi.1996.270.2.g314.

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We investigated whether the oncogenic activation of p21ras or pp60c-src, which is frequently observed in colorectal cancers, induced alterations of sugar uptake in human colonic cells. We therefore examined hexose transporter expression and/or activity in Caco-2 cells transfected either with an activated human (Val-12) Ha-ras gene or with the polyoma middle T (PyMT) oncogene, a constitutive activator of pp60c-src tyrosine kinase activity. Experiments were performed at day 20 of culture, when Caco-2 cells express enterocyte-specific GLUT-2, GLUT-5, and SGLT-1 transporters in addition to GLUT-1 and GLUT-3. Along with increased glucose consumption rates, both oncogene-transfected cells exhibited increased levels of GLUT-1 and GLUT-3 mRNAs and/or immunoreactive proteins compared with control vector Caco-2 cells. In contrast, oncogene-transfected cells lost GLUT-2, GLUT-5, and SGLT-1 expression as determined by Northern and/or Western blot analyses and/or specific transport assays. The oncogene-induced repressive effect on these enterocyte-specific hexose transporters extended to brush-border hydrolases and villin but not to tight junctional protein ZO-1. In conclusion, oncogenic p21ras and PyMT/pp60c-src induce severe deregulation of hexose transporter expression in Caco-2 cells, which is manifested by 1) increased GLUT-1 and GLUT-3 expression and 2) repression of GLUT-2, GLUT-5, and SGLT-1, which parallels repression of some markers of the enterocyte-like differentiated phenotype of Caco-2 cells.
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40

Gilbert, F., V. R. Potluri, M. P. Short, C. L. Kau, and F. Lalatta. "Retinoblastoma, chromosome abnormalities and oncogene expression." Ophthalmic Paediatrics and Genetics 8, no. 1 (January 1987): 3–10. http://dx.doi.org/10.3109/13816818709028508.

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41

Oni, Olusola O. A. "Proto-oncogene expression during fracture repair." Injury 31, no. 5 (June 2000): 363–66. http://dx.doi.org/10.1016/s0020-1383(00)00004-8.

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42

Nagao, Minako, Yukihito Ishizaka, Akira Nakagawara, Kimitoshi Kohno, Michihiko Kuwano, Tomoko Tahira, Fumio Itoh, Isuzu Ikeda, and Takashi Sugimura. "Expression ofretProto-oncogene in Human Neuroblastomas." Japanese Journal of Cancer Research 81, no. 4 (April 1990): 309–12. http://dx.doi.org/10.1111/j.1349-7006.1990.tb02566.x.

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43

Wang, Da-Gong, Aaros A. B. Barros D'Sa, Colin F. Johnston, and Keith D. Buchanan. "Oncogene expression in carotid body tumors." Cancer 77, no. 12 (June 15, 1996): 2581–87. http://dx.doi.org/10.1002/(sici)1097-0142(19960615)77:12<2581::aid-cncr23>3.0.co;2-n.

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44

Wang, Da-Gong, Colin F. Johnston, and Keith D. Buchanan. "Oncogene expression in gastroenteropancreatic neuroendocrine tumors." Cancer 80, no. 4 (August 15, 1997): 668–75. http://dx.doi.org/10.1002/(sici)1097-0142(19970815)80:4<668::aid-cncr4>3.0.co;2-j.

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45

Groner, Bernd. "Oncogene expression in mammary epithelial cells." Journal of Cellular Biochemistry 49, no. 2 (June 1992): 128–36. http://dx.doi.org/10.1002/jcb.240490205.

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46

Carstens, C., E. Messe, K. D. Zang, and N. Blin. "Human KRAS oncogene expression in meningioma." Cancer Letters 43, no. 1-2 (December 1988): 37–41. http://dx.doi.org/10.1016/0304-3835(88)90210-8.

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47

Höfler, Heinz, Christine Ruhri, Barbara Pütz, Gerhard Wirnsberger, and Hubert Häuser. "Oncogene expression in endocrine pancreatie tumors." Virchows Archiv B Cell Pathology 55, no. 1 (November 1988): 355–61. http://dx.doi.org/10.1007/bf02896594.

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48

Gottifredi, V., A. Peschiaroli, G. M. Fimia, and R. Maione. "p53-independent apoptosis induced by muscle differentiation stimuli in polyomavirus large T-expressing myoblasts." Journal of Cell Science 112, no. 14 (July 15, 1999): 2397–407. http://dx.doi.org/10.1242/jcs.112.14.2397.

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Abnormal proliferation signals, driven by cellular or viral oncogenes, can result in the induction of apoptosis under sub-optimal cell growth conditions. The tumor suppressor p53 plays a central role in mediating oncogene-induced apoptosis, therefore transformed cells lacking p53 are generally resistant to apoptosis-promoting treatments. In a previous work we have reported that the expression of polyomavirus large T antigen causes apoptosis in differentiating myoblasts and that this phenomenon is dependent on the onset of muscle differentiation in the absence of a correct cell cycle arrest. Here we report that polyomavirus large T increases the levels and activity of p53, but these alterations are not involved in the apoptotic mechanism. Apoptosis in polyomavirus large T-expressing myoblasts is not prevented by the expression of a p53 dominant-negative mutant nor it is increased by p53 over-expression. Moreover, forced differentiation induced through the over-expression of the muscle regulatory factor MyoD, leads to apoptosis without altering p53 function and, more significantly, even in a p53-null background. Our results indicate that apoptosis induced by the activation of muscle differentiation pathways in oncogene-expressing cells can occur in a p53-independent manner.
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49

Cowley, B. D., L. J. Chadwick, J. J. Grantham, and J. P. Calvet. "Elevated proto-oncogene expression in polycystic kidneys of the C57BL/6J (cpk) mouse." Journal of the American Society of Nephrology 1, no. 8 (February 1991): 1048–53. http://dx.doi.org/10.1681/asn.v181048.

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Polycystic kidney disease in the C57BL/6J (cpk) mouse is an autosomal recessive disorder which leads to the rapid development of renal cysts and kidney failure during the first 3 to 4 postnatal weeks. Previously, we showed that the cystic kidneys of affected mice have abnormally elevated levels of c-myc mRNA. In the study presented here, it is shown that mRNAs for the proto-oncogenes c-fos and c-Kiras, as well as c-myc, are markedly elevated in cystic kidneys, suggesting that there is a more general abnormality in gene expression associated with the disease. It is also evident that there are two stages to this abnormal proto-oncogene expression. In the first stage, which occurs up through the second postnatal week, there are modest increases in proto-oncogene mRNA which parallel the increased cell proliferation that accompanies cyst growth at this time. In the second stage, which occurs after the second postnatal week, there are markedly elevated levels of proto-oncogene mRNA that are seen at a time when cell proliferation is declining. The development of this latter stage suggests either that there is a fundamental abnormality intrinsic to polycystic kidneys that leads to uncontrolled proto-oncogene expression later in disease progression or that there is a secondary response in the kidney to the progressive renal failure.
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50

Watkins, David, France Dion, Michel Poisson, Jean-Yves Delattre, and Guy A. Rouleau. "Analysis of oncogene expression in primary human gliomas: Evidence for increased expression of the ros oncogene." Cancer Genetics and Cytogenetics 72, no. 2 (February 1994): 130–36. http://dx.doi.org/10.1016/0165-4608(94)90128-7.

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