Journal articles: 'Colon cell lines'

1

O’Donoghue, Tristan, and Andrej Podlutsky. "DNA Repair in Colon Cancer Cell Lines." FASEB Journal 34, S1 (April 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.08754.

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Kleivi, Kristine, Manuel R. Teixeira, Mette Eknæs, Chieu B. Diep, Kjetill S. Jakobsen, Richard Hamelin, and Ragnhild A. Lothe. "Genome signatures of colon carcinoma cell lines." Cancer Genetics and Cytogenetics 155, no. 2 (December 2004): 119–31. http://dx.doi.org/10.1016/j.cancergencyto.2004.03.014.

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Yang, S. K., L. Eckmann, and M. F. Kagnoff. "Colon epithelial cell lines express multiple chemokines." Gastroenterology 108, no. 4 (April 1995): A946. http://dx.doi.org/10.1016/0016-5085(95)28090-1.

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VAN KLINKEN, B. JAN-WILLEM, ESMERALDA OUSSOREN, JAN-JOHAN WEENINK, HANS A. BÜLLER, JAN DEKKER, and ALEXANDRA W. C. EINERHAND. "Mucin expression in colon adenocarcinoma cell lines." Biochemical Society Transactions 23, no. 4 (November 1, 1995): 529S. http://dx.doi.org/10.1042/bst023529s.

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Warns, Jessica, Gurdeep Marwarha, Natalie Freking, and Othman Ghribi. "27-hydroxycholesterol decreases cell proliferation in colon cancer cell lines." Biochimie 153 (October 2018): 171–80. http://dx.doi.org/10.1016/j.biochi.2018.07.006.

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Reda, F., J. Borjac, R. Fakhouri, and J. Usta. "Cytotoxic effect ofMoringa oleiferaon colon cancer cell lines." Acta Horticulturae, no. 1158 (April 2017): 269–78. http://dx.doi.org/10.17660/actahortic.2017.1158.30.

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Ophir, I., E. Cohen, and Y. Ben Shaul. "Apical polarity in human colon carcinoma cell lines." Tissue and Cell 27, no. 6 (December 1995): 659–66. http://dx.doi.org/10.1016/s0040-8166(05)80021-7.

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Hasenoehrl, Carina, David Feuersinger, Melanie Kienzl, and Rudolf Schicho. "GPR55-Mediated Effects in Colon Cancer Cell Lines." Medical Cannabis and Cannabinoids 2, no. 1 (February 22, 2019): 22–28. http://dx.doi.org/10.1159/000496356.

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The cannabinoid-responsive G protein-coupled receptor GPR55 and its endogenous ligand L-α-lysophosphatidylinositol (LPI) have been reported to play a role in several cancers. A proliferation-enhancing effect of GPR55 has been described for several cancer cell lines and LPI has been found elevated in cancer patients. The aim of this study was to investigate whether GPR55 signaling had an effect on the proliferation of colon cancer cell lines. Using cell viability assays and Western blotting, we show that stable overexpression of the GPR55 receptor led to a growth advantage of SW480 cells per se. Proliferation of native colon cancer cell lines, however, was not affected by pharmacological manipulation of GPR55. Interestingly though, GPR55 signaling was responsive to treatment with both the GPR55 agonist LPI and the antagonist CID16020046 in the overexpressing cancer cell lines. This was evident through significantly increased or decreased levels of phosphorylated ERK1/2, respectively. Taken together, our findings suggest that GPR55 is constitutively activated in overexpressing colon cancer cells affecting ERK1/2 phosphorylation and cell proliferation.

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Imperlini, Esther, Irene Colavita, Marianna Caterino, Peppino Mirabelli, Daniela Pagnozzi, Luigi Del Vecchio, Rosa Di Noto, Margherita Ruoppolo, and Stefania Orrù. "The secretome signature of colon cancer cell lines." Journal of Cellular Biochemistry 114, no. 11 (September 13, 2013): 2577–87. http://dx.doi.org/10.1002/jcb.24600.

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Russo, Suzanne, Nan Li, Kevin Lee, Yaguang Xi, Bing Zhu, Bernard Gary, Veronica Ramirez, et al. "Phosphodiesterase 10, a novel target in colon cancer." Journal of Clinical Oncology 32, no. 3_suppl (January 20, 2014): 503. http://dx.doi.org/10.1200/jco.2014.32.3_suppl.503.

