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Journal articles on the topic 'Mouse carcinoma cells'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 February 2022

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1

Li, Rongshan, Jorge L. Yao, Patricia A. Bourne, P. Anthony di Sant'Agnese, and Jiaoti Huang. "Frequent Expression of Human Carcinoma-Associated Antigen, a Mucin-Type Glycoprotein, in Cells of Prostatic Carcinoma." Archives of Pathology & Laboratory Medicine 128, no. 12 (December 1, 2004): 1412–17. http://dx.doi.org/10.5858/2004-128-1412-feohca.

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Abstract Context.—Human carcinoma-associated antigen (HCA) is a mucin glycoprotein recognized by antibodies raised against epiglycanin, the latter having been originally purified from mouse mammary carcinoma cells. Human carcinoma-associated antigen expression is increased in sera of patients with various carcinomas, including prostatic carcinoma. However, to our knowledge, expression of HCA in benign and neoplastic prostatic tissue has not been studied. Objective.—To compare the expression of HCA in cells of primary and metastatic prostatic carcinomas with its expression in non–carcinoma-associated cells. Design.—We studied 40 cases of primary and 36 cases of metastatic prostatic carcinomas by immunohistochemical staining with anti-HCA monoclonal antibodies G1 and HAE3. The blocks from primary carcinomas also contained normal prostatic tissue (40 cases), benign prostatic hyperplasia (16 cases), and high-grade prostatic intraepithelial neoplasia (32 cases). Results.—The 2 antibodies stained carcinomas more frequently than normal prostatic tissue, hyperplasia, and prostatic intraepithelial neoplasia (P < .001). The differences in the staining of low-grade versus high-grade tumors was not statistically significant with either antibody. The staining was present in the cytoplasm and on the luminal membrane surface of the tumor cells and in the luminal secretions. In metastatic prostatic carcinomas, G1 and HAE3 staining was positive in 44% and 67% of the cases, respectively. Conclusions.—Our results showed that mucin protein HCA is overexpressed in cells of prostatic carcinoma, which may have value in diagnosis and therapy. Its role in carcinogenesis also merits further study.

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2

Sleigh, Merilyn J. "Differentiation and proliferation in mouse embryonal carcinoma cells." BioEssays 14, no. 11 (November 1992): 769–75. http://dx.doi.org/10.1002/bies.950141109.

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3

Paterno, G. D., C. N. Adra, and M. W. McBurney. "X chromosome reactivation in mouse embryonal carcinoma cells." Molecular and Cellular Biology 5, no. 10 (October 1985): 2705–12. http://dx.doi.org/10.1128/mcb.5.10.2705.

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The embryonal carcinoma cell line, C86S1, carries two X chromosomes, one of which replicates late during S phase of the cell cycle and appears to be genetically inactive. C86S1A1 is a mutant which lacks activity of the X-encoded enzyme, hypoxanthine phosphoribosyltransferase (HPRT). Treatment of C86S1A1 cells with DNA-demethylating agents, such as 5-azacytidine (5AC), resulted in (i) the transient expression in almost all cells of elevated levels of HPRT and three other enzymes encoded by X-linked genes and (ii) the stable expression of HPRT in up to 5 to 20% of surviving cells. Most cells which stably expressed HPRT had two X chromosomes which replicated in early S phase. C86S1A1 cells which had lost the inactive X chromosome did not respond to 5AC. These results suggest that DNA demethylation results in the reactivation of genes on the inactive X chromosome and perhaps in the reactivation of the entire X chromosome. No such reactivation occurred in C86S1A1 cells when the cells were differentiated before exposure to 5AC. Thus, the process of X chromosome inactivation may be a sequential one involving, as a first step, methylation of certain DNA sequences and, as a second step, some other mechanism(s) of transcriptional repression.

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4

Paterno, G. D., C. N. Adra, and M. W. McBurney. "X chromosome reactivation in mouse embryonal carcinoma cells." Molecular and Cellular Biology 5, no. 10 (October 1985): 2705–12. http://dx.doi.org/10.1128/mcb.5.10.2705-2712.1985.

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The embryonal carcinoma cell line, C86S1, carries two X chromosomes, one of which replicates late during S phase of the cell cycle and appears to be genetically inactive. C86S1A1 is a mutant which lacks activity of the X-encoded enzyme, hypoxanthine phosphoribosyltransferase (HPRT). Treatment of C86S1A1 cells with DNA-demethylating agents, such as 5-azacytidine (5AC), resulted in (i) the transient expression in almost all cells of elevated levels of HPRT and three other enzymes encoded by X-linked genes and (ii) the stable expression of HPRT in up to 5 to 20% of surviving cells. Most cells which stably expressed HPRT had two X chromosomes which replicated in early S phase. C86S1A1 cells which had lost the inactive X chromosome did not respond to 5AC. These results suggest that DNA demethylation results in the reactivation of genes on the inactive X chromosome and perhaps in the reactivation of the entire X chromosome. No such reactivation occurred in C86S1A1 cells when the cells were differentiated before exposure to 5AC. Thus, the process of X chromosome inactivation may be a sequential one involving, as a first step, methylation of certain DNA sequences and, as a second step, some other mechanism(s) of transcriptional repression.

