2 edition of Transcriptional regulation of the asparagine synthetase gene in Chinese hamster ovary cells. found in the catalog.
Transcriptional regulation of the asparagine synthetase gene in Chinese hamster ovary cells.
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These two systems are well understood. In mamrnalian cells, including Chinese hamster ovary (CHO) cells, the asparagine synthetase (AS) enzymatic activity is up-regulated in response to amino acid starvation.
This indicates a conserved adaptation response. The AS gene of CHO cells has been extensively studied at the biochemical level. It provides a. The expression of asparagine synthetase activity [L-aspartate:ammonia ligase (AMP-forming), EC ] in cultured Chinese hamster ovary (CHO) cells is regulated by asparagine.
transcriptional regulation of the human asparagine synthetase gene by nutrient availability by ione parra barbosa-tessmann a dissertation presented to the graduate school of the university of florida in partial fulfillment of the requirements for the degree of doctor of philosophy university of florida page 2 to my family.
page 3. Transcriptional regulation of the human asparagine synthetase gene by carbohydrate availability Article (PDF Available) in Biochemical Journal (Pt 1)(1) May with 23 Reads. Transcription of the asparagine synthetase (AS) gene is induced by amino acid deprivation.
The present data illustrate that this gene is also under transcriptional control by carbohydrate availability. Incubation of human HepG2 hepatoma cells in glucose-free medium resulted in an increased AS mRNA content, reaching a maximum of about fold over control cells after approx.
12 h. We have studied the regulation of expression of the asparagine synthetase (AS) gene in ts11 cells, a mutant of BHK hamster cells which encodes Transcriptional regulation of the asparagine synthetase gene in Chinese hamster ovary cells. book temperature-sensitive AS and therefore does not produce endogenous asparagine at degrees C.
Incubation of ts11 cells at the nonpermissive temperature drastically increases the level of AS mRNA, and the stimulation of AS mRNA expression. The regulation of asparagine synthetase in wild type Chinese hamster ovary cells and in several mutant strains containing defective aminoacyl-tRNA synthe- tases has been studied.
The Mammalian Asparagine Synthetase Gene. The human ASNS gene, a schema of which is illustrated in Fig. 2 A, was first assigned to chromosome 7 by analyses of somatic cell hybrids ().Greco et al. established that the ASNS locus is derived from the long arm of human chromosome 7, and in situ hybridization mapped the locus more precisely to chromosome region 7q ().
Overlapping cDNAs for Chinese hamster ovary (CHO) asparagine synthetase (AS) were isolated from a library prepared from an AS-overproducing cell line. The sequence was determined and shown to contain an open reading frame encoding a protein of M r 64, The predicted amino acid sequence for the CHO AS enzyme was compared to that of the human.
Andrulis I L, Hatfield G W, Arfin S M. Asparaginyl-tRNA aminoacylation levels and asparagine synthetase expression in cultured Chinese hamster ovary cells. J Biol Chem ; Greco A, Gong S S, Ittman M, Basilico C. Organization and expression of the cell cycle gene, tsl 1, that encodes asparagine synthetase.
Asparaginyl-tRNA aminoacylation levels and asparagine synthetase expression in cultured Chinese hamster ovary cells. J Biol Chem. Nov 10; (21)– Arfin SM, Simpson DR, Chiang CS, Andrulis IL, Hatfield GW.
A role for asparaginyl-tRNA in the regulation of asparagine synthetase in a mammalian cell line. In common with certain other lymphoid neoplasms, cells of the human lymphocytic leukemia lines and are asparagine (ASN) auxotrophs.
Asparagine synthetase (ASY), which is a housekeeping. Asparaginyl-tRNA aminoacylation levels and asparagine synthetase expression in cultured Chinese hamster ovary cells.
J Biol Chem. Nov 10; (21)– Andrulis IL, Shotwell M, Evans-Blackler S, Zalkin H, Siminovitch L, Ray PN. Fine structure analysis of the Chinese hamster AS gene encoding asparagine synthetase. Gene. P. Pohjanpelto, E. HölttäDeprivation of a single amino acid induces protein synthesis-dependent increases in c-Jun, c-myc, and ornithine decarboxylase mRNAs in Chinese hamster ovary cells Molecular and Cellular Biology, 10 (), pp.
