Academic literature on the topic 'Chinese Hamster Ovary cells'

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Journal articles on the topic "Chinese Hamster Ovary cells"

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Kaiden, Adina, and Sharon S. Krag. "Dolichol metabolism in Chinese hamster ovary cells." Biochemistry and Cell Biology 70, no. 6 (June 1, 1992): 385–89. http://dx.doi.org/10.1139/o92-060.

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The addition of oligosaccharide to asparagine residues of soluble and membrane-associated proteins in eukaryotic cells involves a polyisoprenoid lipid carrier, dolichol. In Chinese hamster ovary cells, the major isomer of this polyisoprenol has 19 isoprenyl units, the terminal one being saturated. Our laboratory has developed a procedure to analyze the levels and nature of the cell's dolichyl derivatives. Chinese hamster ovary cells contain predominately activated, anionic dolichol derivatives, such as oligosaccharyl pyrophosphoryldolichol, monoglycosylated phosphoryldolichols, and dolichyl phosphate. Our studies show that in growing cells there is continual synthesis of total dolichol. Also, preliminary data suggest there is no catabolism or secretion of this lipid. The level of dolichyl phosphate did not change significantly under a variety of conditions where the levels of enzyme activities utilizing dolichyl phosphate did change. These results suggested that these enzymes had access to the same pool of dolichyl phosphate and had similar Km values for this lipid.Key words: dolichol, dolichyl phosphate, metabolism, Chinese hamster ovary cells.
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Mahajan, Aditya D., Aislinn R. Daniels, Yim J. Rodriguez, and Maria-Teresa Herd. "Ultrasound characterization of Chinese hamster ovary cells." Journal of the Acoustical Society of America 132, no. 3 (September 2012): 1987. http://dx.doi.org/10.1121/1.4755333.

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Baycin-Hizal, Deniz, David L. Tabb, Raghothama Chaerkady, Lily Chen, Nathan E. Lewis, Harish Nagarajan, Vishaldeep Sarkaria, et al. "Proteomic Analysis of Chinese Hamster Ovary Cells." Journal of Proteome Research 11, no. 11 (October 5, 2012): 5265–76. http://dx.doi.org/10.1021/pr300476w.

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Lin, M. F., C. L. Wu, and T. C. Wang. "Pesticide clastogenicity in Chinese hamster ovary cells." Mutation Research/Genetic Toxicology 188, no. 3 (July 1987): 241–50. http://dx.doi.org/10.1016/0165-1218(87)90095-4.

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Luskey, K. L. "Conservation of promoter sequence but not complex intron splicing pattern in human and hamster genes for 3-hydroxy-3-methylglutaryl coenzyme A reductase." Molecular and Cellular Biology 7, no. 5 (May 1987): 1881–93. http://dx.doi.org/10.1128/mcb.7.5.1881.

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Regulation of the expression of 3-hydroxy-3-methyglutaryl coenzyme A (HMG-CoA) reductase is a critical step in controlling cholesterol synthesis. Previous studies in cultured Chinese hamster ovary cells have shown that HMG-CoA reductase is transcribed from a cholesterol-regulated promoter to yield a heterogeneous collection of mRNAs with 5' untranslated regions of 68 to 670 nucleotides in length. Synthesis of these molecules is initiated at multiple sites, and multiple donor sites are used to excise an intron in the 5' untranslated region. In the current paper, I report that human HMG-CoA reductase gene resembles the Chinese hamster gene in having multiple sites of transcription initiation that are subject to suppression by cholesterol. The human gene differs from the hamster gene in that a single donor splice site is used to excise the intron in the 5' untranslated region. All of the resulting RNAs have short 5' untranslated regions of 68 to 100 nucleotides. This difference in the splicing pattern of the first intron is species specific and not a peculiarity of cultured cells in that HMG-CoA reductase mRNAs from Syrian hamster livers resemble those of the cultured Chinese hamster ovary cells. Comparison of the DNA sequences of the HMG-CoA reductase promoters from three different species--humans, Syrian hamsters, and Chinese hamsters--shows a highly conserved region of 179 nucleotides that extends from 220 to 42 nucleotides upstream of the transcription initiation sites. This region is 88% identical between the human and Chinese hamster promoter. When fused to the coding region of the Escherichia coli chloramphenicol acetyltransferase gene, this highly conserved region of the reductase gene directs the cholesterol-regulated expression of chloramphenicol acetyltransferase in transfected hamster cells, further indicating the interspecies conservation of the regulatory elements.
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Luskey, K. L. "Conservation of promoter sequence but not complex intron splicing pattern in human and hamster genes for 3-hydroxy-3-methylglutaryl coenzyme A reductase." Molecular and Cellular Biology 7, no. 5 (May 1987): 1881–93. http://dx.doi.org/10.1128/mcb.7.5.1881-1893.1987.