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5

LUO, Huaxing, Yingxue HAO, Bo TANG, Dongzhu ZENG, Yan SHI, and Peiwu YU. "Mouse forestomach carcinoma cells immunosuppress macrophages through TGF-?1." Turkish Journal of Gastroenterology 23, no. 6 (December 1, 2012): 658–65. http://dx.doi.org/10.4318/tjg.2012.0563.

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6

Batth, Balvinder K., Rachana Tripathi, and Usha K. Srinivas. "Curcumin-induced differentiation of mouse embryonal carcinoma PCC4 cells." Differentiation 68, no. 2-3 (October 2001): 133–40. http://dx.doi.org/10.1046/j.1432-0436.2001.680207.x.

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7

Pierce, G. Barry, Juan Arechaga, Alan Jones, Andrea Lewellyn, and Robert S. Wells. "The fate of embryonal-carcinoma cells in mouse blastocysts." Differentiation 33, no. 3 (February 1987): 247–53. http://dx.doi.org/10.1111/j.1432-0436.1987.tb01564.x.

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8

Lockett, Trevor J., and Merilyn J. Sleigh. "Oncogene expression in differentiating F9 mouse embryonal carcinoma cells." Experimental Cell Research 173, no. 2 (December 1987): 370–78. http://dx.doi.org/10.1016/0014-4827(87)90277-1.

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9

Simonneau, Michel, Bernard Eddé, Jean-François Nicolas, and Hedwig Jakob. "Single channel currents in mouse embryonal multipotential carcinoma cells." Cell Differentiation 17, no. 1 (July 1985): 21–28. http://dx.doi.org/10.1016/0045-6039(85)90534-2.

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10

Hassan, Bardes B., Lucas A. Altstadt, Wessel P. Dirksen, Said M. Elshafae, and Thomas J. Rosol. "Canine Thyroid Cancer: Molecular Characterization and Cell Line Growth in Nude Mice." Veterinary Pathology 57, no. 2 (February 21, 2020): 227–40. http://dx.doi.org/10.1177/0300985819901120.

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Thyroid cancer is the most common endocrine malignancy in dogs. Dogs and humans are similar in the spontaneous development of thyroid cancer and metastasis to lungs; however, thyroid cancer has a higher incidence of metastasis in dogs. This study developed a preclinical nude mouse model of canine thyroid cancer using a canine thyroid adenocarcinoma cell line (CTAC) and measured the expression of important invasion and metastasis genes in spontaneous canine thyroid carcinomas and CTAC cells. CTAC cells were examined by electron microscopy. Short tandem repeat analysis was performed for both the original neoplasm and CTAC cells. CTAC cells were transduced with luciferase and injected subcutaneously and into the tail vein. Tumors and metastases were monitored using bioluminescent imaging and confirmed with gross necropsy and histopathology. Invasion and metastasis genes were characterized in 8 follicular thyroid carcinomas (FTCs), 4 C-cell thyroid carcinomas, 3 normal thyroids, and CTAC cells. CTAC cells grew well as xenografts in the subcutis, and they resembled the primary neoplasm. Metastasis to the kidney and lung occurred infrequently following subcutaneous and tail vein injection of CTAC cells. STR analysis confirmed that CTAC cells were derived from the original neoplasm and were of canine origin. Finally, 24 genes were differentially expressed in spontaneous canine thyroid carcinomas, CTAC, and normal thyroids. This study demonstrated the usefulness of a nude mouse model of experimental canine thyroid carcinoma and identified potential molecular targets of canine follicular and C-cell thyroid carcinoma.

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11

Lacotte, S., F. Slits, O. A. Lorenzo, M. Jeremy, O. Graziano, D. Vaihere, G. G. Carmen, M. Philippe, and T. Christian. "Kupffer cells as antigen-presenting cells in mouse livers with hepatocellular carcinoma." Journal of Hepatology 66, no. 1 (2017): S633—S634. http://dx.doi.org/10.1016/s0168-8278(17)31717-8.

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12

Suzuki, Toru, Hyo-Soo Kim, Masahiko Kurabayashi, Hiroshi Hamada, Hideta Fujii, Masanori Aikawa, Masafumi Watanabe, et al. "Preferential Differentiation of P19 Mouse Embryonal Carcinoma Cells Into Smooth Muscle Cells." Circulation Research 78, no. 3 (March 1996): 395–404. http://dx.doi.org/10.1161/01.res.78.3.395.

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13

Martin, S. L. "Ribonucleoprotein particles with LINE-1 RNA in mouse embryonal carcinoma cells." Molecular and Cellular Biology 11, no. 9 (September 1991): 4804–7. http://dx.doi.org/10.1128/mcb.11.9.4804.

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The LINE-1 repeat family is interspersed throughout mammalian genomes and is thought to be the result of duplicative transposition of LINE-1 sequences via an RNA intermediate. This report describes a ribonucleoprotein particle with LINE-1 RNA in the mouse embryonal carcinoma cell line F9. This ribonucleoprotein particle is a potential intermediate in the transposition of LINE-1 in the mouse genome.

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14

Martin, S. L. "Ribonucleoprotein particles with LINE-1 RNA in mouse embryonal carcinoma cells." Molecular and Cellular Biology 11, no. 9 (September 1991): 4804–7. http://dx.doi.org/10.1128/mcb.11.9.4804-4807.1991.

