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Journal articles on the topic 'C-Fos'

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Author: Grafiati

Published: 4 June 2021

Last updated: 22 February 2023

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1

Portal, M. M., G. O. Ferrero, and B. L. Caputto. "N-Terminal c-Fos tyrosine phosphorylation regulates c-Fos/ER association and c-Fos-dependent phospholipid synthesis activation." Oncogene 26, no. 24 (December 11, 2006): 3551–58. http://dx.doi.org/10.1038/sj.onc.1210137.

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2

Lee, Sung-Ho. "Effect of Swimming Exercise of c-fos, c-jun Expression in Rat Hippocampus." Journal of the Korea Contents Association 11, no. 1 (January 28, 2011): 245–53. http://dx.doi.org/10.5392/jkca.2011.11.1.245.

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3

Ferguson, Mark W. J. "Death and c-fos." Nature 366, no. 6453 (December 1993): 308. http://dx.doi.org/10.1038/366308b0.

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4

Morgan, J. M., and J. Curran. "Death and c-fos." Nature 366, no. 6453 (December 1993): 308. http://dx.doi.org/10.1038/366308c0.

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5

Cahill, Michael A. "c-Fos transrepression revisited." FEBS Letters 400, no. 1 (January 2, 1997): 9–10. http://dx.doi.org/10.1016/s0014-5793(96)01349-x.

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6

Kang, Sang-Min, Seri Lim, Seung-Jae Won, Ye-Jin Shin, Yun-Sook Lim, Byung-Yoon Ahn, and Soon B. Hwang. "c-Fos regulates hepatitis C virus propagation." FEBS Letters 585, no. 20 (September 8, 2011): 3236–44. http://dx.doi.org/10.1016/j.febslet.2011.08.041.

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7

Копаева, М. Ю., А. М. Азиева, А. Б. Черепов, М. В. Нестеренко, and И. Ю. Зарайская. "Human lactoferrin enhances the expression of transcription factor c-Fos in neuronal cultures under stimulated conditions." Nauchno-prakticheskii zhurnal «Patogenez», no. 1 (March 31, 2021): 74–78. http://dx.doi.org/10.25557/2310-0435.2021.01.74-78.

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Целью настоящей работы стало исследование влияния лактоферрина (Лф) человека на экспрессию транскрипционного фактора c-Fos в первичных нейрональных культурах после физиологической стимуляции, определение клеточной локализации Лф человека и возможной колокализации экзогенного белка с индуцированной экспрессией c-Fos. Методы. Первичные диссоциированные клеточные культуры получали из гиппокампа головного мозга новорожденных мышей (Р0-Р1) линии С57Вl/6. Индукцию экспрессии белка c-Fos в клетках осуществляли путем трехкратного добавления 50 мМ KСl в культуральную среду на 8-й день культивирования in vitro. Анализ содержания c-Fos проводили иммунофлюоресцентным методом через 2 часа после стимуляции. Результаты. Лф детектировался как в цитоплазме, так и в ядрах отдельных клеток культуры после стимуляции KСl. В ядрах некоторых клеток была выявлена колокализация включения Лф и экспрессии c-Fos. Было обнаружено, что предварительное введение Лф в культуральную среду увеличивало количество клеток, экспрессирующих c-Fos после добавления 50 мМ KСl. The aims of this research were 1) to study the effect of human lactoferrin (Lf) on the expression of the c-Fos transcription factor in primary neuronal cultures after physiological stimulation; 2) to determine the cellular localization of human Lf and possible colocalization of an exogenous protein with induced c-Fos expression. Methods. Primary dissociated cell cultures were obtained from the hippocampus of newborn C57Bl/6 mice (P0-P1). The expression of c-Fos was induced by addition of 50 mM KCl to the culture medium at 8 day in vitro. c-Fos content was analyzed by immunofluorescence 2 hrs after stimulation. Results. Lf was detected in cytoplasm and in nuclei after stimulation KCl. Lf inclusion and c-Fos expression were colocalized in the nuclei of some cells. Thus, results showed that pretreatment with Lf led to increase in the number of cells expressing c-Fos after exposure to 50 mM KCl.

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8

Coronella-Wood, June, Jerome Terrand, Haipeng Sun, and Qin M. Chen. "c-Fos Phosphorylation Induced by H2O2Prevents Proteasomal Degradation of c-Fos in Cardiomyocytes." Journal of Biological Chemistry 279, no. 32 (May 10, 2004): 33567–74. http://dx.doi.org/10.1074/jbc.m404013200.

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9

Yuan, Zhongmin, Shoufang Gong, Jingyan Luo, Zhihao Zheng, Bin Song, Shanshan Ma, Jiaoli Guo, et al. "Opposing Roles for ATF2 and c-Fos in c-Jun-Mediated Neuronal Apoptosis." Molecular and Cellular Biology 29, no. 9 (March 2, 2009): 2431–42. http://dx.doi.org/10.1128/mcb.01344-08.

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ABSTRACT The activator protein 1 (AP-1) transcription factor c-Jun is crucial for neuronal apoptosis. However, c-Jun dimerization partners and the regulation of these proteins in neuronal apoptosis remain unknown. Here we report that c-Jun-mediated neuronal apoptosis requires the concomitant activation of activating transcription factor-2 (ATF2) and downregulation of c-Fos. Furthermore, we have observed that c-Jun predominantly heterodimerizes with ATF2 and that the c-Jun/ATF2 complex promotes apoptosis by triggering ATF activity. Inhibition of c-Jun/ATF2 heterodimerization using dominant negative mutants, small hairpin RNAs, or decoy oligonucleotides was able to rescue neurons from apoptosis, whereas constitutively active ATF2 and c-Jun mutants were found to synergistically stimulate apoptosis. Bimolecular fluorescence complementation analysis confirmed that, in living neurons, c-Fos downregulation facilitates c-Jun/ATF2 heterodimerization. A chromatin immunoprecipitation assay also revealed that c-Fos expression prevents the binding of c-Jun/ATF2 heterodimers to conserved ATF sites. Moreover, the presence of c-Fos is able to suppress the expression of c-Jun/ATF2-mediated target genes and, therefore, apoptosis. Taken together, our findings provide evidence that potassium deprivation-induced neuronal apoptosis is mediated by concurrent upregulation of c-Jun/ATF2 heterodimerization and downregulation of c-Fos expression. This paradigm demonstrates opposing roles for ATF2 and c-Fos in c-Jun-mediated neuronal apoptosis.