2 and 3), and among these is asparagine synthetase (A.S.), 1 which catalyzes the glutamine- and ATP-dependent conversion of aspartic acid to asparagine. Arfin and co-workers (4, 5) showed that starvation of Chinese hamster ovary cells for asparagine decreased the level of asparaginyl-tRNA Asn with a.
Asparagine synthetase (or aspartate-ammonia ligase) is a chiefly cytoplasmic enzyme that generates asparagine from aspartate. This amidation reaction is similar to that promoted by glutamine enzyme is ubiquitous in its distribution in mammalian organs, but basal expression is relatively low in tissues other than the exocrine pancreas.
Chevalier C, Bourgeois E, Just D, Raymond P. Metabolic regulation of asparagine synthetase gene expression in maize (Zea mays L.) root tips.
Plant J. 9: (). Chiyo T, Hongo S, Takeda M. Expression of asparagine synthetase mRNA through asparagine independent signal transduction pathway that might involve protein kinase C in BALB3T3 cells. Regulation of Asparagine Synthetase by Amino Acids. Asparagine synthetase (AS) catalyzes the synthesis of asparagine and glutamate from aspartate, ATP, and glutamine (10).
Arfin et al. (11) demonstrated that incubation of Chinese hamster ovary cells in medium lacking asparagine decreased the aminoacylation of tRNA Asn and increased AS activity. Regulation of Histone Gene Expression in Human Cells DISCUSSION: M.
Adesnik, B. Nelkin, and P. Reczek Amplification of the Metallothionein-I Gene in Cadmium- and Zinc-Resistant Chinese Hamster Ovary Cells DNA Transfer of Bacterial Asparagine Synthetase into Mammalian Cells.
Andrulis IL, Hatfield WG and Arfin SM () Asparaginyl t-RNA aminoacylation levels in asparagine synthetase expression in cultured chinese hamster ovary cells. J Biol Chem. Andrulis IL, Hatfield GW, Arfin SM. Asparaginyl-tRNA aminoacylation levels and asparagine synthetase expression in cultured Chinese hamster ovary cells.
J Biol Chem. Nov 10; (21)– Gong SS, Guerrini L, Basilico C. Regulation of asparagine synthetase gene expression by amino acid starvation.
gene expression in eukaryotic cells. FASEB J.i; 8: Key Words: amino acids. nutrient control transcriptional regula-tion transport asparagine synthetase. ribosomal proteins IN BACTERIA, DEPLETION OF A SINGLE amino acid from the medium leads to increased transcription of genes coding for the enzymes in the corresponding pathway.
The conse. A reduction of asparagine leads to cell death, since exposure to L-asparaginase in vitro induces the fragmentation of DNA and morphological changes typical of apoptosis in a mouse lymphoma cell line 6 and in NIH3T3 cells.
7 An asparagine deficiency can be evoked by the intracellular depletion of glutamate and glutamine. 7 The apoptosis of. Dah H. Ho, Ti Li Loo, in Encyclopedia of Cancer (Second Edition), V Drug Resistance. Resistance to LAS therapy can occur through natural selection of a subpopulation of tumor cells with enhanced asparagine synthetase activity or through reactivation of the asparagine synthetase gene in response to a fall in intracellular asparagine activity.
Another resistance mechanism is the. TFEB and ZKSCAN3 – the master autophagy regulators. Although transcriptional regulators of core mammalian autophagy-related proteins were previously known, the transcriptional regulation by TFEB enables a rapid induction of autophagy-related proteins that are involved in all steps of the process, and its overexpression is sufficient to induce autophagy (Settembre et al., ).
Liao, M. L., and Sunstrom, N. () A transient expression vector for recombinant protein production in Chinese hamster ovary cells, Journal Of Chemical Technology And Biotechnol 82– CrossRef Google Scholar. Mammalian cells have evolved complex cellular responses to changes in environment, including nutrient availability.
The asparagine synthetase gene, ASNS, encoding the enzyme that catalyzes the synthesis of asparagine and glutamate using glutamine and aspartate, is a gene for which transcription is highly regulated by the nutritional status of the cell ().
Mammalian cells are the main tool for the production of therapeutic proteins, viruses for gene therapy, and cells for cell therapy. In production processes cell metabolism is the main driver that causes changes in the growth environment and affects productivity and product quality.
Of all nutrients, glucose has the most prominent impact on bioprocesses. Abstract. Transcription from the human asparagine synthetase (AS) gene is increased in response to either amino acid (amino acid response) or glucose (unfolded protein response) two independent pathways converge on the same set of genomic cis-elements within the AS promoter, which are referred to as nutrient-sensing response element (NSRE)-1 and -2, both of which are.
