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2 edition of Repression of dihydrofolate reductase synthesis during myogenesis found in the catalog.

Repression of dihydrofolate reductase synthesis during myogenesis

Edward Eric Schmidt

Repression of dihydrofolate reductase synthesis during myogenesis

identification and characterization of a transcriptional regulatory mechanism

by Edward Eric Schmidt

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  • 5 Currently reading

Published .
Written in English

    Subjects:
  • Myogenesis.,
  • Genetic regulation.

  • Edition Notes

    Statementby Edward Eric Schmidt.
    The Physical Object
    Pagination225 leaves, bound :
    Number of Pages225
    ID Numbers
    Open LibraryOL15188442M

    Sp1 regulates promoters of epidermal growth factor receptor (FGFR1) [16,89, 92, ], hamster dihydrofolate reductase [43,82], insulin-like growth factor-binding protein 2 [58], insulin-like.   INTRODUCTION. Thymidylate synthase (TS) (EC ) catalyses the reductive methylation of dUMP by meTHF (N 5,methylenetetrahydrofolate) to generate thymidylate (dTMP) and dihydrofolate [].As the reaction is the last step of the sole dTMP de novo synthesis pathway essential for DNA synthesis, and also for cell division and survival, TS is an important enzyme target in .

    This chapter talks about dihydrofolate reductase inhibitors (DHFR), nitroheterocycles (furans), and 8-hydroxyquinolines. Trimethoprim and brodimoprim contain two nitrogen atoms on the pyrimidine ring which are easily protonable according to the pH of environment. Co-trimoxazole is one of the main antibacterial agents for the treatment of uncomplicated cystitis. Repression of the human dihydrofolate reductase gene by a non-coding interfering transcript.

    Targeting plant DIHYDROFOLATE REDUCTASE with antifolates and mechanisms for genetic resistance Maxime G. Corral 1,2, Joel Haywood, Luca H. Stehl1,3, Keith A. Stubbs1, Monika W. Murcha1,2 and Joshua S. Mylne1,2,* 1School of Molecular Sciences, The University of Western Australia, 35 Stirling Highway, Crawley, Perth , Australia, 2The ARC Centre of Excellence in Plant Energy Biology, . folate reductase activity and rates of dihydrofolate reductase synthesis. In addition, a revertant population grown over cell doublings in the absence of methotrexate constitutes a homogeneous population of apparently stable cells with fluo- rescence intensities and dihydrofolate reductase .


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Repression of dihydrofolate reductase synthesis during myogenesis by Edward Eric Schmidt Download PDF EPUB FB2

Repression of dihydrofolate reductase synthesis during myogenesis: identification and characterization of a transcriptional regulatory mechanismCited by: 1. Repression of dihydrofolate reductase synthesis during myogenesis: identification and characterization of a transcriptional regulatory mechanism Author: Schmidt, Edward Eric Created Date: 3/25/ AM.

Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene.

It is found in the q11→q22 region of chromosome 5. Bacterial species possess distinct DHFR enzymes BRENDA: BRENDA entry. Abstract. Dihydrofolate reductase (DHFR) enzyme is preferentially synthesized in proliferative cells.

A mouse muscle cell line resistant to microM methotrexate was developed to investigate the molecular levels at which DHFR is down-regulated during myogenic withdrawal from the cell by: Yuan Lin, Stanton L.

Gerson, in Gene Therapy of Cancer (Third Edition), Dihydrofolate Reductase (DHFR) Dihydrofolate reductase is an enzyme that converts dihydrofolate to tetrahydrofolate and is involved in purines and thymidylate synthesis.

It is encoded by the human DHFR gene. Antifolate drugs, methotrexate (MTX) and trimetrexate, can tightly bind to DHFR and inhibit DNA synthesis.

Dihydrofolate Reductase Assay Kit was obtained from Sigma-Aldrich. The assay was based on the ability of DHFR to catalyze the reversible NADPH-dependent reduction of dihydrofolic acid to tetrahydrofolic acid. The assay systerm contained mM dihydrofolate, mM NADPH, mM KCl and unit rh DHFR in phosphate buffer, pH   Dihydrofolate reductase from Mycobacterium tuberculosis catalyzes the NAD(P)H dependent reduction of dihydrofolate, yielding NAD(P) + and tetrahydrofolate, the primary one carbon unit carrier in biology.

Tetrahydrofolate needs to be recycled so that reactions involved in dTMP synthesis and purine metabolism are maintained. Folates (B9 vitamins) are essential cofactors in one-carbon metabolism. Since C1 transfer reactions are involved in synthesis of nucleic acids, proteins, lipids, and other biomolecules, as well as in epigenetic control, folates are vital for all living organisms.