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10

Velazquez, Fabiola N., Beatriz L. Caputto, and François D. Boussin. "c-Fos importance for brain development." Aging 7, no. 12 (December 17, 2015): 1028–29. http://dx.doi.org/10.18632/aging.100862.

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11

Lee, J., K. Mehta, MB Blick, JU Gutterman, and G. Lopez-Berestein. "Expression of c-fos, c-myb, and c-myc in human monocytes: correlation with monocytic differentiation." Blood 69, no. 5 (May 1, 1987): 1542–45. http://dx.doi.org/10.1182/blood.v69.5.1542.1542.

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Abstract Terminal differentiation of human monocytic leukemia cells (THP-1 cells) was associated with the induction of c-fos, the down regulation of c-myb, and no significant change in the level of c-myc expression. Gamma interferon, which resulted in a slight decrease in c-myb but no change in c-fos or c-myc expression, had a transient antiproliferative effect without a morphological or functional differentiation of THP-1 cells. Resting human peripheral blood monocytes have a high c-fos, a low c-myc, and no detectable c-myb expression. These findings suggest that a switch in c-fos/c-myb expression is associated with the terminal differentiation of cells of the monocytic lineage.

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12

Lee, J., K. Mehta, MB Blick, JU Gutterman, and G. Lopez-Berestein. "Expression of c-fos, c-myb, and c-myc in human monocytes: correlation with monocytic differentiation." Blood 69, no. 5 (May 1, 1987): 1542–45. http://dx.doi.org/10.1182/blood.v69.5.1542.bloodjournal6951542.

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Terminal differentiation of human monocytic leukemia cells (THP-1 cells) was associated with the induction of c-fos, the down regulation of c-myb, and no significant change in the level of c-myc expression. Gamma interferon, which resulted in a slight decrease in c-myb but no change in c-fos or c-myc expression, had a transient antiproliferative effect without a morphological or functional differentiation of THP-1 cells. Resting human peripheral blood monocytes have a high c-fos, a low c-myc, and no detectable c-myb expression. These findings suggest that a switch in c-fos/c-myb expression is associated with the terminal differentiation of cells of the monocytic lineage.

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13

Bossis, Guillaume, Cécile E. Malnou, Rosa Farras, Elisabetta Andermarcher, Robert Hipskind, Manuel Rodriguez, Darja Schmidt, Stefan Muller, Isabelle Jariel-Encontre, and Marc Piechaczyk. "Down-Regulation of c-Fos/c-Jun AP-1 Dimer Activity by Sumoylation." Molecular and Cellular Biology 25, no. 16 (August 15, 2005): 6964–79. http://dx.doi.org/10.1128/mcb.25.16.6964-6979.2005.

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ABSTRACT The inducible transcriptional complex AP-1, composed of c-Fos and c-Jun proteins, is crucial for cell adaptation to many environmental changes. While its mechanisms of activation have been extensively studied, how its activity is restrained is poorly understood. We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229. Sumoylation of c-Fos preferentially occurs in the context of c-Jun/c-Fos heterodimers. Using nonsumoylatable mutants of c-Fos and c-Jun as well as a chimeric protein mimicking sumoylated c-Fos, we show that sumoylation entails lower AP-1 transactivation activity. Interestingly, single sumoylation at any of the three acceptor sites of the c-Fos/c-Jun dimer is sufficient to substantially reduce transcription activation. The lower activity of sumoylated c-Fos is not due to inhibition of protein entry into the nucleus, accelerated turnover, and intrinsic inability to dimerize or to bind to DNA. Instead, cell fractionation experiments suggest that decreased transcriptional activity of sumoylated c-Fos is associated with specific intranuclear distribution. Interestingly, the phosphorylation of threonine 232 observed upon expression of oncogenically activated Ha-Ras is known to superactivate c-Fos transcriptional activity. We show here that it also inhibits c-Fos sumoylation, revealing a functional antagonism between two posttranslational modifications, each occurring within a different moiety of a bipartite transactivation domain of c-Fos. Finally we report that the sumoylation of c-Fos is a dynamic process that can be reversed via multiple mechanisms. This supports the idea that this modification does not constitute a final inactivation step that necessarily precedes protein degradation.

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14

Feng, J. L., and B. Villeponteau. "Serum stimulation of the c-fos enhancer induces reversible changes in c-fos chromatin structure." Molecular and Cellular Biology 10, no. 3 (March 1990): 1126–33. http://dx.doi.org/10.1128/mcb.10.3.1126-1133.1990.

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Transcription of the proto-oncogene c-fos is known to be activated by growth factors in serum and subsequently repressed by the Fos protein. We show that generalized DNase I sensitivity of c-fos chromatin correlates closely with enhancer activity during induction, repression, and superinduction of the c-fos gene. Within 90 s of serum stimulation, proximal DNA sequences on both sides of the enhancer exhibit increased DNase I sensitivity. Within 5 min, elevated DNase I sensitivity spreads to chromatin at the distal 3' end of the c-fos gene. These results suggest that an open state of chromatin is propagated in both directions from the enhancer. The induced alterations in chromatin structure precede the increased transcriptional activity of the c-fos gene, suggesting that these changes in chromatin structure potentiate transcription.