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Regulation of the expression of 3-hydroxy-3-methyglutaryl coenzyme A (HMG-CoA) reductase is a critical step in controlling cholesterol synthesis. Previous studies in cultured Chinese hamster ovary cells have shown that HMG-CoA reductase is transcribed from a cholesterol-regulated promoter to yield a heterogeneous collection of mRNAs with 5' untranslated regions of 68 to 670 nucleotides in length. Synthesis of these molecules is initiated at multiple sites, and multiple donor sites are used to excise an intron in the 5' untranslated region. In the current paper, I report that human HMG-CoA reductase gene resembles the Chinese hamster gene in having multiple sites of transcription initiation that are subject to suppression by cholesterol. The human gene differs from the hamster gene in that a single donor splice site is used to excise the intron in the 5' untranslated region. All of the resulting RNAs have short 5' untranslated regions of 68 to 100 nucleotides. This difference in the splicing pattern of the first intron is species specific and not a peculiarity of cultured cells in that HMG-CoA reductase mRNAs from Syrian hamster livers resemble those of the cultured Chinese hamster ovary cells. Comparison of the DNA sequences of the HMG-CoA reductase promoters from three different species--humans, Syrian hamsters, and Chinese hamsters--shows a highly conserved region of 179 nucleotides that extends from 220 to 42 nucleotides upstream of the transcription initiation sites. This region is 88% identical between the human and Chinese hamster promoter. When fused to the coding region of the Escherichia coli chloramphenicol acetyltransferase gene, this highly conserved region of the reductase gene directs the cholesterol-regulated expression of chloramphenicol acetyltransferase in transfected hamster cells, further indicating the interspecies conservation of the regulatory elements.
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Choi, Min-Ho, Hyun-Myoung Cha, Sun-Mi Kim, Yong-Soo Choi, and Dong-Il Kim. "Effects of Silkworm Gland Hydrolysate on Albumin-erythropoietin Production in Transgenic Chinese Hamster Ovary Cells." KSBB Journal 28, no. 2 (April 27, 2013): 86–91. http://dx.doi.org/10.7841/ksbbj.2013.28.2.86.

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Chiang, T. R., and L. McConlogue. "Amplification and expression of heterologous ornithine decarboxylase in Chinese hamster cells." Molecular and Cellular Biology 8, no. 2 (February 1988): 764–69. http://dx.doi.org/10.1128/mcb.8.2.764.

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We have developed an amplifiable mammalian expression vector based on the enzyme ornithine decarboxylase (ODC). We show greater than 700-fold amplification of this vector in ODC-deficient Chinese hamster ovary cells. A passive coamplified marker, dihydrofolate reductase (dhfr), was amplified and overexpressed 1,000-fold. This ODC vector was a dominant marker in a variety of cell types and displayed at least 300-fold amplification in wild-type Chinese hamster ovary cells.
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Chiang, T. R., and L. McConlogue. "Amplification and expression of heterologous ornithine decarboxylase in Chinese hamster cells." Molecular and Cellular Biology 8, no. 2 (February 1988): 764–69. http://dx.doi.org/10.1128/mcb.8.2.764-769.1988.

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We have developed an amplifiable mammalian expression vector based on the enzyme ornithine decarboxylase (ODC). We show greater than 700-fold amplification of this vector in ODC-deficient Chinese hamster ovary cells. A passive coamplified marker, dihydrofolate reductase (dhfr), was amplified and overexpressed 1,000-fold. This ODC vector was a dominant marker in a variety of cell types and displayed at least 300-fold amplification in wild-type Chinese hamster ovary cells.
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Yang, Ganglong, Yingwei Hu, Shisheng Sun, Chuanzi Ouyang, Weiming Yang, Qiong Wang, Michael Betenbaugh, and Hui Zhang. "Comprehensive Glycoproteomic Analysis of Chinese Hamster Ovary Cells." Analytical Chemistry 90, no. 24 (November 20, 2018): 14294–302. http://dx.doi.org/10.1021/acs.analchem.8b03520.