This work presents a complete study of a plant DHFR-TS (dihydrofolate reductase-thymidylate synthase) gene family that implements. Dihydrofolate reductase is a small enzyme that plays a supporting role, but an essential role, in the building of DNA and other processes.

It manages the state of folate, a snaky organic molecule that shuttles carbon atoms to enzymes that need them in their reactions. Johnson LF, Fuhrman CL, Wiedemann LM.

Regulation of dihydrofolate reductase gene expression in mouse fibroblasts during the transition from the resting to growing state. J Cell Physiol. Dec; 97 (3 Pt 2 Suppl 1)– Mariani BD, Slate DL, Schimke RT. S phase-specific synthesis of dihydrofolate reductase in Chinese hamster ovary cells.

Human dihydrofolate reductase (DHFR) was previously thought to be the only enzyme capable of the reduction of dihydrofolate to tetrahydrofolate; an essential reaction necessary to ensure a continuous supply of biologically active folate. DHFR has been studied extensively from a number of perspectives because of its role in health and disease.

Although the presence of a number of. Folate inhibitors antagonize the synthesis of folic acid and are used for treating bacterial, fungal and protozoal infections. • This antimicrobial drug class includes sulfonamides, dihydrofolate reductase inhibitors and combinations of these two subclasses.

Major indications for the use of folate inhibitor combinations are urinary tract infections, enteric infections caused by susceptible. Characterization of thymidylate synthetase and dihydrofolate reductase from Plasmodium berghei.

International Journal for Parasitology14 (5), DOI: /(84)X. Kamalendu Nath, Edward W. Baptist. Cloning of a yeast dihydrofolate reductase gene in Escherichia coli. Farnham PJ, Means AL. Sequences downstream of the transcription initiation site modulate the activity of the murine dihydrofolate reductase promoter.

Mol Cell Biol. Apr; 10 (4)– [PMC free article] Chen S, Mills L, Perry P, Riddle S, Wobig R, Lown R, Millette RL. Background: Methotrexate targets dihydrofolate reductase (DHFR) and thymidylate synthase (TYMS) to prevent cancer growth, and increases DHFR expression when applied. Results: TYMS resistant to methotrexate inhibits the methotrexate induced increase in DHFR expression.

Conclusion: Thymidine synthesis regulates post-transcriptional expression of DHFR and TYMS. Abstract. Earlier studies showed that administration of MTX to patients leads to an increase in the level of DHFR protein in both normal and leukemic leukocytes as well as in erythrocytes within hours to days.

1,2,3 In vitro studies using a human lymphoblastoid cell line showed that increase in DHFR protein is not transcriptionally mediated but was abolished by cycloheximide treatment. Abstract:Dihydrofolate reductase (DHFR) enzyme catalyzes the reduction of dihydrofolate to tetrahydrofolate using NADPH as a cofactor to restore the reduced folate pools for reactions requiring one carbon transfer.

Folates are required for de novo synthesis of purines and thymidylate, as well as glycine, methionine and serine. Reductase Promoter Activity During Myogenepis. Abstract approved: Gary F. Merrill, Ph.D. The E2F consensus site is found within the promoters of several genes that are preferentially expressed in replicating cells.

An E2F site is located at the transcription start of the dihydrofolate reductase (DHFR) gene promoter and is. that during periods of exponential growth the in- creases in dihydrofolate reductase activity, rate of pro- tein synthesis, and steady state levels of mRNA parallel the general increases in cell volume and protein con- tent associated with normal progression through the.

Repression of Dihydrofolate Reductase Synthesis during Myogenesis: Identification and Characterization of a Transcriptional Regualtory Mechanism: Gary F. Merrill Yung-Jin Chang: PhD: Analysis of Ras Gene Mutations in Rainbow Trout Tumors George S. Bailey: Jiuoing Ji: PhD. Mammalian dihydrofolate reductases can also catalyze the transfer of a hydride ion to the C-7 position of folate in a reaction affording dihydrofolate, thus enabling the utilization of the fully oxidized vitamin from nutritional sources.

Despite its apparent simplicity, on the basis of an extraordinarily large amount of experimental data, the reaction catalyzed by dihydrofolate reductase.the rate of dihydrofolate reductase RNA synthesis could be measured and not the steady state levels.

Santiago et al. () showed that a min pulse gave dihydrofolate reductase transcription rate mea- surements comparable to those obtained using a 5-min pulse.

This rate was also the same as that obtained from transcription reactions.Notably, chicken liver dihydrofolate reductase, which is incapable of binding to T.

spiralis TS mRNA, repressed the translation of TS. Discover the world's research 17+ million members.