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15

Feng, J. L., and B. Villeponteau. "Serum stimulation of the c-fos enhancer induces reversible changes in c-fos chromatin structure." Molecular and Cellular Biology 10, no. 3 (March 1990): 1126–33. http://dx.doi.org/10.1128/mcb.10.3.1126.

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Transcription of the proto-oncogene c-fos is known to be activated by growth factors in serum and subsequently repressed by the Fos protein. We show that generalized DNase I sensitivity of c-fos chromatin correlates closely with enhancer activity during induction, repression, and superinduction of the c-fos gene. Within 90 s of serum stimulation, proximal DNA sequences on both sides of the enhancer exhibit increased DNase I sensitivity. Within 5 min, elevated DNase I sensitivity spreads to chromatin at the distal 3' end of the c-fos gene. These results suggest that an open state of chromatin is propagated in both directions from the enhancer. The induced alterations in chromatin structure precede the increased transcriptional activity of the c-fos gene, suggesting that these changes in chromatin structure potentiate transcription.

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16

Prywes, R., T. M. Fisch, and R. G. Roeder. "Transcriptional Regulation of c-fos." Cold Spring Harbor Symposia on Quantitative Biology 53 (January 1, 1988): 739–48. http://dx.doi.org/10.1101/sqb.1988.053.01.084.

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17

Walsh, Kenneth. "MyoD and c-fos expression." Nature 365, no. 6447 (October 1993): 611–12. http://dx.doi.org/10.1038/365611b0.

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18

Harel-Bellan, A. "MyoD and c-fos expression." Nature 365, no. 6447 (October 1993): 612. http://dx.doi.org/10.1038/365612a0.

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19

NAKAO, S., J. KURATA, T. ARAI, M. MURAKAWA, T. ADACHI, M. N. AVRAMOV, K. MORI, O. YASUHARA, I. TOOYAMA, and H. KIMURA. "Lignocaine-induced convulsion does not induce c-fos protein (c-Fos) in rat hippocampus." Acta Anaesthesiologica Scandinavica 38, no. 8 (November 1994): 845–51. http://dx.doi.org/10.1111/j.1399-6576.1994.tb04016.x.

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20

Wilson, T., and R. Treisman. "Fos C-terminal mutations block down-regulation of c-fos transcription following serum stimulation." EMBO Journal 7, no. 13 (December 1988): 4193–202. http://dx.doi.org/10.1002/j.1460-2075.1988.tb03316.x.

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21

Araujo, F. C., A. B. Reis, C. A. Oliveira, and F. M. Reis. "Expression of the proto-oncogene c-fos and the immunolocalization of c-Fos, phosphorylated c-Fos and ERbeta proteins in the human testis." Fertility and Sterility 88 (September 2007): S384. http://dx.doi.org/10.1016/j.fertnstert.2007.07.1276.

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22

Roffler-Tarlov, S., J. J. Brown, E. Tarlov, J. Stolarov, D. L. Chapman, M. Alexiou, and V. E. Papaioannou. "Programmed cell death in the absence of c-Fos and c-Jun." Development 122, no. 1 (January 1, 1996): 1–9. http://dx.doi.org/10.1242/dev.122.1.1.

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Programmed cell death, or apoptosis, is a normal process in the development of a variety of embryonic and adult tissues, and is also observed in several pathological conditions. Several recent studies, using both expression and functional assays, have implicated the transcription factor, AP-1, in the regulation of programmed cell death, and specifically implicate the genes c-fos and c-jun, as well as some other family members. If the products of the c-fos and/or c-jun genes are essential components in the cascade of events that leads to programmed cell death in mammalian cells, it follows that cell death would not occur in mice lacking functional copies of these genes. We have made use of null mutations in the c-fos and c-jun genes that were produced by gene targeting (Johnson, R.S., Spiegelman, B.M. and Papaioannou, V.E. (1992). Cell 71, 577–586; Johnson, R.S., Van Lingen, B., Papaioannou, V.E. and Spiegelman, B.M. (1993). Genes Dev. 7, 1309–1317) to investigate this possibility. Cell death was assayed using an in situ apoptosis assay in c-fos null embryos and adults, c-jun null embryos, and c-fos/c-jun double null embryos compared with control mice. The occurrence of cell death in c-fos null mice was also assessed in two experimental conditions that normally lead to neuronal cell death. The first was unilateral section of the sciatic nerve in neonates, which leads to the death of anterior horn cells of the spinal cord on the operated side. The second was a genetic cross combining the weaver mutation, which causes death of cerebellar granule cells, with the c-fos mutation. Our results show that programmed cell death occurs normally in developing embryonic tissues and adult thymus and ovary, regardless of the absence of a functional c-fos gene. Furthermore, absence of c-fos had no effect on neuronal cell death in the spinal cord following sciatic nerve section, or in heterozygous weavers' cerebellae. Finally, the results show that programmed cell death can take place in embryos lacking both Fos and Jun.

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23

Kim, JeongHyun, Kevin Montagne, Takashi Ushida, and Katsuko S. Furukawa. "10205 Effect of Hydrostatic pressure on chondrogenesis and c-Fos." Proceedings of Conference of Kanto Branch 2014.20 (2014): _10205–1_—_10205–2_. http://dx.doi.org/10.1299/jsmekanto.2014.20._10205-1_.

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24

Faraldi, F., A. Calzolari, M. Forni, F. L. Chiarelli Mincione, and G. Alfieri. "Immunohistochemical Analysis of c-Fos and c-Jun in Retinoblastoma." Acta geneticae medicae et gemellologiae: twin research 45, no. 1-2 (April 1996): 289–91. http://dx.doi.org/10.1017/s0001566000001483.