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The LINE-1 repeat family is interspersed throughout mammalian genomes and is thought to be the result of duplicative transposition of LINE-1 sequences via an RNA intermediate. This report describes a ribonucleoprotein particle with LINE-1 RNA in the mouse embryonal carcinoma cell line F9. This ribonucleoprotein particle is a potential intermediate in the transposition of LINE-1 in the mouse genome.

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15

Burkuš, J., A. Navarrete Santos, M. Schindler, J. Babeľová, J. S. Jung, A. Špirková, M. Kšiňanová, et al. "Adiponectin stimulates glucose uptake in mouse blastocysts and embryonic carcinoma cells." Reproduction 159, no. 3 (March 2020): 227–39. http://dx.doi.org/10.1530/rep-19-0251.

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Preimplantation embryos are sensitive to maternal hormones affecting embryonic signal transduction and metabolic functions. We examined whether adiponectin, the most abundantly secreted adipokine, can influence glucose transport in mouse embryonic cells. In mouse blastocysts full-length adiponectin stimulated glucose uptake, while no effect of globular adiponectin was found. Full-length adiponectin stimulated translocation of GLUT8 glucose transporter to the cell membrane; we did not detect significant changes in the intracellular localization of GLUT4 glucose transporter in adiponectin-treated blastocysts. To study adiponectin signaling in detail, we used embryoid bodies formed from mouse embryonic carcinoma cell (ECC) line P19. We confirmed the expression of adiponectin receptors in these cells. Similar to mouse blastocysts, full-length adiponectin, but not globular adiponectin, stimulated glucose uptake in ECC P19 embryoid bodies. Moreover, full-length adiponectin stimulated AMPK and p38 MAPK phosphorylation. These results indicate that besides AMPK, p38 MAPK is a potential target of adiponectin in mouse embryonic cells. AMPK inhibitor did not influence the adiponectin-stimulated p38 MAPK phosphorylation, indicating independent action of these two signaling pathways. In mouse embryos adiponectin acts as a hormonal regulator of glucose uptake, which becomes especially important in phases with reduced levels of circulating insulin. Our results suggest that adiponectin maintains the glucose supply for early embryos under hypoinsulinaemic conditions, for example, in mothers suffering from type 1 diabetes mellitus.

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16

Kong, Liangsheng, Jingyuan Li, Yongli Liu, Zhiwei Sun, Shixia Zhou, Junling Tang, Ting Ye, Jianyu Wang, and H. Rosie Xing. "Neuralized1a regulates asymmetric division in mouse Lewis lung carcinoma cells." Life Sciences 206 (August 2018): 70–76. http://dx.doi.org/10.1016/j.lfs.2018.05.033.

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17

Kim, Youngsoo, and Susan M. Fischer. "Transcriptional Regulation of Cyclooxygenase-2 in Mouse Skin Carcinoma Cells." Journal of Biological Chemistry 273, no. 42 (October 16, 1998): 27686–94. http://dx.doi.org/10.1074/jbc.273.42.27686.

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18

Liu, Lei, Xian-hua Chen, Jia Huang, Jun-ji Lin, Wan-min Lin, and Ping Xu. "NSSR1 promotes neuronal differentiation of mouse embryonic carcinoma P19 cells." NeuroReport 15, no. 5 (April 2004): 823–28. http://dx.doi.org/10.1097/00001756-200404090-00017.

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19

Sørensen, Belinda Halling, Line Jee Hartmann Rasmussen, Bjørn Sindballe Broberg, Thomas Kjær Klausen, Daniel Peter Rafael Sauter, Ian Henry Lambert, Anders Aspberg, and Else Kay Hoffmann. "Integrin β1, Osmosensing, and Chemoresistance in Mouse Ehrlich Carcinoma Cells." Cellular Physiology and Biochemistry 36, no. 1 (2015): 111–32. http://dx.doi.org/10.1159/000374057.

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Background/Aims: Altered expression of the integrin family of cell adhesion receptors has been associated with initiation, progression, and metastasis of solid tumors as well as in the development of chemoresistance. Here, we investigated the role of integrins, in particular integrin β1, in cell volume regulation and drug-induced apoptosis in adherent and non-adherent Ehrlich ascites cell lines. Methods: Adhesion phenotypes were verified by colorimetric cell-adhesion-assay. Quantitative real-time PCR and western blot were used to compare expression levels of integrin subunits. Small interfering RNA was used to silence integrin β1 expression. Regulatory volume decrease (RVD) after cell swelling was studied with calcein-fluorescence-self-quenching and Coulter counter analysis. Taurine efflux was estimated with tracer technique. Caspase assay was used to determine apoptosis. Results: We show that adherent cells have stronger fibronectin binding and a significantly increased expression of integrin α5, αv, and β1 at mRNA and protein level, compared to non-adherent cells. Knockdown of integrin β1 reduced RVD of the adherent but not of the non-adherent cells. Efflux of taurine was unaffected. In contrast to non-adherent, adherent cells exhibited chemoresistance to chemotherapeutic drugs (cisplatin and gemcitabine). However, knockdown of integrin β1 promoted cisplatin-induced caspase activity in adherent cells. Conclusion: Our data identifies integrin β1 as a part of the osmosensing machinery and regulator of cisplatin resistance in adherent Ehrlich cells.