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Dissertations / Theses on the topic "Chinese Hamster Ovary cells"

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Syddall, Katie Louise. "Directed evolution of Chinese Hamster Ovary cells." Thesis, University of Sheffield, 2016. http://etheses.whiterose.ac.uk/13836/.

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Goh, Shireen. "Micro-bioreactor design for Chinese hamster ovary cells." Thesis, Massachusetts Institute of Technology, 2013. http://hdl.handle.net/1721.1/82368.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Materials Science and Engineering, 2013.
Cataloged from PDF version of thesis.
Includes bibliographical references (p. 195-203).
The research objective is to design a micro-bioreactor for the culture of Chinese Hamster Ovary (CHO) cells. There is an increasing demand for upstream development in high-throughput micro-bioreactors specifically for the recombinant CHO cell line, an important cell line for producing recombinant protein therapeutics. In order to translate a micro-bioreactor originally designed by our group for bacteria to CHO cells, there would need to be significant modifications in the design of the micro-bioreactor due to the extreme sensitivity of CHO cells to physical and chemical stresses. Shear stresses inside the growth chamber will have to be reduced by three orders of magnitude. Moreover, the long doubling time of CHO cells requires a 2 weeks long culture. In a high surface to volume ratio micro-bioreactor, evaporation becomes a major problem. Contamination control is also vital for CHO cultures. In addition, the offline sampling volume required for validation necessitates a doubling of the working volume to 2mL. The newly designed Resistive Evaporation Compensated Actuated (RECA) micro-bioreactor is fully characterized in this thesis to ensure that the design meets the physical specifications of the required CHO cell culture conditions. The RECA micro-bioreactor will be tested with industrial recombinant CHO cell lines. This work is done in collaboration with Genzyme, USA and Sanofi-Aventis, Frankfurt. In this thesis, we also propose the use of dielectric spectroscopy electrodes for online cell viability sensing of CHO cells in micro-bioreactors. The electrodes are fabricated on polycarbonate, a biocompatible and optically clear thermoplastic that will be one of the future base material for microfluidic devices which can be rapidly prototyped. To demonstrate the viability of dielectric spectroscopy as an online viability sensor for CHO cells in a micro-bioreactor, the electrodes are used to characterize samples taken daily from a CHO shake flask batch culture without any sample modifications. Two different electrode geometries and correction methods will be compared to find the optimal system for viability measurements in a micro-bioreactor.
by Shireen Goh.
Ph.D.
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Medvedeva, Natalia Gennadievna. "Influence of cell environment on micronucleation in Chinese hamster ovary cells." Texas A&M University, 2004. http://hdl.handle.net/1969.1/2790.

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The irradiation of cells in culture is an essential part of many radiation biology experiments. Since these experiments necessarily involve the irradiation of cell culture vessels and nutrient medium, the possibility of effects due to the interactions of irradiated material with growing cells needed to be investigated. In the present study the micronucleus frequency in Chinese hamster ovary (CHO) cells as a function of such parameters as type of radiation, type of cell substrate, changes in cell environment, and time course of the effect were characterized. Observations of the persistence of micronucleus formation in irradiated CHO cells reveal that the number of cells containing micronuclei reaches its maximum within nine hours after irradiation and remain elevated for at least five days. The influence of the cell environment on micronucleus formation in CHO cells was examined by plating cells in preirradiated nutrient medium or on preirradiated cell culture vessels. In all experiments, pre-irradiation of the cell substrate (the culture dish or culture dish filled with medium) led to a significantly higher micronucleus frequency than when cells were plated on un-irradiated substrate. The difference is most pronounced at the lowest doses examined. These results suggest that methods of cell culture vessel sterilization and the composition of cell attachment surfaces could be confounding factors, particularly in the experiments which are intended to examine the response of cells exposed to low doses of ionizing radiation.
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Burford, Neil Thornton. "Cell signalling in Chinese hamster ovary cells expressing recombinant muscarinic receptors." Thesis, University of Leicester, 1994. http://hdl.handle.net/2381/33575.