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AbstractThe c-fos promoter is negatively regulated by the retinoblastoma (Rb)-suceptibility-gene- encoded protein as well as by other genes involved in the control of transcription, cell cycle regulation and neoplastic transformation. We have examined by immunohistochemistry the c-Fos and c-Jun proteins in five cases of retinoblastoma in order to evaluate eventual alterations in their expression in vivo, possibly related to a gene mutation or to loss of Rb negative control.

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25

Morello, D., M. J. Fitzgerald, C. Babinet, and N. Fausto. "c-myc, c-fos, and c-jun regulation in the regenerating livers of normal and H-2K/c-myc transgenic mice." Molecular and Cellular Biology 10, no. 6 (June 1990): 3185–93. http://dx.doi.org/10.1128/mcb.10.6.3185-3193.1990.

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We investigated the mechanisms of regulation of c-myc, c-fos, and c-jun at the early stages of liver regeneration in mice. We show that the transient increase in steady-state levels of c-myc mRNA at the start of liver regeneration is most probably regulated by posttranscriptional mechanisms. Although there was a marked increase in c-myc transcriptional initiation shortly after partial hepatectomy, a block in elongation prevented the completion of most transcripts. To gain further information on the mechanism of regulation of c-myc expression during liver regeneration, we used transgenic mice harboring the human c-myc gene driven by the H-2K promoter. In these animals, the murine c-myc responded to the growth stimulus generated by partial hepatectomy, whereas the expression of the transgene was constitutive and did not change in the regenerating liver. However, the mRNA from both genes increased markedly after cycloheximide injection, suggesting that the regulation of c-myc mRNA abundance in the regenerating liver differs from that occurring after protein synthesis inhibition. Furthermore, we show that in normal mice c-fos and c-jun mRNA levels and transcriptional rates increase within 30 min after partial hepatectomy. c-fos transcriptional elongation was restricted in nongrowing liver, but the block was partially relieved in the regenerating liver. Nevertheless, for both c-fos and c-jun, changes in steady-state mRNA detected after partial hepatectomy were much greater than the transcriptional increase. In the regenerating liver of H-2K/c-myc mice, c-fos and c-jun expression was diminished, whereas mouse c-myc expression was enhanced in comparison with that in nontransgenic animals.

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26

Morello, D., M. J. Fitzgerald, C. Babinet, and N. Fausto. "c-myc, c-fos, and c-jun regulation in the regenerating livers of normal and H-2K/c-myc transgenic mice." Molecular and Cellular Biology 10, no. 6 (June 1990): 3185–93. http://dx.doi.org/10.1128/mcb.10.6.3185.

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We investigated the mechanisms of regulation of c-myc, c-fos, and c-jun at the early stages of liver regeneration in mice. We show that the transient increase in steady-state levels of c-myc mRNA at the start of liver regeneration is most probably regulated by posttranscriptional mechanisms. Although there was a marked increase in c-myc transcriptional initiation shortly after partial hepatectomy, a block in elongation prevented the completion of most transcripts. To gain further information on the mechanism of regulation of c-myc expression during liver regeneration, we used transgenic mice harboring the human c-myc gene driven by the H-2K promoter. In these animals, the murine c-myc responded to the growth stimulus generated by partial hepatectomy, whereas the expression of the transgene was constitutive and did not change in the regenerating liver. However, the mRNA from both genes increased markedly after cycloheximide injection, suggesting that the regulation of c-myc mRNA abundance in the regenerating liver differs from that occurring after protein synthesis inhibition. Furthermore, we show that in normal mice c-fos and c-jun mRNA levels and transcriptional rates increase within 30 min after partial hepatectomy. c-fos transcriptional elongation was restricted in nongrowing liver, but the block was partially relieved in the regenerating liver. Nevertheless, for both c-fos and c-jun, changes in steady-state mRNA detected after partial hepatectomy were much greater than the transcriptional increase. In the regenerating liver of H-2K/c-myc mice, c-fos and c-jun expression was diminished, whereas mouse c-myc expression was enhanced in comparison with that in nontransgenic animals.

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27

Gajate, Consuelo, Maria Teresa Alonso, Thomas Schimmang, and Faustino Mollinedo. "C-Fos Is Not Essential for Apoptosis." Biochemical and Biophysical Research Communications 218, no. 1 (January 1996): 267–72. http://dx.doi.org/10.1006/bbrc.1996.0047.

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28

Kim, S. J., and C. R. Kahn. "Insulin stimulates phosphorylation of c-Jun, c-Fos, and Fos-related proteins in cultured adipocytes." Journal of Biological Chemistry 269, no. 16 (April 1994): 11887–92. http://dx.doi.org/10.1016/s0021-9258(17)32656-x.

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29

Kerr, L., J. Holt, and L. Matrisian. "Growth factors regulate transin gene expression by c-fos-dependent and c-fos-independent pathways." Science 242, no. 4884 (December 9, 1988): 1424–27. http://dx.doi.org/10.1126/science.2462278.

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30

Levi, Ben-Zion, John W. Kasik, and Keiko Ozato. "c-fos antisense RNA blocks expression of c-fos gene in F9 embryonal carcinoma cells." Cell Differentiation and Development 25 (November 1988): 95–101. http://dx.doi.org/10.1016/0922-3371(88)90105-0.

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31

Yu, Chang-Tze Ricky, Jiunn-Chyi Wu, Mei-Chih Liao, Shih-Lan Hsu, and Chi-Ying F. Huang. "Identification of c-Fos as a mitotic phosphoprotein: regulation of c-Fos by Aurora-A." Journal of Biomedical Science 15, no. 1 (October 10, 2007): 79–87. http://dx.doi.org/10.1007/s11373-007-9209-8.