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20

Rhee, Juong G., Hubert A. Eddy, George H. Harrison, and Omar M. Salazar. "Heat-Sensitive State of Mouse Mammary Carcinoma Cells in Tumors." Radiation Research 123, no. 2 (August 1990): 165. http://dx.doi.org/10.2307/3577540.

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21

Bloemers, S. M., R. Leurs, M. J. Smit, S. Verheule, L. G. J. Tertoolen, H. Timmerman, and S. W. Delaat. "Mouse P19 Embryonal Carcinoma Cells Express Functional Histamine H1-Receptors." Biochemical and Biophysical Research Communications 191, no. 1 (February 1993): 118–25. http://dx.doi.org/10.1006/bbrc.1993.1192.

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22

Hidaka, K., T. Morisaki, S. H. Byun, K. Hashido, K. Toyama, and T. Mukai. "The MEF2B Homolog Differentially Expressed in Mouse Embryonal Carcinoma Cells." Biochemical and Biophysical Research Communications 213, no. 2 (August 1995): 555–60. http://dx.doi.org/10.1006/bbrc.1995.2167.

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23

Astigiano, Simonetta, Patrizia Damonte, Sara Fossati, Luca Boni, and Ottavia Barbieri. "Fate of embryonal carcinoma cells injected into postimplantation mouse embryos." Differentiation 73, no. 9-10 (December 2005): 484–90. http://dx.doi.org/10.1111/j.1432-0436.2005.00043.x.

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24

Jung-Testas, Ingrid, and Etienne-Emile Baulieu. "Testosterone-induced responsiveness to androgen in Shionogi mouse carcinoma cells." Experimental Cell Research 170, no. 1 (May 1987): 250–58. http://dx.doi.org/10.1016/0014-4827(87)90134-0.

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25

Jung-Testas, I., and E. E. Baulieu. "Hormone and anti-hormone action in mouse mammary carcinoma cells." Journal of Steroid Biochemistry 25 (January 1986): 134. http://dx.doi.org/10.1016/0022-4731(86)90814-9.

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26

Bellone, Matteo, Monica Ceccon, Matteo Grioni, Elena Jachetti, Arianna Calcinotto, Anna Napolitano, Massimo Freschi, Giulia Casorati, and Paolo Dellabona. "iNKT Cells Control Mouse Spontaneous Carcinoma Independently of Tumor-Specific Cytotoxic T Cells." PLoS ONE 5, no. 1 (January 13, 2010): e8646. http://dx.doi.org/10.1371/journal.pone.0008646.

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27

Martin, S. L., and D. Branciforte. "Synchronous expression of LINE-1 RNA and protein in mouse embryonal carcinoma cells." Molecular and Cellular Biology 13, no. 9 (September 1993): 5383–92. http://dx.doi.org/10.1128/mcb.13.9.5383.

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L1, or LINE-1, is a repetitive DNA family found in all mammalian genomes that have been examined. At least a few individual members of the L1 family are functional transposable elements. Expression of these active elements leads to new insertions of L1 into the genomic DNA by the process of retrotransposition. We have detected coexpression of full-length, sense-strand L1 RNA transcripts and L1-encoded protein in mouse embryonal carcinoma cell lines. Both of these L1 expression products are candidates for intermediates in the retrotransposition process. L1 protein is found in what appear to be cytoplasmic aggregates and is not localized to any known cytoplasmic organelles. The six embryonal carcinoma cell lines tested were chosen to represent commitment to different developmental pathways in early mouse embryogenesis. The only two cell lines that express L1 are unique among the six in that they have a strong predilection to differentiate into extraembryonic endoderm. This observation is consistent with L1 expression and transposition in primordial germ cells of the mouse. An important implication of these studies is that L1 expression may provide a new marker for use in determining the origin of primordial germ cells during mouse embryogenesis.

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28

Martin, S. L., and D. Branciforte. "Synchronous expression of LINE-1 RNA and protein in mouse embryonal carcinoma cells." Molecular and Cellular Biology 13, no. 9 (September 1993): 5383–92. http://dx.doi.org/10.1128/mcb.13.9.5383-5392.1993.

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L1, or LINE-1, is a repetitive DNA family found in all mammalian genomes that have been examined. At least a few individual members of the L1 family are functional transposable elements. Expression of these active elements leads to new insertions of L1 into the genomic DNA by the process of retrotransposition. We have detected coexpression of full-length, sense-strand L1 RNA transcripts and L1-encoded protein in mouse embryonal carcinoma cell lines. Both of these L1 expression products are candidates for intermediates in the retrotransposition process. L1 protein is found in what appear to be cytoplasmic aggregates and is not localized to any known cytoplasmic organelles. The six embryonal carcinoma cell lines tested were chosen to represent commitment to different developmental pathways in early mouse embryogenesis. The only two cell lines that express L1 are unique among the six in that they have a strong predilection to differentiate into extraembryonic endoderm. This observation is consistent with L1 expression and transposition in primordial germ cells of the mouse. An important implication of these studies is that L1 expression may provide a new marker for use in determining the origin of primordial germ cells during mouse embryogenesis.