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Agonist stimulation of recombinant m1, m2, and m3 muscarinic receptors, expressed in Chinese hamster ovary (CHO) cells, was compared. Carbachol binding affinity, and its modification by cations, guanine nucleotides and PTX pretreatment, was compared in washed membrane preparations of each of the CHO cell clones. Functional responses, determined by carbachol stimulation, were: [35S]GTPS binding in membranes; Ins(l,4,5)P3 accumulation in intact cells; 45ca2+ release from permeabilized cells; and cAMP accumulation in intact cells. m2-Transfected CHO cells were found to couple to AC, mediating inhibition of forskolin-stimulated cAMP accumulation, via PTX-sensitive G proteins. After PTX pretreatment of these cells, carbachol mediated a small potentiation of forskolin-stimulated cAMP accumulation, though with a much lower carbachol potency compared with the inhibitory response. m1 and m3-transfected CHO cell clones were found to couple with both PTX-sensitive and PTX-insensitive G proteins, at relatively high levels of receptor expression. The PTX- insensitive G proteins mediated agonist-stimulated PLC activation and were involved in the activation of AC (though at a much lower potency). The mechanism, by which m1, m2 and m3 muscarinic receptors stimulated AC activity was not thought to be due to crosstalk via PLC activity. The level of m3 muscarinic receptor expression, in CHO cells, was found to markedly affect both the potency, and the maximal responsiveness, with which carbachol mediated PLC activation and AC activation. Furthermore, at lower levels of receptor expression, m3 muscarinic receptors appeared to couple to a lesser extent with PTX-sensitive G proteins. The study, therefore, concluded that comparisons of agonist-mediated responses between muscarinic receptor subtypes, expressed in CHO cells, must be performed at similar levels of receptor expression. At similar receptor densities, m1 and m3 muscarinic receptors, in CHO cells, produced very similar responses to carbachol.
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Thompson, Ben C. "Design of transient production systems with Chinese hamster ovary cells." Thesis, University of Sheffield, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.578708.

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Transient protein production by cultured mammalian cells from transfected episomal DNA is frequently used in bioindustry to generate small quantities of candidate therapeutic products during early stages of process development. However, transient production processes typically exhibit low productivity, limiting their use at scale. In this thesis, three distinct but complementary approaches were evaluated for the de novo design of a high productivity scaleable transient production process starting with the discrete raw materials: transfection reagent, Chinese hamster ovary cell line, plasmid DNA and chemically defined medium. (1) Optimisation of CHO host cell transfection: The optimal combination of continuous basal parameters underpinning polyethylenimine (PEI) mediated transfection (relative concentrations of PEI, plasmid DNA and cells) was determined utilising Design of Experiments (DoE) methodology. Optimum transfection conditions were cell line specific - highly dependent upon resistance to PEI cytotoxicity. Comparing different CHO cell hosts operating at their unique optima, variations in specific productivity were limited by the rate of polyplex endocytosis. (2) Modulation of the cell culture environment: Combinations of environmental variables were evaluated using factorial screening to determine an optimal cell culture regime for transient production. For the CHO cells used in this study, the addition of valproic acid, recombinant insulin-like growth factor and a reduced culture temperature were found to interact synergistically to maximise recombinant product yield at an increased cell concentration. (3) Production process design: Utilising response surface modelling to determine key process interactions, transient transfection and medium environment optima were effectively combined to create an intensified, high cell density process exhibiting a five-fold increase in volumetric titre. Combining these approaches, volumetric yield for a transient monoclonal antibody production process was increased from 2 mg L-1 to > 90 mg L-1 - the highest transient volumetric titre achieved with un-genetically modified CHO cells in a chemically defined environment to date.
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Coppen, Steven Russell. "Studies on the aggregation of recombinant Chinese hamster ovary cells." Thesis, University of Kent, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.262373.

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Gounari, F. "DNA methylation and gene-expression in Chinese hamster ovary cells." Thesis, Imperial College London, 1986. http://hdl.handle.net/10044/1/38022.

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Renner, Wolfgang Andreas. "Genetic engineering of the cell cycle regulation of Chinese hamster ovary cells /." [S.l.] : [s.n.], 1995. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=11056.

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Spanos, Jonathon L. "Characterisation of IGFBP-5 protease activity in Chinese hamster ovary cells /." Title page and contents only, 2002. http://web4.library.adelaide.edu.au/theses/09SB/09sbr729.pdf.