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32

Pukac, L. A., J. J. Castellot, T. C. Wright, B. L. Caleb, and M. J. Karnovsky. "Heparin inhibits c-fos and c-myc mRNA expression in vascular smooth muscle cells." Cell Regulation 1, no. 5 (April 1990): 435–43. http://dx.doi.org/10.1091/mbc.1.5.435.

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Heparin is a potent inhibitor of vascular smooth muscle cell (VSMC) growth. In this paper we show that heparin suppressed the induction of c-fos and c-myc mRNA in rat and calf VSMC. This effect of heparin is closely associated with its growth-inhibitory activity, as shown by isolating and characterizing a strain of rat VSMC that was resistant to heparin's antiproliferative effect; heparin did not suppress c-fos mRNA induction in these cells. Moreover, neither a nonantiproliferative heparin fragment or other glycosaminoglycans that lack growth-inhibitory activity repressed c-fos or c-myc mRNA levels. The effect of heparin on c-fos mRNA induction was selective for specific mitogens, as heparin inhibited c-fos mRNA induction in phorbol 12-myristate 13-acetate (TPA) stimulated but not epidermal growth factor (EGF) stimulated VSMC. The effect of heparin on gene expression is independent of ongoing protein synthesis, and inhibition of c-fos mRNA is at the transcriptional level. These results suggest that heparin may selectively inhibit a protein kinase C-dependent pathway for protooncogene induction and that this may be one mechanism used by heparin to inhibit cell proliferation.

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33

Tsurumi, C., N. Ishida, T. Tamura, A. Kakizuka, E. Nishida, E. Okumura, T. Kishimoto, M. Inagaki, K. Okazaki, and N. Sagata. "Degradation of c-Fos by the 26S proteasome is accelerated by c-Jun and multiple protein kinases." Molecular and Cellular Biology 15, no. 10 (October 1995): 5682–87. http://dx.doi.org/10.1128/mcb.15.10.5682.

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c-Fos is associated with c-Jun to increase the transcription of a number of target genes and is a nuclear proto-oncoprotein with a very short half-life. This instability of c-Fos may be important in regulation of the normal cell cycle. Here we report a mechanism for degradation of c-Fos. Coexpression of c-Fos and c-Jun in HeLa cells caused marked increase in the instability of c-Fos, whereas v-Fos, the retroviral counterpart of c-Fos, was stable irrespective of the coexpression of c-Jun. Interestingly, deletion of the C-terminal PEST region of c-Fos, which is altered in v-Fos by a frameshift mutation, greatly enhanced its stability, with loss of the effect of c-Jun on its stability. c-Fos synthesized in vitro was degraded by the 26S proteasome in a ubiquitin-dependent fashion. Simple association with c-Jun had no effect on the degradation of c-Fos, but the additions of three protein kinases, mitogen-activated protein kinase, casein kinase II, and CDC2 kinase, resulted in marked acceleration of its degradation by the proteasome-ubiquitin system, though only in the presence of c-Jun. In contrast, v-Fos and c-Fos with a truncated PEST motif were not degraded, suggesting that they escaped from down-regulation by breakdown. These findings indicate a new oncogenic pathway induced by acquisition of intracellular stability of a cell cycle modulatory factor.

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34

Kunimi, Kazuto, Tadao Uchibayashi, and Haruo Hisazumi. "OVEREXPRESSION OF C-MYC, C-FOS AND HARVEY RAS ONCOGENES IN RENAL CANCERS." Japanese Journal of Urology 82, no. 12 (1991): 1924–29. http://dx.doi.org/10.5980/jpnjurol1989.82.1924.

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35

Lu, L., and C. D. Logsdon. "CCK, bombesin, and carbachol stimulate c-fos, c-jun, and c-myc oncogene expression in rat pancreatic acini." American Journal of Physiology-Gastrointestinal and Liver Physiology 263, no. 3 (September 1, 1992): G327—G332. http://dx.doi.org/10.1152/ajpgi.1992.263.3.g327.

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To identify possible nuclear signals mediating long-term regulation of the pancreas by gastrointestinal hormones, the expression of c-fos, c-jun, and c-myc was investigated in rat pancreatic acini. Stimulation of the acini with cholecystokinin octapeptide (CCK-8, 100 pM), bombesin (10 nM), or carbachol (10 microM), but not gastrin (100 nM), secretin (100 nM), or vasoactive intestinal peptide (10 nM) induced an increase in oncogene mRNA expression. The percent increases of c-fos, c-jun, and c-myc mRNA were 207 +/- 40, 171 +/- 26, and 46 +/- 19 (n = 5) for CCK-8; 223 +/- 71, 159 +/- 31, and 43 +/- 21 (n = 5) for bombesin; and 125 +/- 51, 123 +/- 58, and 67 +/- 19 (n = 5) for carbachol, respectively. CCK-induced increases in oncogene mRNA were rapid and transient. c-fos and c-jun mRNA levels were increased after 30 min stimulation, peaked at 1 h, and returned to basal level in 2 h. Activation of c-myc was more prolonged with levels remaining elevated for at least 3 h. The effects of CCK-8 were concentration dependent. Detectable stimulation was seen at 10 pM; maximal stimulation occurred at 10 nM and was not affected by further increase in the concentration of CCK-8. JMV-180, a high-affinity site CCK receptor agonist and low-affinity site antagonist, alone did not stimulate c-fos mRNA expression but inhibited c-fos mRNA expression induced by CCK-8. These results suggest that the interaction between CCK and the low-affinity state of the CCK receptor is responsible for oncogene activation.

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36

Sariban, E., T. Mitchell, A. Rambaldi, and DW Kufe. "c-sis but not c-fos gene expression is lineage specific in human myeloid cells." Blood 71, no. 2 (February 1, 1988): 488–93. http://dx.doi.org/10.1182/blood.v71.2.488.488.