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29

Bhat, K., M. W. McBurney, and H. Hamada. "Functional cloning of mouse chromosomal loci specifically active in embryonal carcinoma stem cells." Molecular and Cellular Biology 8, no. 8 (August 1988): 3251–59. http://dx.doi.org/10.1128/mcb.8.8.3251.

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Chromosomal loci that are specifically active in embryonal carcinoma stem cells were cloned from the mouse genome by functional selection. P19 cells, a pluripotent embryonal carcinoma cell line, were transfected with an enhancer trap (a plasmid containing an enhancerless inactive neo gene), and NEO+ transformants were isolated. All of the NEO+ cell lines retained pluripotency and expressed the neo gene. When the cells were induced to differentiate, most of the cell lines continued to express the neo gene, while the neo gene in some cell lines became repressed. From the latter group of cell lines, we have cloned the integrated neo gene plus the flanking cellular DNA sequences. Three of the six cloned DNAs possessed a high NEO+-transforming activity in undifferentiated P19 cells. Among these three, two (015 and 052) were inactive in differentiated P19 cells and NIH 3T3 cells, while the remaining one was active in these differentiated cells. Deletion analysis suggested that both 015 and 052 contain two regulatory elements (promoter and enhancer) of cellular DNA origin. The putative enhancer and promoter are separated by at least 6 kilobases in 015 and 1 kilobase in 052. Therefore, 015 and 052 cloned fragments contain regulatory DNA elements that are specifically active in the embryonal carcinoma stem cells.

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30

Bhat, K., M. W. McBurney, and H. Hamada. "Functional cloning of mouse chromosomal loci specifically active in embryonal carcinoma stem cells." Molecular and Cellular Biology 8, no. 8 (August 1988): 3251–59. http://dx.doi.org/10.1128/mcb.8.8.3251-3259.1988.

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Chromosomal loci that are specifically active in embryonal carcinoma stem cells were cloned from the mouse genome by functional selection. P19 cells, a pluripotent embryonal carcinoma cell line, were transfected with an enhancer trap (a plasmid containing an enhancerless inactive neo gene), and NEO+ transformants were isolated. All of the NEO+ cell lines retained pluripotency and expressed the neo gene. When the cells were induced to differentiate, most of the cell lines continued to express the neo gene, while the neo gene in some cell lines became repressed. From the latter group of cell lines, we have cloned the integrated neo gene plus the flanking cellular DNA sequences. Three of the six cloned DNAs possessed a high NEO+-transforming activity in undifferentiated P19 cells. Among these three, two (015 and 052) were inactive in differentiated P19 cells and NIH 3T3 cells, while the remaining one was active in these differentiated cells. Deletion analysis suggested that both 015 and 052 contain two regulatory elements (promoter and enhancer) of cellular DNA origin. The putative enhancer and promoter are separated by at least 6 kilobases in 015 and 1 kilobase in 052. Therefore, 015 and 052 cloned fragments contain regulatory DNA elements that are specifically active in the embryonal carcinoma stem cells.

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31

Andrews, P. W., M. M. Matin, A. R. Bahrami, I. Damjanov, P. Gokhale, and J. S. Draper. "Embryonic stem (ES) cells and embryonal carcinoma (EC) cells: opposite sides of the same coin." Biochemical Society Transactions 33, no. 6 (October 26, 2005): 1526–30. http://dx.doi.org/10.1042/bst0331526.

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Embryonal carcinoma (EC) cells are the stem cells of teratocarcinomas, and the malignant counterparts of embryonic stem (ES) cells derived from the inner cell mass of blastocyst-stage embryos, whether human or mouse. On prolonged culture in vitro, human ES cells acquire karyotypic changes that are also seen in human EC cells. They also ‘adapt’, proliferating faster and becoming easier to maintain with time in culture. Furthermore, when cells from such an ‘adapted’ culture were inoculated into a SCID (severe combined immunodeficient) mouse, we obtained a teratocarcinoma containing histologically recognizable stem cells, which grew out when the tumour was explanted into culture and exhibited properties of the starting ES cells. In these features, the ‘adapted’ ES cells resembled malignant EC cells. The results suggest that ES cells may develop in culture in ways that mimic changes occurring in EC cells during tumour progression.

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32

Wang, Liangsu, and Gilbert A. Schultz. "Expression of Oct-4 during differentiation of murine F9 cells." Biochemistry and Cell Biology 74, no. 4 (July 1, 1996): 579–84. http://dx.doi.org/10.1139/o96-062.

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Oct-4 is a transcription factor that shares a common structural motif with members of the POU family. The mRNA for Oct-4 is found in growing oocytes and in totipotent or pluripotent cells of the early mouse embryo. Oct-4 is down-regulated in embryos during differentiation events associated with blastocyst implantation and gastrulation. Oct-4 gene expression is also down-regulated when murine embryonic stem cells or embryonal carcinoma cells are induced to differentiate in the presence of retinoic acid. A polyclonal antibody that can recognize a unique peptide sequence in the C-terminus of mouse Oct-4 has been prepared. It specifically recognizes Oct-4 protein as tested by Western blots and gel mobility shift assays. This antibody has been used to measure Oct-4 protein levels during retinoic acid induced differentiation of F9 embryonal carcinoma cells. It was observed that Oct-4 protein was abundant in undifferentiated F9 cells but decreased to levels below detection as the cells differentiated, consistent with changes in levels of expression in early embryos.Key words: octamer, DNA-binding protein, transcription factor, embryonal carcinoma cells.