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GLASS, JAMES RUSSELL. "POLYAMINE-MEDIATED DEGRADATION OF ORNITHINE DECARBOXYLASE IN CHINESE HAMSTER OVARY CELLS." Diss., The University of Arizona, 1987. http://hdl.handle.net/10150/184002.

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The objective of this research was to identify specific mechanisms involved in the regulation of ornithine decarboxylase, the first enzyme in the polyamine biosynthetic pathway. Immunochemical techniques were used to study post-translational modifications of the ODC protein in relation to activity alterations. Initial experimentation showed that Chinese hamster cells maintained in a defined medium express an ODC protein stable to intracellular degradation. Treatment of these cells with exogenous ornithine or polyamines resulted in a rapid loss of enzyme activity, without detectable changes in the enzyme specific activity. The loss of enzyme activity was a result of accelerated ODC degradation, as determined by immunoprecipitation of pre-labeled protein. In addition, spermidine, but not ornithine, totally inhibited new ODC synthesis. The mechanism of accelerated ODC degradation was investigated and found to occur by an apparent novel mechanism. Degradation of ODC was both ubiquitin-independent and non-lysosomal, and there was also no detectable accumulation of a modified form of ODC protein. In addition, it was found that a component of protein synthesis is required for this process, as inhibitors (cycloheximide, emetine, puromycin) blocked polyamine-accelerated degradation. ODC cDNA was used to synthesize both ODC specific mRNA and protein using in vitro synthesis. These systems may allow the generation of sufficient quantities of material which can be used to recreate in vitro the specific components involved in polyamine inhibition of ODC synthesis and the protease(s) responsible for degradation. The major finding of this work is the direct demonstration that ODC is a stable intracellular protein in the absence of putrescine and spermidine depleted cells (Chapter 2). In addition, that degradation occurs by a novel mechanism, with a requirement for some component of protein synthesis (Chapter 3). Finally, these studies describe the in vitro production of ODC protein and mRNA, which should facilitate further studies of polyamine regulation of ODC degradation and synthesis (Chapter 4).
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Books on the topic "Chinese Hamster Ovary cells"

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Ward, Michael A. Homologous recombination at the APRT locus in Chinese hamster ovary cells. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1992.

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Ang, Cheng Eng. Apoptosis in Chinese hamster ovary duk cell cultures and its implications. Manchester: University of Manchester, 1996.

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O'Beirne, Carole P. Effects of modulators of phosphorylation on P-glycoprotein in multi-drug resistant chinese hamster ovary cells. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1992.

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Anwar, Rashida. The control of heterologous protein production in recombinant Chinese hamster cells. Manchester: University of Manchester, 1994.

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Bulseco, Dylan A. Muscarinic receptor-effector coupling in Chinese hamster ovary cells. 1996.

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Elliott, Elizabeth Margaret. The -tubulin gene family of Chinese hamster ovary cells. 1985.

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Bulseco, Dylan A. Muscarinic receptor-effector coupling in Chinese hamster ovary cells. 1996.

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Wei, Cuihong. Transcriptional regulation of the asparagine synthetase gene in Chinese hamster ovary cells. 1999.

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Barrett, Michael Thomas. Gene amplification of asparagine synthetase in albizziin-resistant Chinese hamster ovary cells. 1993.

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Grant, Stephen. Gene inactivation in cultured Chinese hamster cells. 1986.

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Book chapters on the topic "Chinese Hamster Ovary cells"

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De Leon Gatti, M., K. Wlaschin, A. Rink, A. Sanny, K. S. Tan, P. M. Nissom, P. F. Ong, et al. "Genomic Exploration on Chinese Hamster Ovary Cells." In Animal Cell Technology Meets Genomics, 23–29. Dordrecht: Springer Netherlands, 2004. http://dx.doi.org/10.1007/1-4020-3103-3_3.

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Yamane-Ohnuki, Naoko, Kazuya Yamano, and Mitsuo Satoh. "Biallelic Gene Knockouts in Chinese Hamster Ovary Cells." In Chromosomal Mutagenesis, 1–16. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-232-8_1.