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503 Background: Elevation of intracellular cGMP is known to inhibit tumor proliferation and induce apoptosis, although the phosphodiesterase (PDE) isozymes that regulate cGMP levels in tumor cells have not been well studied. We report first evidence that PDE10 is elevated in colon tumors compared with normal colon and suggest that PDE10 inhibitors can be used for the treatment or prevention of colon cancer. Methods: PDE10 protein and mRNA levels were measured in human colon tumor cells (HT29, HCT116, SW480, Caco2), normal colonocytes (NCM460), human clinical samples, and ApcMin/+ mouse model. Two chemically distinct PDE10 selective inhibitors, PQ-10 and Pf-2545920, were tested against the cell lines. The NCI-60 panel of human tumor cell lines was also screened against Pf-2545920 to identify potential differences in sensitivity among histologically diverse tumor types. We also performed siRNA knockdown studies in colonocytes and tumor cell lines. To determine the effect of the PDE10 siRNA knockdown on cyclic nucleotide hydrolysis, whole cell lysates from transfected cells were assayed for PDE activity using cGMP or cAMP as substrates. Results: PDE10 levels were low in normal colonocytes (NCM460) and elevated in tumor cell lines. Similarly, PDE10 was elevated human clinical specimens and the ApcMin+/ mouse model compared with normal mucosa. PDE10 inhibitors and siRNA selectively inhibited colonic tumor growth while stable knockdown inhibited colony formation and increased doubling time. Pf-2545920 also supressed growth of all cell lines within the NCI-60 panel. In comparison with lysates from vector control cells, transfection with PDE10 siRNA reduced cGMP hydrolysis by ~35% in both HCT116 and HT29 cell lines, but did not affect cGMP hydrolysis in colonocytes; siRNA did not significantly affect cAMP degradation in all 3 cell lines. Conclusions: PDE10 plays a role in colon tumorgenesis whereby inhibitors can selectively suppress tumor cell growth. The mechanism by which PDE10 inhibition affects growth appears to involve activation of cGMP/PKG signalling. PDE10 represents a novel anticancer target for the treament and prevention of colon cancer.

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Yang, Li-Guang, Xiang-An Tian, Xiao-Yan Li, Jian-Guo Huang, Nai-Qing Liu, and Qin-Li Sun. "Trolox induces inhibition of cell proliferation and apoptosis in human colon cancer cells." Bangladesh Journal of Pharmacology 10, no. 4 (November 6, 2015): 931. http://dx.doi.org/10.3329/bjp.v10i4.23651.

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<p class="Abstract">In the present study, the effect of trolox on human colon cancer cell lines was investigated. The results revealed that trolox treatment caused inhibition of cell growth in T84 and HCT-15 colon cancer cell lines in a dose-dependent manner. The inhibition was significant at 50 µM of trolox after 48 hours in both cell lines. Trolox treatment promoted expression of p38 and inhibited expression of survivin and Akt. It also induced cleavage of PARP and caspase-3 and ultimately induced apoptosis in T84 and HCT-15 cells. The tumor growth was inhibited significantly in the xenotransplanted mice on treatment with trolox compared to the control group. Since trolox treatment exhibits inhibitory effect on the proliferation of colon cancer cells and inhibits tumor growth in vivo therefore, can be of therapeutic importance for the treatment of colon cancer.</p><p> </p>

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Israelsson, Stina, Nina Jonsson, Maria Gullberg, and A. Michael Lindberg. "Cytolytic replication of echoviruses in colon cancer cell lines." Virology Journal 8, no. 1 (2011): 473. http://dx.doi.org/10.1186/1743-422x-8-473.

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13

Latta, R. K., H. Fiander, N. W. Ross, C. Simpson, and H. Schneider. "Toxicity of bile acids to colon cancer cell lines." Cancer Letters 70, no. 3 (July 1993): 167–73. http://dx.doi.org/10.1016/0304-3835(93)90227-z.

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Singh, P., Z. Xu, B. Dai, S. Rajaraman, N. Rubin, and B. Dhruva. "Incomplete processing of progastrin expressed by human colon cancer cells: role of noncarboxyamidated gastrins." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 3 (March 1, 1994): G459—G468. http://dx.doi.org/10.1152/ajpgi.1994.266.3.g459.

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Gastrin is mitogenic for several colon cancers. To assess a possible autocrine role of gastrin in colon cancers, we examined human colon cancer cell lines for expression of gastrin mRNA and various forms of gastrin. Gastrin mRNA was not detected in the majority of colon cancer cell lines by Northern hybridization but was detected in all human colon cancer lines by the sensitive method of reverse transcriptase-polymerase chain reaction (PCR). Gastrin mRNA was quantitated by the competitive PCR method. The majority of cell lines expressed very low levels of gastrin mRNA (< 1-5 copies/cell); only one cell line expressed > 20 copies/cell. The mature carboxyamidated form of gastrin was not detected in any of the cell lines by radioimmunoassay or immunocytochemistry. Results suggested that either gastrin mRNA expressed by colon cancer cells was altered (mutated) or posttranslational processing of progastrin was incomplete. Gastrin cDNA from all the colon cancer cell lines had an identical sequence to the published sequence of human gastrin cDNA. Specific antibodies against precursor forms of gastrin were used, and significant concentrations of nonamidated (glycine-extended) and prepro forms of gastrin were measured in tumor extracts of representative colon cancer cell lines. The presence of precursor forms of gastrin suggested a lack of one or more of the processing enzymes and/or cofactors. Significant concentrations of the processing enzyme (peptidylglycine alpha-amidating monooxygenase) were detected in colon cancer cells by immunocytochemistry. Therefore, lack of other cofactors or enzymes may be contributing to incomplete processing of precursor forms of gastrin, which merits further investigation. Since low levels of gastrin mRNA were expressed by the majority of human colon cancer cell lines and progastrin was incompletely processed, it seems unlikely that gastrin can function as a viable autocrine growth factor for colon cancer cells. High concentrations of glycine-extended gastrin-17 (GG) (> 10(-6) M) were mitogenic for a gastrin-responsive human colon cancer (DLD-1) cell line in vitro. It remains to be seen if GG or other precursor forms of gastrin are similarly mitogenic in vivo, which may then lend credibility to a possible autocrine role of gastrinlike peptides in colon cancers.