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Abstract Expression of both the c-fos and c-sis protooncogenes during myeloid differentiation has been detected in cells of the monocytic lineage. Since an increase in c-fos transcripts was not detected during dimethylsulfoxide induced HL-60 granulocytic differentiation, it was suggested that within the myeloid series c-fos gene expression might be lineage specific. In the present study, we have determined whether expression of the c-fos and c-sis genes is indeed specific for the monocytic pathway or rather common to both the granulocyte and monocyte pathways. C-fos and c-sis gene expression was analyzed in freshly isolated human granulocytes and monocytes, in human HL-60 promyelocytic leukemia cells induced to differentiate along the granulocytic or monocytic pathway, in myeloblasts from five patients with the M1 or M2 subtype of acute myeloblastic leukemia (AML) and in blasts from six patients with M4 myelomonocytic leukemia. The level of c-fos mRNA was fifteen times higher in granulocytes as compared with monocytes. An increase in c-fos expression was also found in HL-60 cells differentiated along the granulocytic pathway after exposure to hypoxanthine, hexamethylene bisacetamide, and the combination of retinoic acid and dibutyryl adenosine 3′5′ cyclic monophosphate. Three of 5 M1 and M2 leukemic myeloblast preparations depleted of lymphoid and monocytic cells and all six M4 leukemic cells expressed c-fos transcripts. In contrast, c-sis gene transcripts were detectable in monocytes and during drug induced monocytic differentiation of the HL- 60 cells but not in granulocytes during granulocytic differentiation of the HL-60 cells or in AML samples. Thus, in the myeloid series, c-sis gene expression is lineage specific while expression of the c-fos gene is found in both lineages and may be related to metabolic pathways common to both granulocytes and monocytes.

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37

Sariban, E., T. Mitchell, A. Rambaldi, and DW Kufe. "c-sis but not c-fos gene expression is lineage specific in human myeloid cells." Blood 71, no. 2 (February 1, 1988): 488–93. http://dx.doi.org/10.1182/blood.v71.2.488.bloodjournal712488.

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Expression of both the c-fos and c-sis protooncogenes during myeloid differentiation has been detected in cells of the monocytic lineage. Since an increase in c-fos transcripts was not detected during dimethylsulfoxide induced HL-60 granulocytic differentiation, it was suggested that within the myeloid series c-fos gene expression might be lineage specific. In the present study, we have determined whether expression of the c-fos and c-sis genes is indeed specific for the monocytic pathway or rather common to both the granulocyte and monocyte pathways. C-fos and c-sis gene expression was analyzed in freshly isolated human granulocytes and monocytes, in human HL-60 promyelocytic leukemia cells induced to differentiate along the granulocytic or monocytic pathway, in myeloblasts from five patients with the M1 or M2 subtype of acute myeloblastic leukemia (AML) and in blasts from six patients with M4 myelomonocytic leukemia. The level of c-fos mRNA was fifteen times higher in granulocytes as compared with monocytes. An increase in c-fos expression was also found in HL-60 cells differentiated along the granulocytic pathway after exposure to hypoxanthine, hexamethylene bisacetamide, and the combination of retinoic acid and dibutyryl adenosine 3′5′ cyclic monophosphate. Three of 5 M1 and M2 leukemic myeloblast preparations depleted of lymphoid and monocytic cells and all six M4 leukemic cells expressed c-fos transcripts. In contrast, c-sis gene transcripts were detectable in monocytes and during drug induced monocytic differentiation of the HL- 60 cells but not in granulocytes during granulocytic differentiation of the HL-60 cells or in AML samples. Thus, in the myeloid series, c-sis gene expression is lineage specific while expression of the c-fos gene is found in both lineages and may be related to metabolic pathways common to both granulocytes and monocytes.

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38

Holt, J. T. "Antisense rescue defines specialized and generalized functional domains for c-Fos protein." Molecular and Cellular Biology 13, no. 6 (June 1993): 3821–30. http://dx.doi.org/10.1128/mcb.13.6.3821-3830.1993.

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Serum induces the expression of a number of proteins with similar transcriptional properties, including those encoded by the proto-oncogenes c-fos and c-jun. This study employs a novel antisense rescue method to determine whether antisense-resistant genes (constructed by deletion of antisense RNA target sequences) can replace c-fos expression during serum-induced DNA synthesis. Immunoprecipitation studies and nuclease protection assays demonstrated that anti-fos RNA inhibited endogenous c-fos expression but did not inhibit expression of transfected antisense-resistant mutant c-fos genes. The results of nuclear-labelling and cellular-proliferation studies indicated that C terminally truncated Fos mutants, including FBR v-fos, could not rescue endogenous Fos, although full-length and minimally truncated c-fos expression vectors could restore serum-induced DNA synthesis in cells expressing anti-fos RNA. Overexpression of c-Jun protein (Jun) could not restore serum-induced DNA synthesis to cells expressing inducible anti-fos RNA despite equivalent transactivation of an AP-1 target gene. Thus, the antisense rescue method defines a specialized function for c-Fos protein which is distinct from the function(s) of Jun and/or transforming FBR v-Fos proteins.

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39

Holt, J. T. "Antisense rescue defines specialized and generalized functional domains for c-Fos protein." Molecular and Cellular Biology 13, no. 6 (June 1993): 3821–30. http://dx.doi.org/10.1128/mcb.13.6.3821.