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Rohde, Michael F., Viswanatham Katta, Patricia Derby, and Robert S. Rush. "Characterization of Recombinant Glycoproteins from Chinese Hamster Ovary Cells." In ACS Symposium Series, 408–23. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1995-0619.ch021.

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Davidson, Jeffrey N., and Robert S. Jamison. "Expressing Enzymatic Domains of Hamster CAD in CAD-Deficient Chinese Hamster Ovary Cells." In Purine and Pyrimidine Metabolism in Man VIII, 591–95. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2584-4_123.

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Morris, Arvia E., Chi-Chang Lee, Karmen Hodges, Teri L. Aldrich, Carol Krantz, Pauline S. Smidt, and James N. Thomas. "Expression Augmenting Sequence Element (EASE) Isolated From Chinese Hamster Ovary Cells." In Animal Cell Technology, 529–34. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5404-8_84.

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Thoring, Lena, and Stefan Kubick. "Versatile Cell-Free Protein Synthesis Systems Based on Chinese Hamster Ovary Cells." In Methods in Molecular Biology, 289–308. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8730-6_19.

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Gerber, Mark A., Kimberly A. Lacy, Jennifer Cresswell, Nan Lin, Kevin J. Kayser, and Matthew V. Caple. "Cell Xpress™-Assisted Analysis of Clone Stability in Recombinant Chinese Hamster Ovary Cells." In Cells and Culture, 35–39. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-3419-9_7.

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Bein, Kiflai, and David R. Evans. "de novo Pyrimidine Nucleotide Biosynthesis in Synchronized Chinese Hamster Ovary Cells." In Purine and Pyrimidine Metabolism in Man VIII, 545–48. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2584-4_115.

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Rajendra, Yashas, Sowmya Balasubramanian, and David L. Hacker. "Large-Scale Transient Transfection of Chinese Hamster Ovary Cells in Suspension." In Methods in Molecular Biology, 45–55. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6972-2_3.

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Toshihiro, I. I., Makoto Murakami, Masahiro Mizuguchi, Ken Matsumoto, and Kazukiyo Onodera. "Production of Recombinant Human Thyroid Peroxidase in Chinese Hamster Ovary Cells." In Animal Cell Technology: Developments Towards the 21st Century, 385–89. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0437-1_61.

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Conference papers on the topic "Chinese Hamster Ovary cells"

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Metzger, N. K., P. R. T. Jess, L. Paterson, E. M. Wright, and K. Dholakia. "Optical binding of Chinese hamster ovary cells." In Optics & Photonics 2005, edited by Kishan Dholakia and Gabriel C. Spalding. SPIE, 2005. http://dx.doi.org/10.1117/12.618745.

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Chakraborty, Nilay, Michael A. Menze, Heidi Elmoazzen, Steve C. Hand, and Mehmet Toner. "Choline Chloride Improves the Desiccation Tolerance of Chinese Hamster Ovary Cells." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19606.

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Recently there has been much interest in using sugars such as trehalose to preserve mammalian cells in a dry state as an alternative to cryopreservation (1–5). However, some studies indicate that sugars alone may not be sufficient to prevent cell injury during drying. Other factors like sodium toxicity, ionic imbalance and pH excursions during dehydration are a few of the mechanisms that have been hypothesized to decrease the viability of mammalian cells. In the present study, we investigated whether or not substituting sodium chloride with choline chloride (2-hydroxy-N, N,N-trimethylethanaminium chloride) in the preservation medium improves desiccation tolerance of Chinese Hamster Ovary (CHO) cells.
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Liu, Yagang, Gregory J. Sonek, Curtis F. Chapman, Bruce J. Tromberg, Pasquale Patrizio, Yona Tadir, and Michael W. Berns. "Microthermometry of laser-heated Chinese hamster ovary cells and sperm cells." In Photonics West '95, edited by Steven L. Jacques. SPIE, 1995. http://dx.doi.org/10.1117/12.209917.

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Salimi, Elham, Katrin Braasch, Michael Butler, Douglas J. Thomson, and Greg E. Bridges. "Dielectrophoresis study of electroporation effects on Chinese hamster ovary cells." In 2014 16th International Symposium on Antenna Technology and Applied Electromagnetics (ANTEM). IEEE, 2014. http://dx.doi.org/10.1109/antem.2014.6887659.