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15

KE, J., X. WU, X. WU, X. HE, L. LIAN, Y. ZOU, X. HE, et al. "A subpopulation of CD24+ cells in colon cancer cell lines possess stem cell characteristics." Neoplasma 59, no. 03 (2012): 282–88. http://dx.doi.org/10.4149/neo_2012_036.

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16

Wang, Rui, In-Kiu Kwon, Muthusamy Thangaraju, Nagendra Singh, Kebin Liu, Philippe Jay, Franz Hofmann, Vadivel Ganapathy, and Darren D. Browning. "Type 2 cGMP-dependent protein kinase regulates proliferation and differentiation in the colonic mucosa." American Journal of Physiology-Gastrointestinal and Liver Physiology 303, no. 2 (July 15, 2012): G209—G219. http://dx.doi.org/10.1152/ajpgi.00500.2011.

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Signaling through cGMP has emerged as an important regulator of tissue homeostasis in the gastrointestinal tract, but the mechanism is not known. Type 2 cGMP-dependent protein kinase (PKG2) is a major cGMP effector in the gut epithelium, and the present studies have tested its importance in the regulation of proliferation and differentiation in the mouse colon and in colon cancer cell lines. Tissue homeostasis was examined in the proximal colon of Prkg2 −/− mice using histological markers of proliferation and differentiation. The effect of ectopic PKG2 on proliferation and differentiation was tested in vitro using inducible colon cancer cell lines. PCR and luciferase reporter assays were used to determine the importance of Sox9 downstream of PKG2. The colons of Prkg2 −/− mice exhibited crypt hyperplasia, increased epithelial apoptosis, and reduced numbers of differentiated goblet and enteroendocrine cells. Ectopic PKG2 was able to inhibit proliferation and induce Muc2 and CDX2 expression in colon cancer cells, but did not significantly affect cell death. PKG2 reduced Sox9 levels and signaling, suggesting possible involvement of this pathway downstream of cGMP in the colon. The work presented here demonstrates a novel antiproliferative and prodifferentiation role for PKG2 in the colon. These homeostatic functions of PKG2 were reproducible in colon cancer cells lines where downregulation of Sox9 is a possible mechanism. The similarities in phenotype between PKG2 and GCC knockout mice positions PKG2 as a likely mediator of the homeostatic effects of cGMP signaling in the colon.

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17

Cox, Helen M. "Receptors for calcitonin gene related peptide (CGRP) in gastrointestinal epithelia." Canadian Journal of Physiology and Pharmacology 73, no. 7 (July 1, 1995): 974–80. http://dx.doi.org/10.1139/y95-135.

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A pharmacological comparison of calcitonin gene related peptide (CGRP) receptors expressed in normal rat colon mucosa and two human adenocarcinoma cell lines has been undertaken. Using voltage-clamp techniques electrogenic ion transport was continuously monitored across either mucosal preparations or confluent epithelial monolayers grown on permeable supports. The data presented at this meeting show that CGRP receptors are preferentially located on the basolateral epithelial surface and that their stimulation by a variety of CGRP analogues results in enhanced Cl− secretion mediated via a cyclic AMP dependent mechanism. Responses to rat αCGRP in rat descending colon mucosa and in the adenocarcinoma cell line Colony-29 are insensitive to the inhibitory effects of the C-terminal fragment human CGRP(8–37); however, significant inhibition of rat αCGRP responses was observed in the parent epithelial cell line HCA-7. This together with the subtle differences seen in agonist orders of potency in the three preparations indicates that different CGRP receptor subtypes exist in the basolateral domains of HCA-7 compared with rat colon and Colony-29 epithelia.Key words: calcitonin gene related peptide, receptors, ion transport, rat colon, epithelial cell lines.

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18

Xu, Mei-Hua. "Effect of indomethacin on cell cycle proteins in colon cancer cell lines." World Journal of Gastroenterology 11, no. 11 (2005): 1693. http://dx.doi.org/10.3748/wjg.v11.i11.1693.

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Whitehead, Robert H., and Pamela S. Robinson. "Establishment of conditionally immortalized epithelial cell lines from the intestinal tissue of adult normal and transgenic mice." American Journal of Physiology-Gastrointestinal and Liver Physiology 296, no. 3 (March 2009): G455—G460. http://dx.doi.org/10.1152/ajpgi.90381.2008.

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It has proved to be impossible to culture epithelial cells from the gastrointestinal tract of adult animals. Researchers have had to use either cell lines derived from newborn rat small intestine or colon carcinoma cell lines that have retained some of the properties of the gastrointestinal mucosa. We have described a method for establishing conditionally immortalized cell lines from the stomach, small intestine, colon, pancreas, and liver from tissue obtained from a transgenic mouse strain carrying a temperature-sensitive mutant of the SV40 large T gene (the “Immortomouse”). This immortalizing gene has proved to be useful for establishing cell lines from a number of transgenic mice following crossbreeding of the Immortomouse with the transgenic mouse of interest. These cell lines are being used in numerous studies. In this review we describe the methods for developing such lines and list the range of cell lines that have been developed from colon, small intestine, stomach, liver, and pancreas of a number of transgenic mice.