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33

LUO, HUAXING, YINGXUE HAO, BO TANG, DONGZHU ZENG, YAN SHI, and PEIWU YU. "Mouse forestomach carcinoma cells immunosuppress macrophages through transforming growth factor-β1." Molecular Medicine Reports 5, no. 4 (February 3, 2012): 988–92. http://dx.doi.org/10.3892/mmr.2012.777.

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34

Johnson, Sandra A. S., and Ronald S. Pardini. "Antioxidant Enzyme Response to Hypericin in EMT6 Mouse Mammary Carcinoma Cells." Free Radical Biology and Medicine 24, no. 5 (March 1998): 817–26. http://dx.doi.org/10.1016/s0891-5849(97)00364-x.

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35

Astakhova, T. M., and N. P. Sharova. "Exclusion of immune proteasomes from mouse ascitic carcinoma Krebs-II cells." Biology Bulletin 33, no. 3 (May 2006): 216–23. http://dx.doi.org/10.1134/s1062359006030022.

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36

Nishigaki, Fusako, Shozo Sakuma, Toshikazu Ogawa, Susumu Miyata, Toshitaka Ohkubo, and Toshio Goto. "FK506 induces chondrogenic differentiation of clonal mouse embryonic carcinoma cells, ATDC5." European Journal of Pharmacology 437, no. 3 (February 2002): 123–28. http://dx.doi.org/10.1016/s0014-2999(02)01269-4.

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37

Groot, Rolf P. de, Jon Schoorlemmer, Siebe T. van Ganesen, and Wiebe Kruijer. "Differential expression ofjunandfosgenes during differentiation of mouse P19 embryonal carcinoma cells." Nucleic Acids Research 18, no. 11 (1990): 3195–202. http://dx.doi.org/10.1093/nar/18.11.3195.

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38

Cremisi, C., and C. Babinet. "Negative regulation of early polyomavirus expression in mouse embryonal carcinoma cells." Journal of Virology 59, no. 3 (1986): 761–63. http://dx.doi.org/10.1128/jvi.59.3.761-763.1986.

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39

Ugorski, Maciej, Peter Påhlsson, Danuta Dus, and Bo Nilsson. "Glycosphingolipids in lectin-resistant variants of mouse lewis lung carcinoma cells." International Journal of Cancer 43, no. 1 (January 15, 1989): 93–101. http://dx.doi.org/10.1002/ijc.2910430119.

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40

Colburn, N. H., N. Raab-Traub, D. Becker, Y. Cao, and D. Winterstein. "Transforming activity of nasopharyngeal carcinoma DNA detectable in mouse JB6 cells." International Journal of Cancer 44, no. 6 (December 15, 1989): 1012–16. http://dx.doi.org/10.1002/ijc.2910440613.

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41

Wen, Jianyan, Qing Xia, Cailing Lu, Lina Yin, Juan Hu, Yanhua Gong, Bin Yin, et al. "Proteomic analysis of cardiomyocytes differentiation in mouse embryonic carcinoma P19CL6 cells." Journal of Cellular Biochemistry 102, no. 1 (2007): 149–60. http://dx.doi.org/10.1002/jcb.21285.

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Loh, T. P., L. L. Sievert, and R. W. Scott. "Proviral sequences that restrict retroviral expression in mouse embryonal carcinoma cells." Molecular and Cellular Biology 7, no. 10 (October 1987): 3775–84. http://dx.doi.org/10.1128/mcb.7.10.3775.

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Embryonal carcinoma (EC) cells are nonpermissive for retrovirus replication. Restriction of retroviral expression in EC cells was studied by using DNA transfection techniques. To investigate the activity of the Moloney murine leukemia virus (M-MuLV)enhancer and promoter sequences, the M-MuLV long terminal repeat and the defined long terminal repeat deletions were linked to neo structural gene sequences that encode resistance to the neomycin analog G418. Transient expression data and drug resistance frequencies support the findings that the M-MuLV enhancer is not active in EC cells but that promoter sequences are functional. In addition, a proviral DNA fragment that encodes the leader RNA sequence of a M-MuLV recombinant retrovirus was found to restrict expression specifically in EC cells. Deletion analysis of the leader fragment localized the inhibitory sequences to a region that spans the M-MuLV tRNA primer binding site. It is not known whether restriction occurs at a transcriptional or posttranscriptional level, but steady-state RNA levels in transient expression assays were significantly reduced.

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43

Francavilla, A., A. Di Leo, M. Barone, M. P. Scavo, and B. Pesetti. "Stem cells and hepatocellular carcinoma in an HBV-transgenic mouse model." Digestive and Liver Disease 39, no. 3 (March 2007): A1. http://dx.doi.org/10.1016/j.dld.2006.12.021.