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Serum induces the expression of a number of proteins with similar transcriptional properties, including those encoded by the proto-oncogenes c-fos and c-jun. This study employs a novel antisense rescue method to determine whether antisense-resistant genes (constructed by deletion of antisense RNA target sequences) can replace c-fos expression during serum-induced DNA synthesis. Immunoprecipitation studies and nuclease protection assays demonstrated that anti-fos RNA inhibited endogenous c-fos expression but did not inhibit expression of transfected antisense-resistant mutant c-fos genes. The results of nuclear-labelling and cellular-proliferation studies indicated that C terminally truncated Fos mutants, including FBR v-fos, could not rescue endogenous Fos, although full-length and minimally truncated c-fos expression vectors could restore serum-induced DNA synthesis in cells expressing anti-fos RNA. Overexpression of c-Jun protein (Jun) could not restore serum-induced DNA synthesis to cells expressing inducible anti-fos RNA despite equivalent transactivation of an AP-1 target gene. Thus, the antisense rescue method defines a specialized function for c-Fos protein which is distinct from the function(s) of Jun and/or transforming FBR v-Fos proteins.

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40

McBride, Kevin, and Mona Nemer. "The C-Terminal Domain of c-fos Is Required for Activation of an AP-1 Site Specific forjun-fos Heterodimers." Molecular and Cellular Biology 18, no. 9 (September 1, 1998): 5073–81. http://dx.doi.org/10.1128/mcb.18.9.5073.

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ABSTRACT The proto-oncogenes jun and fos are members of the AP-1 family of transcription factors, which activate transcription of target genes via the tetradecanoyl phorbol acetate response element (TRE). Both jun and foscontain activation domains, but their relative contributions to transcriptional activation of different TREs remain unclear. It is not apparent whether the cellular availability of specific AP-1 members is the major determinant for regulation of TREs or whether other factors including the TRE sequence itself contribute to selectivity. We have identified in the promoter of the rat atrial natriuretic factor (ANF) a novel AP-1 site which is unresponsive to jun homodimers and is inducible only in the presence of c-fos. This activation is potentiated by mitogen-activated protein (MAP) kinase. The jun proteins appear to be required solely to tether c-fos to the promoter, and c-fos mutants lacking putative activation domains abrogate transactivation. Unexpectedly, the oncogenic form of c-foswhich diverges most significantly in the carboxy-terminal 50 amino acids is unable to mediate transactivation at this specialized AP-1 site. Mutations within the C terminus of c-fos at serine residues that are phosphorylation targets for growth factors and MAP kinase completely abrogate transactivation and block potentiation by MAP kinase. Using GAL4 fusions, we show that the 90-amino-acid C terminus of c-fos contains autonomous activation domains and that the serine residues are essential for full activity. These results suggest that phosphorylation of the C terminus of c-fos affects its transactivation properties and provide evidence for novel regulatory mechanisms that may contribute to biologic specificities of the AP-1 transcription complex.

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41

Yuen, Man-Fung, Pui-Chee Wu, Vicky Ching-Har Lai, Johnson Yiu-Nam Lau, and Ching-Lung Lai. "Expression of c-Myc, c-Fos, and c-Jun in hepatocellular carcinoma." Cancer 91, no. 1 (January 1, 2001): 106–12. http://dx.doi.org/10.1002/1097-0142(20010101)91:1<106::aid-cncr14>3.0.co;2-2.

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42

Gilman, M. Z., L. A. Berkowitz, J. R. Feramisco, B. R. Franza, R. M. Graham, K. T. Riabowol, and W. A. Ryan. "Intracellular Mediators of c-fos Induction." Cold Spring Harbor Symposia on Quantitative Biology 53 (January 1, 1988): 761–67. http://dx.doi.org/10.1101/sqb.1988.053.01.086.

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43

He, Huiling, Xiao-Mei Qi, Johannes Grossmann, and Clark W. Distelhorst. "c-Fos Degradation by the Proteasome." Journal of Biological Chemistry 273, no. 39 (September 25, 1998): 25015–19. http://dx.doi.org/10.1074/jbc.273.39.25015.

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44

Janknecht, Ralf. "Regulation of the c-fos Promoter." Immunobiology 193, no. 2-4 (July 1995): 137–42. http://dx.doi.org/10.1016/s0171-2985(11)80536-x.

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45

Ofir, Rivka, V. J. Dwarki, Dana Rashid, and Inder M. Verma. "Phosphorylation of the C terminus of Fos protein is required for transcriptional transrepression of the c-fos promoter." Nature 348, no. 6296 (November 1990): 80–82. http://dx.doi.org/10.1038/348080a0.

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46

Wu, Bin. "Expression of c-fos and c-jun proto-oncogenes by ovine preimplantation embryos." Zygote 4, no. 3 (August 1996): 211–17. http://dx.doi.org/10.1017/s0967199400003129.

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SummaryThe c-fos and c-jun proto-oncogenes are involved in the regulation of gene expression, cell proliferation, differentiation and tumorigenesis. Embryogenesis, like tumorigenesis, involves dramatic cell growth, cleavage and differentiation processes. Activation of the c-fos and c-jun proto-oncogenes in sheep conceptuses during the period of rapid growth and elongation was examined using reverse transcription and polymerase chain reaction (RT-PCR). The specificity of PCR products was determined by Southern blot hybridisation analysis with a non-radioactive DNA probe. A band corresponding to a 507 bp fragment (predicted amplified c-fos gene cDNA product) was observed in 3 of 9 day-13, 1 of 4 day-14 and 1 of 2 day-16 embryos. Meanwhile, a 400 bp c-jun transcript was aslo detected in 1 or 2 day-12, 3 of 9 day-13 and 2 of 2 day-16 embroyos. These results suggest that mRNA transcripts of c-fos and c-jun proto-oncogenes were specifically expressed during the period of ovine embryonic elongation and may have a possible role in preimplantation embryonic development of sheep.

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47

Grigoriadis, AE, K. Schellander, ZQ Wang, and EF Wagner. "Osteoblasts are target cells for transformation in c-fos transgenic mice." Journal of Cell Biology 122, no. 3 (August 1, 1993): 685–701. http://dx.doi.org/10.1083/jcb.122.3.685.