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Miao, Xiaofei, Zengyao Li, Ye Zhang, and Tong Wang. "MicroRNA-4284 inhibits colon cancer epithelial-mesenchymal transition by down-regulating Perilipin 5." STEMedicine 2, no. 6 (March 16, 2021): e85. http://dx.doi.org/10.37175/stemedicine.v2i6.85.

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Background: MicroRNA (miR) has been suggested in the development of several types of cancer; yet, the exact function of miR-4284 in colon cancer remains elusive. Methods: MiR-4284 expression was assessed in normal colon cell line CCD-18Co, and HT-29 and SW480 cell lines representing human colon cancer. Potential target gene of miR-4284 was predicted using TargetScanHuman, and experimentally verified using luciferase report assay. Wound-healing, cell invasion and attachment were evaluated to determine the effect of miR-4284 on the migration, invasion, and metastatic properties of colon cancer cell lines. Expression of epithelial-mesenchymal transition (EMT) phenotypic protein hallmarks, including N-cadherin, E-cadherin, as well as Vimentin, was also evaluated. Results: MiR-4284 was significantly decreased in colon cancer cell lines, and Perilipin 5 (PLIN5) was found to be directly targeted by miR-4284. Ectopic expression of miR-4284 significantly reduced endogenous expression level of PLIN5 in colon cancer cell lines, suppressing migration, invasion, and metastatic phenotypes. In addition, re-introducing miR-4284 reversed the expression profile of EMT markers. Conclusion: Our findings for the first time identify miR-4284 as an anti-tumor miRNA in colon cancer, which acts to reduce PLIN5 and inhibit EMT, leading to inhibited colon cancer tumorigenesis. These results highlight the potential of miR-4284 as a therapeutic target in metastatic colon cancer.

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Schlottmann, Klaus, Frank-Peter Wachs, Rene C. Krieg, Juergen Schoelmerich, and Gerhard Rogler. "Bile salt induced apoptosis in colon cancer cell lines: Mechanisms and differences to primary colon epithelial cells." Gastroenterology 118, no. 4 (April 2000): A553. http://dx.doi.org/10.1016/s0016-5085(00)84345-0.

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22

Liu, Y., H. Huang, B. Yuan, L. Zhuang, T. Luo, and Q. Zhang. "Lentivirus-Mediated Knockdown of NOB1 Suppresses the Proliferation of Colon Cancer Cells." Zeitschrift für Gastroenterologie 52, no. 05 (May 2014): 429–35. http://dx.doi.org/10.1055/s-0033-1356338.

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AbstractNOB1 is important for ribosome biogenesis and protein degradation. Previous studies showed that it could regulate the growth and colony-formation ability of ovarian, breast and hepatocellular carcinoma cells. However, its function in colon cancer cells is largely unknown. In this study, we found that NOB1 could express in 6 different colon cancer cell lines. Lentivirus-mediated shRNA targeted NOB1 could suppress the endogenous gene expression. NOB1 depletion significantly inhibited cell proliferation and colony formation ability, as determined by MTT and colony formation assays. Flow cytometry analysis showed NOB1 silencing arrested cell cycle in G0 / G1 phase. Moreover, the percentage of cells at sub-G1 phase dramatically increased after NOB1 knockdown. These results indicate that NOB1 may play an important role in the growth and tumorigensis of colon cancer and knockdown of NOB1 may be a potential therapeutic method for colon cancer in the future.

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23

Miyake, Katsunori, Feng Li, Yasuhiro Tezuka, Suresh Awale, and Shigetoshi Kadota. "Cytotoxic Activity of Quassinoids from Eurycoma longifolia." Natural Product Communications 5, no. 7 (July 2010): 1934578X1000500. http://dx.doi.org/10.1177/1934578x1000500704.

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Twenty-four quassinoids isolated from Eurycoma longifolia Jack were investigated for their cytotoxicity against a panel of four different cancer cell lines, which includes three murine cell lines [colon 26-L5 carcinoma (colon 26-L5), B16-BL6 melanoma (B16-BL6), Lewis lung carcinoma (LLC)] and a human lung A549 adenocarcinoma (A549) cell line. Among the tested compounds, eurycomalactone (9) displayed the most potent activity against all the tested cell lines; colon 26-L5 (IC50 = 0.70 μM), B16-BL6 (IC50 = 0.59 μM), LLC (IC50 = 0.78 μM), and A549 (IC50 = 0.73 μM). These activities were comparable to clinically used anticancer agent doxorubicin (colon 26-L5, IC50 = 0.76 μM; B16-BL6, IC50 = 0.86 μM; LLC, IC50 = 0.80 μM; A549, IC50 = 0.66 μM).

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Chen, Ying-Xuan. "Histone acetylation regulates p21WAF1expression in human colon cancer cell lines." World Journal of Gastroenterology 10, no. 18 (2004): 2643. http://dx.doi.org/10.3748/wjg.v10.i18.2643.

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25

Arnould, S., I. Hennebelle, P. Canal, R. Bugat, and S. Guichard. "Cellular determinants of oxaliplatin sensitivity in colon cancer cell lines." European Journal of Cancer 39, no. 1 (January 2003): 112–19. http://dx.doi.org/10.1016/s0959-8049(02)00411-2.