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Zettlmeiβl, G., H. Ragg, and H. Karges. "EXPRESSION OF BIOLOGICALLY ACTIVE HUMAN ANTITHROMBIN III IN CHINESE HAMSTER OVARY CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643683.

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Expression of human antithrombin III (AT III) at high levels has been achieved in Chinese hamster ovary (CH0) cells by cotransfection and subsequent coamplification of the transfected sequences. Expression vectors containing the AT III cDNA gene and a dihydrofolate reductase (DHFR) cDNA gene were transfected into CH0 DHFR-deficient cells. About 20% of the DHFR+ transformants secreted recombinant human AT III into the medium. Stepwise selection of the AT III producing DHFR+ -transformants in increasing concentrations of methotrexate generated cells which had amplified the AT III géne. We determined the copy number of the AT III cDNA and the relative amounts of AT III specific mRNA at different stages of the amplification process. Transfected CH0 cell lines expressed elevated immunreactive levels of human AT III.AT III secreted from these cell lines had the same molecular weight (60 kDa), immunological properties and biological activities as AT III obtained from human plasma. In vivo data concerning the inhibition of glycosylation by different drugs suggest that recombinant AT III from CHO cells is glycosylated according to a complex type pattern.
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Khan, Mohammed, Xiaolin Chen, and Jie Xu. "Separation of Non-Viable Chinese Hamster Ovary (CHO) Cells Using Dielectrophoresis in a Deterministic Lateral Displacement Ratchet." In ASME 2020 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2020. http://dx.doi.org/10.1115/imece2020-23520.

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Abstract Chinese hamster ovary (CHO) cell is the most widely used mammalian cell line for commercial production of therapeutic protein. Any presence of non-viable cells in culture medium may adversely affect subsequent functionality of these proteins. Therefore, separation of non-viable cells from suspending medium is critical in biopharmaceutical and biomedical sectors. One such method termed Deterministic Lateral Displacement has already shown promising capabilities in separating cells based on the cell size difference by taking advantage of the predictable flow laminae. However, in cases where size overlaps between viable and non-viable cells are present, separation based solely on size suffers and high-resolution separation techniques are required. Dielectrophoresis, one of the most widely used nonlinear electro-kinetic mechanism, has the potential to manipulate the same size cells depending on the dielectric properties of individual cells. In this work, we demonstrated that a DLD device can be combined with a frequency-based AC electric field to perform high resolution continuous separation of non-viable CHO cells from the viable or productive cells. The behavior of the coupled DLD-DEP device is further investigated by employing numerical simulation to check the effect of geometrical parameters of the DLD arrays, velocities of the flow field and required applied voltages. A moderate row shift fraction with velocity 700μm/s provided a good separation behavior without any trapping. The cell viability was also ensured by maintaining proper electric field which otherwise may cause cell loss due to ion leakage. Our developed numerical model and presented results lay the groundwork for design and fabrication of high resolution DLD-DEP microchips for enhanced separation of viable and nonviable cells.
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Rodaite-Riseviciene, Raminta, Boris Snopok, and Valentinas Snitka. "In situ confocal Raman spectroscopy of single living Chinese hamster ovary cells grown on different substrates." In 2013 IEEE 7th International Conference on Nano/Molecular Medicine and Engnieering (NANOMED). IEEE, 2013. http://dx.doi.org/10.1109/nanomed.2013.6766306.

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WADA, H., M. MURAKOSHI, K. IIDA, S. KUMANO, T. GOMI, K. KIMURA, H. USUKURA, et al. "ATOMIC FORCE MICROSCOPIC IMAGING OF THE INTRACELLULAR MEMBRANE SURFACE OF PRESTIN-EXPRESSING CHINESE HAMSTER OVARY CELLS." In Proceedings of the Ninth International Symposium. WORLD SCIENTIFIC, 2006. http://dx.doi.org/10.1142/9789812773456_0003.

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IIDA, KOJI, MICHIO MURAKOSHI, SHUN KUMANO, KOUHEI TSUMOTO, KATSUHISA IKEDA, IZUMI KUMAGAI, TOSHIMITSU KOBAYASHI, and HIROSHI WADA. "GENERATION OF STABLE CHINESE HAMSTER OVARY CELL LINES EXPRESSING THE MOTOR PROTEIN PRESTIN." In Proceedings of the Final Symposium of the Tohoku University 21st Century Center of Excellence Program. IMPERIAL COLLEGE PRESS, 2006. http://dx.doi.org/10.1142/9781860948800_0010.