The regulation of asparagine synthetase (AS) and CHOP expression by AA availability has been studied at the molecular level (Bruhat et al.Guerrini et al. AS is the gene encoding the enzyme responsible for the biosynthesis of asparagine from aspartate and glutamate.
We have previously shown that asparagine synthetase (AS) mRNA expression can be dramatically up-regulated by asparagine deprivation in ts11 cells, mutants of BHK hamster cells which encode a temperature-sensitive AS. The expression of AS mRNA was also induced upon starvation for one of several essential amino acids in HeLa cells.
Regulation of Metabolic Homeostasis in Cell Culture Bioprocesses Conor M. O'Brien,1 Bhanu Chandra Mulukutla,2 Douglas G. Mashek,3 and Wei-Shou Hu1,* Mammalian cells are the main tool for the production of therapeutic proteins, viruses for gene therapy, and cells for cell therapy.
In. Asparagine synthetase (AS) mRNA in Pisum sativum accumulates preferentially in plants grown in the dark. Nuclear run-on experiments demonstrate that expression of both the AS1 and AS2 genes is negatively regulated by light at the level of transcription.
The M19 mutant of Chinese hamster ovary (CHO) cells is deficient in S2P (Hasan et al., ; Rawson et al., ). It was previously shown that M19 cells are unable to induce the expression of ERSE reporter gene or of the major ER chaperone BiP at either mRNA or protein levels in response to ER stress (Lee et al., ).
page 1 1 the amino acid response induces both dynamic changes of histone modifications at the asparagine synthetase gene and regulation of the early growth response 1 gene by mitogen activated protein kinase signaling pathways by mukundh n.
balasu bramanian a dissertation presented to the graduate school of the university of florida in partial fulfillment of the requirements for the degree of. Transcriptional regulation of genes involved in fatty acid metabolism is considered the major long-term regulatory mechanism controlling lipid homeostasis.
By means of this mechanism, transcription factors, nutrients, hormones and epigenetics control not only fatty acid metabolism, but also many metabolic pathways and cellular functions at the molecular level. dPhosphoglycerate dehydrogenase (Phgdh) is a necessary enzyme for de novo l-serine biosynthesis.
Mutations in the human PHGDH cause serine deficiency disorders characterized by severe neurological symptoms including congenital microcephaly and psychomotor retardation.
We showed previously that targeted disruption of Phgdh in mice causes overall growth retardation with. that hypertonic activation of system A in Chinese hamster ovary (CHO-K1) cells, in contrast to its activation by amino acid deprivation, did not involve increased of the human ATA2 transporter gene by amino acid deprivation is different than that for asparagine synthetase.
Thus, in phenylalanine‐deprived hepatoma cells, the transcriptional activity of the hepatocyte nuclear factor‐1 (HNF‐1) decreased, limiting expression of the albumin gene . Another example is brought about by the activation of ATF2 and c‐jun in homocysteine‐treated endothelial cells, stimulating ATF3 gene.
Introduction. Amino acid availability modulates a number of fundamental steps of gene expression, including transcription factor recruitment, mRNA processing, and translation [for a review see ()].Transcription from specific genes is induced following amino acid deprivation of mammalian cells (2– 4) and among these is asparagine synthetase (ASNS) 2.
Regulation of the Asparagine Synthetase (ASNS) Gene by Nutrient Limitation Asparagine synthetase (ASNS) is one of the earliest amino acid responsive genes to be well characterized.
As described in the previous paragraph, an unusually low level of ASNS expression is responsible, though it may not be the only cause, for the selective sensitivity.Reaction mechanism.
CTP (cytidine triphosphate) synthetase catalyzes the last committed step in pyrimidine nucleotide biosynthesis: ATP + UTP + glutamine → ADP + P i + CTP + glutamate. It is the rate-limiting enzyme for the synthesis of cytosine nucleotides from both the de novo and uridine salvage pathways.
The reaction proceeds by the ATP-dependent phosphorylation of UTP on the 4-oxygen.Asparagine synthetase (ASNS) is deemed to be a promising therapeutic target for the treatment of several cancers, but its functional role in human breast cancer is still unknown.
In this study, we employed RNA interference as an efficient tool to silence endogenous ASNS expression in .