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We have generated transgenic mice expressing the proto-oncogene c-fos from an H-2Kb class I MHC promoter as a tool to identify and isolate cell populations which are sensitive to altered levels of Fos protein. All homozygous H2-c-fosLTR mice develop osteosarcomas with a short latency period. This phenotype is specific for c-fos as transgenic mice expressing the fos- and jun-related genes, fosB and c-jun, from the same regulatory elements do not develop any pathology despite high expression in bone tissues. The c-fos transgene is not expressed during embryogenesis but is expressed after birth in bone tissues before the onset of tumor formation, specifically in putative preosteoblasts, bone-forming osteoblasts, osteocytes, as well as in osteoblastic cells present within the tumors. Primary and clonal cell lines established from c-fos-induced tumors expressed high levels of exogenous c-fos as well as the bone cell marker genes, type I collagen, alkaline phosphatase, and osteopontin/2ar. In contrast, osteocalcin/BGP expression was either low or absent. All cell lines were tumorigenic in vivo, some of which gave rise to osteosarcomas, expressing exogenous c-fos mRNA, and Fos protein in osteoblastic cells. Detailed analysis of one osteogenic cell line, P1, and several P1-derived clonal cell lines indicated that bone-forming osteoblastic cells were transformed by Fos. The regulation of osteocalcin/BGP and alkaline phosphatase gene expression by 1,25-dihydroxyvitamin D3 was abrogated in P1-derived clonal cells, whereas glucocorticoid responsiveness was unaltered. These results suggest that high levels of Fos perturb the normal growth control of osteoblastic cells and exert specific effects on the expression of the osteoblast phenotype.

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48

Sharp, FR, SM Sagar, K. Hicks, D. Lowenstein, and K. Hisanaga. "c-fos mRNA, Fos, and Fos-related antigen induction by hypertonic saline and stress." Journal of Neuroscience 11, no. 8 (August 1, 1991): 2321–31. http://dx.doi.org/10.1523/jneurosci.11-08-02321.1991.

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49

Wang, L. D., M. Wang, A. Todisco, E. Grand, and J. del Valle. "The human histamine H2 receptor regulates c-jun and c-fos in a differential manner." American Journal of Physiology-Cell Physiology 278, no. 6 (June 1, 2000): C1246—C1255. http://dx.doi.org/10.1152/ajpcell.2000.278.6.c1246.

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Previously, we demonstrated that activation of the human H2 receptor (hH2R) leads to an increase in c- fos transcription and cell proliferation. The purpose of these studies was to examine whether hH2R regulates c- jun expression and, if so, explore the mechanisms by which it does so. Histamine induced an increase in c- jun mRNA in human embryonic kidney cells stably transfected with the hH2R (maximal effect: 554.6 ± 86.8% of control). The protein kinase C (PKC) inhibitors staurosporine (10−6 M) and GF-109203X (10−6 M) significantly inhibited histamine-stimulated c- fos mRNA while not altering c- jun expression. The protein kinase A (PKA) pathway inhibitors Rp-cAMP and protein kinase inhibitor did not affect the action of histamine on c- jun or c- fos mRNA. Histamine (10−4M) stimulated extracellularly regulated kinase 2 tyrosine phosphorylation. The specific inhibitor of the mitogen-activated protein (MAP) kinase pathway, PD-98059 (5 × 10−5 M), significantly inhibited histamine-induced c- fos and c- jun mRNA. Of interest, the p70 S6 kinase inhibitor rapamycin (10−6 M) but not wortmannin decreased histamine-stimulated c- jun mRNA by 58.5 ± 12% (mean ± SE, n = 4) while not significantly altering c- fos message. Histamine (10−4 M) also led to an ∼4.5-fold increase in Jun NH2-terminal kinase activity in a PKC-, PKA-, and MAP kinase-independent but rapamycin-sensitive manner. Our findings suggest that histamine stimulates both c- fos and c- jun mRNA in a differential manner. PKC is involved in histamine-mediated c-fos activation, whereas p70 S6 kinase is important for linkage of this receptor to c- jun.

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50

Yeh, C. K., I. S. Ambudkar, and E. Kousvelari. "Differential expression of early response genes, c-jun, c-fos, and jun B, in A5 cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 263, no. 6 (December 1, 1992): G934—G938. http://dx.doi.org/10.1152/ajpgi.1992.263.6.g934.

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We examined the expression of c-fos, c-jun, and jun B after activation of different signal transduction pathways in the A5 rat salivary epithelial cell line. Stimulation of beta-adrenergic receptors by isoproterenol, or addition of 8-bromoadenosine 3',5'-cyclic monophosphate, induces the expression of c-fos and jun B by a protein kinase A-mediated pathway. Phorbol 12-myristate 13-acetate (PMA) induces the expression of all three genes, but with different kinetics. While c-fos and jun B mRNA levels increase early (1 h) after stimulation and transiently, those of c-jun remain higher than control even after stimulation for 8 h and return to basal levels by 24 h. Inhibitors of protein kinase C block the effect of PMA on c-fos, c-jun, and jun B expression, indicating that these genes are also regulated by a protein kinase C-mediated mechanism in A5 cells. Increases in cytosolic Ca2+ by A23187 or ionomycin induce only the expression of c-fos gene. This induction is abolished when A5 cells are loaded with 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid before treatment with the ionophores, or when serum is excluded from the incubation medium. Exclusion of serum from the medium does not change the effects of isoproterenol or PMA on c-fos, c-jun, or jun B. These results strongly suggest that serum factors act synergistically with Ca2+ to induce c-fos expression in A5 cells. The studies presented here indicate that different signal transduction pathways operate in A5 cells for the induction of c-fos, c-jun, and jun B genes.

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