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26

Pires, A. S., C. R. Marques, J. C. Encarnação, T. J. Gonçalves, A. C. Mamede, J. E. Casalta-Lopes, A. C. Gonçalves, A. M. Abrantes, A. B. Sarmento-Ribeiro, and M. F. Botelho. "756: Ascorbic acid-induced cytotoxicity in colon cancer cell lines." European Journal of Cancer 50 (July 2014): S182. http://dx.doi.org/10.1016/s0959-8049(14)50664-8.

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27

Hamidinia, Maryam, Mohammad Ramezani, and Zahra Mojtahedi. "Cytotoxic/Proliferative Effects of Umbelliprenin on Colon Cancer Cell Lines." Annals of Colorectal Research 1, no. 3 (December 30, 2013): 101–5. http://dx.doi.org/10.17795/acr-12476.

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28

Jaganathan, Saravana Kumar, Abhijit Mazumdar, Dilip Mondhe, and Mahitosh Mandal. "Apoptotic effect of eugenol in human colon cancer cell lines." Cell Biology International 35, no. 6 (April 28, 2011): 607–15. http://dx.doi.org/10.1042/cbi20100118.

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Mathur, Priya S., Rosa M. Xicola, Xavier Llor, and Angela L. Tyner. "50 PTK6 Antagonizes the EMT in Colon Cancer Cell Lines." Gastroenterology 146, no. 5 (May 2014): S—14. http://dx.doi.org/10.1016/s0016-5085(14)60050-0.

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30

Hanauske, AR, J. Buchok, W. Scheithauer, and DD Von Hoff. "Human colon cancer cell lines secrete α TGF-like activity." British Journal of Cancer 55, no. 1 (January 1987): 57–59. http://dx.doi.org/10.1038/bjc.1987.12.

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Windham, T. Christopher, Nila U. Parikh, Doris R. Siwak, Justin M. Summy, David J. McConkey, Alan J. Kraker, and Gary E. Gallick. "Src activation regulates anoikis in human colon tumor cell lines." Oncogene 21, no. 51 (November 2002): 7797–807. http://dx.doi.org/10.1038/sj.onc.1205989.

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32

Ahmed, D., P. W. Eide, I. A. Eilertsen, S. A. Danielsen, M. Eknæs, M. Hektoen, G. E. Lind, and R. A. Lothe. "Epigenetic and genetic features of 24 colon cancer cell lines." Oncogenesis 2, no. 9 (September 2013): e71-e71. http://dx.doi.org/10.1038/oncsis.2013.35.

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Barkla, David H., Robert H. Whitehead, and Ian P. Hayward. "Effects of cholera toxin on human colon carcinoma cell lines." Pathology 24, no. 4 (1992): 296–301. http://dx.doi.org/10.3109/00313029209068884.

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Duerr, Eva-Maria, Yusuke Mizukami, Kentaro Moriichi, Manish Gala, Won-Seok Jo, Hirotoshi Kikuchi, Ramnik J. Xavier, and Daniel C. Chung. "Oncogenic KRAS regulates BMP4 expression in colon cancer cell lines." American Journal of Physiology-Gastrointestinal and Liver Physiology 302, no. 10 (May 15, 2012): G1223—G1230. http://dx.doi.org/10.1152/ajpgi.00047.2011.

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Activating mutations in the KRAS oncogene are common in colorectal cancer. However, the complete spectrum of KRAS targets that mediate its tumorigenic effect has not yet been fully delineated. We identified bone morphogenetic protein 4 (Bmp4), a transforming growth factor-β family member that regulates development and tissue homeostasis, as a new target of KRAS. In SW480, Hela, and 293 cells, oncogenic KRAS V12 downregulated BMP4 RNA levels, a BMP4 promoter luciferase construct, and Bmp4 protein levels. The MEK inhibitor PD98059 but not the phosphatidylinositol 3-kinase inhibitor LY294002 blocked this downregulation of BMP4. To identify the region of the BMP4 promoter that mediated this regulation by KRAS, serial 5′-deletions of the promoter were generated. An inhibitory region was identified between −3,285 and −3,258 bp in the Bmp4 promoter. In summary, oncogenic KRAS can downregulate Bmp4 through a transcriptional pathway that depends on ERK. These findings point to a unique link between two pathways that are frequently altered in colon cancer.

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Bernet-Camard, Marie Françoise, Marie Hélène Coconnier, Sylvie Hudault, and Alain L. Servin. "Differentiation-Associated Antimicrobial Functions in Human Colon Adenocarcinoma Cell Lines." Experimental Cell Research 226, no. 1 (July 1996): 80–89. http://dx.doi.org/10.1006/excr.1996.0205.

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Stewart, LaMonica V., and Mary L. Thomas. "Retinoids Differentially Regulate the Proliferation of Colon Cancer Cell Lines." Experimental Cell Research 233, no. 2 (June 1997): 321–29. http://dx.doi.org/10.1006/excr.1997.3569.

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Lavagna, Christian, Jean-Luc Burgaud, Piero Del Soldato, and Patrick Rampal. "Antiproliferative Effects of Nitrosulindac on Human Colon Adenocarcinoma Cell Lines." Biochemical and Biophysical Research Communications 284, no. 3 (June 2001): 808–16. http://dx.doi.org/10.1006/bbrc.2001.5057.