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Wasley, Louise C., Andrew J. Dorner, and Randal C. Kaufman. "SYNTHESIS. PROCESSING AND SECRETION OF HUMAN FACTOR VIII IN MAMMALIAN CELLS: REQUIREMENT FOR VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643874.

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In the plasma factor VIII exists as a complex with von Willebrand factor (vWF). The cloning of the cDNA for factor VIII has provided the ability to develop mammalian cell lines which express high levels of factor VIII by using appropriatate expression plasmids and DNA cotransformation with selectable markers. We have studied the synthesis, processing, and secretion of factor VIII expressed in baby hamster kidney cells and in Chinese hamster ovary cells by 35S-methionine pulse and chase labeling and analysis by immunoprecipitation with specific antibodies which recognize the light and heavy chains of factor VIII. In both mammalian cell lines, factor VIII is synthesized as a primary translation product of 230 kDa. A significant amount remains within the endoplasmic reticulum in a stable complex with a glucose regulated protein of 78 kDa. The remainder traverses into the Golgi compartment where it is cleaved to the heavy and light chain forms. Very shortly thereafter the mature factor VIII appears in the conditioned media as the mature heavy and light chain species. Very little single chain factor VIII is secreted into the conditioned media. The accumulation of factor VIII in the conditioned media requires the presence of vWF factor. In the absence of vWF, the factor VIII appears as unassociated heavy and light chains which are rapidly degraded. Bovine, porcine, or human 3WF all effectively stabilize human factor VIII expressed in these rodent cell lines. These results suggest the presence of vWF promotes factor VIII chain association which stabilizes the factor VIII to proteolysis.
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Reports on the topic "Chinese Hamster Ovary cells"

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Holahan, Patricia K., and Martin L. Meltz. Survival of Chinese Hamster Ovary Cells Following Ultrahigh Dose Rate Electron and Bremsstrahlung Radiation. Fort Belvoir, VA: Defense Technical Information Center, April 1990. http://dx.doi.org/10.21236/ada222722.

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Jostes, R. F. Jr, LB Sasser, and R. J. Rausch. TOXICOLOGY STUDIES OF LEWISITE AND SULFUR MUSTARD AGENTS:GENETIC TOXICITY OF LEWISITE (L) IN CHINESE HAMSTER OVARY CELLS. Office of Scientific and Technical Information (OSTI), May 1989. http://dx.doi.org/10.2172/929775.

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Jostes, Jr., R. F., L. B. Sasser, and R. J. Rausch. Toxicology Studies on Lewisite and Sulfur Mustard Agents: Genetic Toxicity of Sulfur Mustard (HD) in Chinese Hamster Ovary Cells Final Report. Office of Scientific and Technical Information (OSTI), May 1989. http://dx.doi.org/10.2172/1086510.

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SRI INTERNATIONAL MENLO PARK CA. LPI845 Liquid Gun Propellant Dermal Toxicity Studies. An Assessment of the LP1846 Utilizing the Mammalian Cell Cytogenetics Assay With Chinese Hamster Ovary (CHO) Cells. Fort Belvoir, VA: Defense Technical Information Center, February 1990. http://dx.doi.org/10.21236/ada238250.

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Yezzi, M. J. Role of protein synthesis in the repair of sublethal x-ray damage in a mutant Chinese hamster ovary cell line. Office of Scientific and Technical Information (OSTI), April 1985. http://dx.doi.org/10.2172/5749675.

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Song, Jian. Test for Chemical Induction of Chromosome Aberrations in Cultured Chinese Hamster Ovary (CHO) Cells with and without Metabolic Activation, Test Article: 3-Nitro-1,2,4-Triazol-5-one (NTO). Fort Belvoir, VA: Defense Technical Information Center, October 2008. http://dx.doi.org/10.21236/ada518834.

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Song, Jian. Test for Chemical Induction of Chromosome Aberration in Cultured Chinese Hamster Ovary (CHO) Cells With and Without Metabolic Activation. Test Article: N,N,N',N'-tetramethyl Ethanediamine (TMEDA). Fort Belvoir, VA: Defense Technical Information Center, June 2008. http://dx.doi.org/10.21236/ada519474.

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