Read and Download eBook Full
Author: Lawanda Schief
Publisher: Page Publishing Inc
Published: 2020-11-08
Total Pages: 162
ISBN-13: 1642148903
DOWNLOAD EBOOKHave you ever wondered how chemicals in the environment affect cancer? Well, this book can give you some scientific insight on how common pesticide chemicals and industrial waste can affect the growth of breast cancer cells.
Author: Kenneth W. McKerns
Publisher: Springer
Published: 1983-06
Total Pages: 296
ISBN-13:
DOWNLOAD EBOOKThe International Foundation for Biochemical Endocrinology is incorporated as a nonprofit research and educational organization. It is dedicated to the dissemination of knowledge, cooperative research programs, and cultural interaction on an international basis. The Foundation is concerned with both basic research and practical applications of biological knowledge to the betterment of humanity. Among our interests are global resource management, human reproduction, hormonal regulation of normal and cancer cells, study of aging and degenerative diseases, brain peptides, peptide neurotransmitter compounds, mechanism of action of hormones, peptide hormone synthesis, and recombinant DNA techniques. This monograph is the ninth sponsored by the Foundation in the Biochemical Endocrinology series. The previous four have been: Hormonally Active Brain Peptides: Structure and Function (1982), K. W. McKerns and V. Pantie, eds.; Reproductive Processes and Contraception (1981), K. W. McKerns, ed.; Synthesis and Release of Adenohypophyseal Hormones (1980), M. Jutisz and K. W. McKerns, eds.; and Structure and Function of the Gonadotropins (1978), K. W. McKerns, ed. These have all been published by Plenum Press.
Author:
Publisher:
Published: 2002
Total Pages: 9
ISBN-13:
DOWNLOAD EBOOKThe estrogen receptor (ER) regulates the expression of genes involved in the growth, proliferation and differentiation of skeletal, cardiovascular, neural and reproductive tissues. A basic scheme for the mechanism for ER action has been developed, but precise details on the interactions between ER and the cellular signaling and transcription machinery required for receptor-mediated regulation of specific target genes are still lacking. We have developed an estrogen responsive system in the fruit fly, Drosophila melanogaster in order to explore the functional interactions between ER and other cellular proteins. Transgenic flies carrying the human ER alpha and an estrogen responsive green fluorescent protein (GFP) reporter gene were constructed. In vivo expression of the GFP reporter gene was observed when larvae were grown on a food source containing steroidal or nonsteroidal estrogens. The induction of the reporter gene by estrogens was blocked upon treatment with tamoxifen, an estrogen antagonist. The polytene chromosomes of Drosophila larval salivary glands will be used to identify transcription cofactors and complexes recruited to an estrogen responsive promoter in vivo.
Author: Richard LeRoy Smith
Publisher:
Published: 2009
Total Pages: 78
ISBN-13:
DOWNLOAD EBOOKEstrogens exert numerous actions throughout the human body, targeting healthy tissue while also enhancing the proliferative capacity of breast cancers. Estrogen signaling is mediated by the estrogen receptor (ER), which binds DNA and ultimately affects the expression of adjacent genes. Current understanding of ER-mediated transcriptional regulation is mostly limited to genes whose transcript levels increase following estrogen exposure, though recent studies demonstrate that direct down-regulation of estrogen-responsive genes is also a significant feature of ER action. We hypothesized that difference in cis-regulatory DNA was a factor in determining target gene expression and performed computational and experimental studies to test this hypothesis. From our in silico analyses, we show that the binding motifs for certain transcription factors are enriched in cis-regulatory sequences adjacent to repressed target genes compared to induced target genes, including the motif for RUNX1. In silico analyses were tested experimentally using dual luciferase reporter assays, which indicate that several ER binding sites are estrogen responsive. Mutagenesis of transcription factor motifs (for ER and RUNX1) reduced the response of reporter gene. Further experiments demonstrated that co-recruitment of ER and RUNX1 is necessary for repression of gene expression at some target genes. These findings highlight a novel interaction between ER and RUNX1 and their role in transcriptional repression in breast cancer.