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Zhang, Jian-jun, Er-xun Ding, Qiang Wang, Xue-yun Chen, and Zhi-ren Fu. "Expression of fas ligand in human colon cancer cell lines." Chinese Journal of Cancer Research 13, no. 4 (December 2001): 262–64. http://dx.doi.org/10.1007/s11670-001-0044-6.

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Seweryn, Ewa, Michał Glehsk, Kamila Środa-Pomianek, Ireneusz Ceremuga, Maciej Włodarczyk, and Andrzej Gamian. "Cytotoxic Effects of Four Aescin Types on Human Colon Adenocarcinoma Cell Lines." Natural Product Communications 9, no. 3 (March 2014): 1934578X1400900. http://dx.doi.org/10.1177/1934578x1400900328.

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Four types of aescin that are available on the pharmaceutical market, β-aescin crystalline, β-aescin amorphous, β-aescin sodium and aescin polysulfate, have been analyzed for their cytotoxic effects on human colon adenocarcinoma (LoVo) and doxorubicin-resistant human colon adenocarcinoma cell lines (LoVo/Dx). Their cytotoxic activities were evaluated by sulforhodamine B (SRB) and methyl tetrazolium (MTT) assays. All four types of aescin exerted strong dose-dependent cytotoxicity to LoVo and, to a lesser degree, LoVo/Dx cell lines. The IC50 value for the LoVo/Dx cell line was higher, but still dose-dependent. Results from both assays demonstrated that β-aescin crystalline has the most cytotoxic activity toward human colon adenocarcinoma cell lines.

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Wang, Can, Yujuan Yue, Bianfei Shao, Zhu Qiu, Junhao Mu, Jun Tang, Xiaofan Han, Tingxiu Xiang, and Guosheng Ren. "Dickkopf-Related Protein 2 is Epigenetically Inactivated and Suppresses Colorectal Cancer Growth and Tumor Metastasis by Antagonizing Wnt/β-Catenin Signaling." Cellular Physiology and Biochemistry 41, no. 5 (2017): 1709–24. http://dx.doi.org/10.1159/000471861.

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Background/Aims: Aberrant activation of the Wnt/β-catenin signaling pathway plays a key role in the pathogenesis of multiple tumors including digestive cancers. Recent studies have reported that Dickkopf-related protein 2 (DKK2) is epigenetically inactivated in numerous types of cancers and that its gene products exhibit tumor-suppressive properties. However, the biological functions and underlying molecular mechanisms of DKK2 in colon carcinoma remains obscure. Methods: We examined the expression of DKK2 in colon tumor cell lines by RT-PCR and its promoter methylation status in colon tumor cell lines and primary tumors by methylation-specific PCR (MSP). Ectopic expression of DKK2 was measured by RT-PCR prior to the other experiments. To investigate the function of DKK2, we assayed colony formation and cell proliferation, utilized flow cytometric analyses of the cell cycle and acridine orange/ethidium bromide (AO/EB) fluorescence staining for apoptosis, and examined wound healing, transwell migration and tumor growth in vivo. Western blots were used to explore the mechanisms of DKK2 in epithelial- mesenchymal transition and canonical Wnt/β-catenin signaling. Results: We show here that downregulation or silencing of DKK2 was closely associated with the hypermethylation status of its promoter and that DKK2 expression could be restored by demethylation treatment. Methylation of the DKK2 promoter was detected in nearly all tumors and tumor-adjacent tissues, but not in normal colon tissues. Ectopic expression of DKK2 in colon cell lines HCT116 and HT-29 inhibited colony formation and cell viability by inducing cell cycle G0/G1 arrest and apoptosis, and growth of stable DKK2-infected HCT116 cells in nude mice was decreased compared to controls. Furthermore, DKK2 restrained cell migration through partial reversal of epithelial-to- mesenchymal transition and also by downregulating several stem cell markers. Our data further showed that restoration of DKK2 expression resulted in downregulation of active β-catenin and its downstream target genes. Conclusion: DKK2 appears to be a functional tumor suppressor regulating tumorigenesis of colorectal cancer by antagonizing Wnt/β-catenin signaling.

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Lachmann, P., R. Benke, V. Schirrmacher, and P. Schlag. "Cell adhesion and migration of different human colon cell lines and primary tumors." Journal of Cancer Research and Clinical Oncology 114, no. 5 (October 1988): 493–96. http://dx.doi.org/10.1007/bf00391498.

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Mermelshtein, A., A. Gerson, S. Walfisch, B. Delgado, G. Shechter-Maor, J. Delgado, A. Fich, and L. Gheber. "Expression of D-type cyclins in colon cancer and in cell lines from colon carcinomas." British Journal of Cancer 93, no. 3 (July 12, 2005): 338–45. http://dx.doi.org/10.1038/sj.bjc.6602709.

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Wang, Yiling, Jiantao He, Shenghui Zhang, Qingbo Yang, Bo Wang, Zhiyu Liu, and Xintian Wu. "Knockdown of Immature Colon Carcinoma Transcript 1 Inhibits Proliferation and Promotes Apoptosis of Non–Small Cell Lung Cancer Cells." Technology in Cancer Research & Treatment 16, no. 5 (July 13, 2016): 559–69. http://dx.doi.org/10.1177/1533034616657977.