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Hawley, Teresa S., Luc A. Sabourin, and Robert G. Hawley. "Comparative analysis of retroviral vector expression in mouse embryonal carcinoma cells." Plasmid 22, no. 2 (September 1989): 120–31. http://dx.doi.org/10.1016/0147-619x(89)90021-8.

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45

Loh, T. P., L. L. Sievert, and R. W. Scott. "Proviral sequences that restrict retroviral expression in mouse embryonal carcinoma cells." Molecular and Cellular Biology 7, no. 10 (October 1987): 3775–84. http://dx.doi.org/10.1128/mcb.7.10.3775-3784.1987.

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Abstract:

Embryonal carcinoma (EC) cells are nonpermissive for retrovirus replication. Restriction of retroviral expression in EC cells was studied by using DNA transfection techniques. To investigate the activity of the Moloney murine leukemia virus (M-MuLV)enhancer and promoter sequences, the M-MuLV long terminal repeat and the defined long terminal repeat deletions were linked to neo structural gene sequences that encode resistance to the neomycin analog G418. Transient expression data and drug resistance frequencies support the findings that the M-MuLV enhancer is not active in EC cells but that promoter sequences are functional. In addition, a proviral DNA fragment that encodes the leader RNA sequence of a M-MuLV recombinant retrovirus was found to restrict expression specifically in EC cells. Deletion analysis of the leader fragment localized the inhibitory sequences to a region that spans the M-MuLV tRNA primer binding site. It is not known whether restriction occurs at a transcriptional or posttranscriptional level, but steady-state RNA levels in transient expression assays were significantly reduced.

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46

Montero-Montero, Lucía, Jaime Renart, Andrés Ramírez, Carmen Ramos, Mariam Shamhood, Rocío Jarcovsky, Miguel Quintanilla, and Ester Martín-Villar. "Interplay between Podoplanin, CD44s and CD44v in Squamous Carcinoma Cells." Cells 9, no. 10 (September 29, 2020): 2200. http://dx.doi.org/10.3390/cells9102200.

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Podoplanin and CD44 are transmembrane glycoproteins involved in inflammation and cancer. In this paper, we report that podoplanin is coordinately expressed with the CD44 standard (CD44s) and variant (CD44v) isoforms in vivo—in hyperplastic skin after a pro-inflammatory stimulus with 12-O-tetradecanoylphorbol-13-acetate (TPA)—and in vitro—in cell lines representative of different stages of mouse-skin chemical carcinogenesis, as well as in human squamous carcinoma cell (SCC) lines. Moreover, we identify CD44v10 in the mouse-skin carcinogenesis model as the only CD44 variant isoform expressed in highly aggressive spindle carcinoma cell lines together with CD44s and podoplanin. We also characterized CD44v3-10, CD44v6-10 and CD44v8-10 as the major variant isoforms co-expressed with CD44s and podoplanin in human SCC cell lines. Immunofluorescence confocal microscopy experiments show that these CD44v isoforms colocalize with podoplanin at plasma membrane protrusions and cell–cell contacts of SCC cells, as previously reported for CD44s. Furthermore, CD44v isoforms colocalize with podoplanin in chemically induced mouse-skin SCCs in vivo. Co-immunoprecipitation experiments indicate that podoplanin physically binds to CD44v3-10, CD44v6-10 and CD44v8-10 isoforms, as well as to CD44s. Podoplanin–CD44 interaction is mediated by the transmembrane and cytosolic regions and is negatively modulated by glycosylation of the extracellular domain. These results point to a functional interplay of podoplanin with both CD44v and CD44s isoforms in SCCs and give insight into the regulation of the podoplanin–CD44 association.

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Petersen, O. W., and B. van Deurs. "Characterization of epithelial membrane antigen expression in human mammary epithelium by ultrastructural immunoperoxidase cytochemistry." Journal of Histochemistry & Cytochemistry 34, no. 6 (June 1986): 801–9. http://dx.doi.org/10.1177/34.6.3009605.

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Ultrastructural immunocytochemistry was used to analyze cell surface distribution and intracellular localization of milk fat globule membrane antigen (MFGM-A) in cryosections from human breast carcinomas and benign breast biopsy specimens. The specimens were fixed in formaldehyde and frozen. Cryostat sections were cut at 15 micron, incubated with mouse monoclonal antibody to MFGM-A, and then with a peroxidase-conjugated goat anti-mouse antibody. After glutaraldehyde fixation, the sections were incubated with diaminobenzidine-H2O2 and further processed for electron microscopy. MFGM-A was specific for epithelial cells. MFGM-A staining was strictly confined to the apical surface membrane of normal ductal epithelium, never involving basolateral membranes below the tight junctions. In normal epithelial cells, MFGM-A was readily detected in cisternae of the endoplasmic reticulum (ER), but only to a lesser extent in Golgi complexes and presumptive secretory vesicles. In carcinoma cells, surface staining for MFGM-A was either distributed in a non-polarized manner on the entire cell surface or else was totally absent. In some carcinoma cells without surface-associated MFGM-A, very pronounced intracellular MFGM-A staining was seen in the ER, in the nuclear envelope, and in annulate lamellae. The observations on MFGM-A expression were supported by studies on a cell culture model system.