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Non–small cell lung cancer, as the most frequent type lung cancer, has lower survival rate of 5 years, despite improvements in surgery and chemotherapy. Previous studies showed immature colon carcinoma transcript 1 is closely related to tumorigenesis of human cancer cells. In the present study, we found immature colon carcinoma transcript 1 was overexpressed in lung cancer tissues using Oncomine database mining, and the biological effect of immature colon carcinoma transcript 1 was investigated in non–small cell lung cancer cell lines 95D and A549. Lentivirus-mediated RNA interference was used to knock down immature colon carcinoma transcript 1 expression in 95D and A549 cells in vitro, and the knockdown efficiency was determined using quantitative real-time polymerase chain reaction and Western blot assay. Knockdown of immature colon carcinoma transcript 1 significantly suppressed non–small cell lung cancer cell proliferation and colony formation ability confirmed by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide and colony formation assay. Flow cytometry was applied to measure cell cycle arrest, and the result showed the cell cycle arrested in G2/M phase in 95D cells and arrested in G0/G1 phase in A549 cells. Furthermore, we measured the levels of cell cycle–associated proteins by Western blot analysis and found immature colon carcinoma transcript 1 –mediated cell proliferation inhibition appeared due to downregulation of cell cycle activator cyclin D1 and upregulation of cell cycle inhibitor p21. In addition, immature colon carcinoma transcript 1 silencing significantly induced non–small cell lung cancer cell apoptosis by annexin V/7-amino-actinomycin D double-staining assay. All our data suggest that immature colon carcinoma transcript 1 may play an important role for non–small cell lung cancer cell proliferation and could be a potential molecular target for diagnosing and treating human non–small cell lung cancer.

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Rao, Poorima BN, and Farah Deeba. "Expressions of biomarkers in MCF7 Breast and Colon Cancer Cell Lines." Journal of Drug Delivery and Therapeutics 10, no. 2 (March 15, 2020): 107–14. http://dx.doi.org/10.22270/jddt.v9i4-s.3993.

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Cancer is one of the leading causes of death which accounts for 13% of total deaths, worldwide. Colorectal and Breast cancer fall under main categories according to World Health Organisation (WHO) cancer facts sheet 1. The need to understand the expression of clinical biomarkers in breast cancer and colon cancer is necessary for diagnosis and therapeutic response. In this article, the expressions of histone H1 and TP53 biomarkers were established for four different colon cancer cell lines and compared with the expressions of MCF7 cell line. The results show varied expression of Histone H1 along with TP53 markers among the cell lines. The results suggest that the linker Histone H1 has shown nuclear localization in HCT 116p53 wt (wild type) cancer cell line whereas it has shown cytoplasmic distribution in the respective null type cell line with intense expression. The result also suggests that a localized distribution in HRA19 cells and a diffused distribution in SNU-C2B cell line. These established results were compared with the expression of the biomarkers in MCF7 in order to get a better understanding. Keywords: Tumour Proteins, p53, H1, MCF-7 cell, HCT116, HRA19.

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Jaszewski, Richard, Ahmed Khan, Fazlul H. Sarkar, Omer Kucuk, Martin Tobi, Abbas Zagnoon, Ravi Dhar, Joseph Kinzie, and Adhip P. N. Majumdar. "Folic acid inhibition of EGFR-mediated proliferation in human colon cancer cell lines." American Journal of Physiology-Cell Physiology 277, no. 6 (December 1, 1999): C1142—C1148. http://dx.doi.org/10.1152/ajpcell.1999.277.6.c1142.

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Although accumulating evidence suggests a chemopreventive role for folic acid in colon cancer, the regulation of this process in unknown. We hypothesize that supplemental folic acid exerts its chemopreventive role by inhibiting mucosal hyperproliferation, an event considered to be central to the initiation of carcinogenesis in the gastrointestinal tract. The present investigation examines the effect of supplemental folic acid on proliferation of Caco-2 and HCT-116 colon cancer cell lines. Furthermore, because certain tyrosine kinases, particularly epidermal growth factor receptor (EGFR), play a role in regulating cell proliferation, we also examined the folic acid-induced changes in tyrosine kinase activity and expression of EGFR. In Caco-2 and HCT-116 cells, maintained in RPMI 1640 medium containing 1 μg/ml folic acid, we observed that the supplemental folic acid inhibited proliferation in a dose-dependent manner. Pretreatment of HCT-116 and Caco-2 cell lines with supplemental folic acid (1.25 μg/ml) completely abrogated transforming growth factor-α (TGF-α)-induced proliferation in both cell lines. Tyrosine kinase activity and the relative concentration of EGFR were markedly diminished in both cell lines following a 24-h exposure to supplemental folic acid. The folic acid-induced inhibition of EGFR tyrosine kinase activity in colon cancer cell lines was also associated with a concomitant reduction in the relative concentration of the 14-kDa membrane-bound precursor form of TGF-α. In conclusion, our data suggest that supplemental folic acid is effective in reducing proliferation in two unrelated colon cancer cell lines and that EGFR tyrosine kinase appears to be involved in regulating this process.

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Fuentes-Baile, María, Daniel Bello-Gil, Elizabeth Pérez-Valenciano, Jesús M. Sanz, Pilar García-Morales, Beatriz Maestro, María P. Ventero, Cristina Alenda, Víctor M. Barberá, and Miguel Saceda. "CLytA-DAAO, Free and Immobilized in Magnetic Nanoparticles, Induces Cell Death in Human Cancer Cells." Biomolecules 10, no. 2 (February 3, 2020): 222. http://dx.doi.org/10.3390/biom10020222.

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D-amino acid oxidase (DAAO) catalyzes the oxidation of D-amino acids generating hydrogen peroxide, a potential producer of reactive oxygen species. In this study, we used a CLytA-DAAO chimera, both free and bound to magnetic nanoparticles, against colon carcinoma, pancreatic adenocarcinoma, and glioblastoma cell lines. We found that the enzyme induces cell death in most of the cell lines tested and its efficiency increases significantly when it is immobilized in nanoparticles. We also tested this enzyme therapy in non-tumor cells, and we found that there is not cell death induction, or it is significantly lower than in tumor cells. The mechanism triggering cell death is apparently a classical apoptosis pathway in the glioblastoma cell lines, while in colon and pancreatic carcinoma cell lines, CLytA-DAAO-induced cell death is a necrosis. Our results constitute a proof of concept that an enzymatic therapy, based on magnetic nanoparticles-delivering CLytA-DAAO, could constitute a useful therapy against cancer and besides it could be used as an enhancer of other treatments such as epigenetic therapy, radiotherapy, and treatments based on DNA repair.

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Sonoyama, Kei, Pimara Pholnukulkit, Masahiko Toyoda, Suriya Rutatip, and Takanori Kasai. "Upregulation of activin A gene by butyrate in human colon cancer cell lines." American Journal of Physiology-Gastrointestinal and Liver Physiology 284, no. 6 (June 1, 2003): G989—G995. http://dx.doi.org/10.1152/ajpgi.00384.2002.

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Activin A has been reported to play a role in the progression of colorectal cancer. Because dietary fiber protects against colorectal cancer, we hypothesized that butyrate, a fermentation product of dietary fiber, may affect the expression of activin A in colon cancer cells. Semiquantitative RT-PCR demonstrated that the activin A gene was upregulated by sodium butyrate in the human colon cancer cell lines HT-29 and Caco-2 in a concentration- and time-dependent manner. However, the activin A gene did not respond to sodium butyrate in the human normal colonic cell line FHC, rat normal intestinal epithelial cell (IEC) line IEC-6, and the explant of rat colon. Flow cytometry and agarose gel electrophoresis of genomic DNA revealed that cell cycle arrest and apoptosis were induced by sodium butyrate but not exogenous activin A in HT-29 cells, indicating that activin A could not act as an autocrine factor in colon cancer cells. By assuming that activin A promotes colorectal cancer spread as a paracrine factor, our findings suggest that butyrate could act as a tumor promoter in some circumstances.

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Dommann, Noëlle, Daniel Sánchez-Taltavull, Linda Eggs, Fabienne Birrer, Tess Brodie, Lilian Salm, Felix Alexander Baier, et al. "The LIM Protein Ajuba Augments Tumor Metastasis in Colon Cancer." Cancers 12, no. 7 (July 15, 2020): 1913. http://dx.doi.org/10.3390/cancers12071913.

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Colorectal cancer, along with its high potential for recurrence and metastasis, is a major health burden. Uncovering proteins and pathways required for tumor cell growth is necessary for the development of novel targeted therapies. Ajuba is a member of the LIM domain family of proteins whose expression is positively associated with numerous cancers. Our data shows that Ajuba is highly expressed in human colon cancer tissue and cell lines. Publicly available data from The Cancer Genome Atlas shows a negative correlation between survival and Ajuba expression in patients with colon cancer. To investigate its function, we transduced SW480 human colon cancer cells, with lentiviral constructs to knockdown or overexpress Ajuba protein. The transcriptome of the modified cell lines was analyzed by RNA sequencing. Among the pathways enriched in the differentially expressed genes, were cell proliferation, migration and differentiation. We confirmed our sequencing data with biological assays; cells depleted of Ajuba were less proliferative, more sensitive to irradiation, migrated less and were less efficient in colony formation. In addition, loss of Ajuba expression decreased the tumor burden in a murine model of colorectal metastasis to the liver. Taken together, our data supports that Ajuba promotes colon cancer growth, migration and metastasis and therefore is a potential candidate for targeted therapy.

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Dunne, Amanda L., Carmel Mothersill, Tracy Robson, George D. Wilson, and David G. Hirst. "Radiosensitization of Colon Cancer Cell Lines by Docetaxel: Mechanisms of Action." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 14, no. 9 (January 1, 2004): 447–54. http://dx.doi.org/10.3727/0965040041791455.

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Waldenmaier, D. "Rapid in vitro chemosensitivity analysis of human colon tumor cell lines." Toxicology and Applied Pharmacology 192, no. 3 (November 1, 2003): 237–45. http://dx.doi.org/10.1016/s0041-008x(03)00257-6.

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Journal articles on the topic 'Colon cell lines'

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