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Mattes, M. J., K. Look, J. L. Lewis, L. J. Old, and K. O. Lloyd. "Three mouse monoclonal antibodies to human differentiation antigens: reactivity with two mucin-like antigens and with connective tissue fibers." Journal of Histochemistry & Cytochemistry 33, no. 11 (November 1985): 1095–102. http://dx.doi.org/10.1177/33.11.3932516.

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Three human differentiation antigens (MU78, MT334, and MQ49) have been defined by mouse monoclonal antibodies developed from mice immunized with ovarian carcinoma cell lines. Their distribution was determined on 148 cultured cell lines of various histologic types and on frozen sections of 16 normal tissues. MU78 was found in fibrillar structures in soft connective tissue with a distribution resembling that of elastin fibers; however, elastin fibers in elastic cartilage and in the aorta were nonreactive. MU78 was detected in cultured carcinoma cells of various histologic types, where it had a nonfibrillar, cytoplasmic distribution, but was not detected in normal epithelial cells in frozen sections. Cultured fibroblasts, astrocytomas, melanomas, and lymphomas did not contain MU78. In cell lines, MU78 appears to be a protein of 2000-5000 daltons. The other two antigens, MT334 and MQ49, are both mucin-like molecules, and the determinants are probably carbohydrate in nature. Of the normal tissues examined, MT334 was detected only in goblet cells of the colon, though it was present in a variety of carcinomas in culture. It was detected as both a cytoplasmic and secreted component. MQ49 was detected in various secretory epithelial cells, in Hassall's corpuscles in the thymus, and in cultured carcinomas of various histologic types. It was found on the cell surface as well as in the cytoplasm and is present on a glycolipid as well as on a sulfated mucin. These results, and results of other recent studies, demonstrate the importance of mucin-like molecules as antigens in epithelial cells and secretions.

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Murphy, S. P., J. J. Gorzowski, K. D. Sarge, and B. Phillips. "Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells." Molecular and Cellular Biology 14, no. 8 (August 1994): 5309–17. http://dx.doi.org/10.1128/mcb.14.8.5309.

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Two distinct murine heat shock transcription factors, HSF1 and HSF2, have been identified. HSF1 mediates the transcriptional activation of heat shock genes in response to environmental stress, while the function of HSF2 is not understood. Both factors can bind to heat shock elements (HSEs) but are maintained in a non-DNA-binding state under normal growth conditions. Mouse embryonal carcinoma (EC) cells are the only mammalian cells known to exhibit HSE-binding activity, as determined by gel shift assays, even when maintained at normal physiological temperatures. We demonstrate here that the constitutive HSE-binding activity present in F9 and PCC4.aza.R1 EC cells, as well as a similar activity found to be present in mouse embryonic stem cells, is composed predominantly of HSF2. HSF2 in F9 EC cells is trimerized and is present at higher levels than in a variety of nonembryonal cell lines, suggesting a correlation of these properties with constitutive HSE-binding activity. Surprisingly, transcription run-on assays suggest that HSF2 in unstressed EC cells does not stimulate transcription of two putative target genes, hsp70 and hsp86. Genomic footprinting analysis indicates that HSF2 is not bound in vivo to the HSE of the hsp70 promoter in unstressed F9 EC cells, although HSF2 is present in the nucleus and the promoter is accessible to other transcription factors and to HSF1 following heat shock. Thus trimerization and nuclear localization of HSF2 do not appear to be sufficient for in vivo binding of HSF2 to the HSE of the hsp70 promoter in unstressed F9 EC cells.

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50

Murphy, S. P., J. J. Gorzowski, K. D. Sarge, and B. Phillips. "Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells." Molecular and Cellular Biology 14, no. 8 (August 1994): 5309–17. http://dx.doi.org/10.1128/mcb.14.8.5309-5317.1994.

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Abstract:

Two distinct murine heat shock transcription factors, HSF1 and HSF2, have been identified. HSF1 mediates the transcriptional activation of heat shock genes in response to environmental stress, while the function of HSF2 is not understood. Both factors can bind to heat shock elements (HSEs) but are maintained in a non-DNA-binding state under normal growth conditions. Mouse embryonal carcinoma (EC) cells are the only mammalian cells known to exhibit HSE-binding activity, as determined by gel shift assays, even when maintained at normal physiological temperatures. We demonstrate here that the constitutive HSE-binding activity present in F9 and PCC4.aza.R1 EC cells, as well as a similar activity found to be present in mouse embryonic stem cells, is composed predominantly of HSF2. HSF2 in F9 EC cells is trimerized and is present at higher levels than in a variety of nonembryonal cell lines, suggesting a correlation of these properties with constitutive HSE-binding activity. Surprisingly, transcription run-on assays suggest that HSF2 in unstressed EC cells does not stimulate transcription of two putative target genes, hsp70 and hsp86. Genomic footprinting analysis indicates that HSF2 is not bound in vivo to the HSE of the hsp70 promoter in unstressed F9 EC cells, although HSF2 is present in the nucleus and the promoter is accessible to other transcription factors and to HSF1 following heat shock. Thus trimerization and nuclear localization of HSF2 do not appear to be sufficient for in vivo binding of HSF2 to the HSE of the hsp70 promoter in unstressed F9 EC cells.

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