Author: Ian E. Alexander
Publisher:
Published: 1991
Total Pages: 418
ISBN-13:
DOWNLOAD EBOOKAuthor: Joseph Sin
Publisher:
Published: 2009
Total Pages: 42
ISBN-13:
DOWNLOAD EBOOKProlonged exposure to increased levels of estrogen has been shown to increase the risk of breast cancer. In addition, estrogen has been shown to cause breast cancer cell proliferation. A common form of breast cancer treatment involved selective estrogen receptor modulation. A molecular explanation of how this works is that estrogen regulates and binds to estrogen receptor (ER), a ligand-dependent transcription factor. ER associated with estrogen induces gene transcription by translocating into the nucleus and binding to estrogen response element. ER also recruits cofactor proteins, which results in chromatin remodeling and gene expression regulation through interacting with histone acetylases or transcriptional machinery. Most studies have focused on the study of how ER can activate gene transcription. Recently, ER has been shown to also repress gene transcription. my research has two parts. The first part was to find genes that were down regulated by estrogen in order to increase the data pool of genes down-regulated by estrogen. Four target genes, ARGN, MGC16169, CALML5, and NFIB are suspected to be involved in down-regulation by ER. However, after conducting validation tests, these genes were determined to not be repressed. The second part includes characterizing the specific effects of co-repressors NCoR, NRIP1, and SMRT. Removal of these co-repressors and subsequent effect of their removal on following four ER target sites, HES1, PSCA, SLC35A1, and MME were studied. A knock down of a single co-repressor did not affect the majority of transcriptional activity in ER repressed target genes. A triple knock down was also conducted in hope that removal of multiple co-repressors might affect repression. However, the triple knock down was a failure and future experiments need to be done. Understanding the mechanisms of ER transcriptional repression would significantly aid the creation of effective treatments for breast cancer.
Author:
Publisher:
Published: 2007
Total Pages:
ISBN-13:
DOWNLOAD EBOOKAuthor: Carol Dianne Curtis-Ducey
Publisher:
Published: 2009
Total Pages: 150
ISBN-13: 9781109571592
DOWNLOAD EBOOKInteraction of estrogen receptor alpha (ERalpha) with 17beta-estradiol (E2) facilitates binding of the receptor to estrogen response elements (EREs) in target genes, which in turn leads to recruitment of coregulatory proteins. To better understand how estrogen-responsive genes are regulated, our laboratory identified a number of proteins that associate with the DNA-bound ERalpha. Our studies demonstrate that the nonmetastatic protein 23 homolog 1 (NM23-H1) interacts with ERalpha, increases ERalpha-ERE complex formation, influences ERalpha-mediated transcription and associates with the promoter region of the endogenous estrogen-responsive progesterone receptor (PR) gene. Furthermore, we show that a second protein, Apurinic/apyrimidinic endonuclease 1 or redox factor-1 (Ape1/Ref-1), interacts with ERalpha, promotes the ERalpha-ERE interaction, influences ERalpha-mediated transactivation, and selectively associates with endogenous, estrogen-responsive genes in MCF-7 cells. Our findings suggest that NM23-H1 and Ape1/Ref-1 are instrumental in modulating expression of estrogen-responsive genes. Interestingly, we demonstrate that Ape1/Ref-1 and NM23-H1, as well as the oxidative stress proteins Cu/Zn superoxide dismutase (SOD1), thioredoxin (Trx) and protein disulfide isomerase (PDI) are overexpressed in human breast cancer tissues. These studies provide a novel link between DNA repair, redox regulation and modulation of ERalpha-mediated transcription.
Author: Carol Dianne Curtis-Ducey
Publisher:
Published: 2009
Total Pages:
ISBN-13:
DOWNLOAD EBOOKInteraction of estrogen receptor alpha (ERalpha) with 17beta-estradiol (E2) facilitates binding of the receptor to estrogen response elements (EREs) in target genes, which in turn leads to recruitment of coregulatory proteins. To better understand how estrogen-responsive genes are regulated, our laboratory identified a number of proteins that associate with the DNA-bound ERalpha. Our studies demonstrate that the nonmetastatic protein 23 homolog 1 (NM23-H1) interacts with ERalpha, increases ERalpha-ERE complex formation, influences ERalpha-mediated transcription and associates with the promoter region of the endogenous estrogen-responsive progesterone receptor (PR) gene. Furthermore, we show that a second protein, Apurinic/apyrimidinic endonuclease 1 or redox factor-1 (Ape1/Ref-1), interacts with ERalpha, promotes the ERalpha-ERE interaction, influences ERalpha-mediated transactivation, and selectively associates with endogenous, estrogen-responsive genes in MCF-7 cells. Our findings suggest that NM23-H1 and Ape1/Ref-1 are instrumental in modulating expression of estrogen-responsive genes. Interestingly, we demonstrate that Ape1/Ref-1 and NM23-H1, as well as the oxidative stress proteins Cu/Zn superoxide dismutase (SOD1), thioredoxin (Trx) and protein disulfide isomerase (PDI) are overexpressed in human breast cancer tissues. These studies provide a novel link between DNA repair, redox regulation and modulation of ERalpha-mediated transcription.
Author: Malcolm G. Parker
Publisher:
Published: 1991
Total Pages: 434
ISBN-13:
DOWNLOAD EBOOKAn overview of the supergene family made up of those nuclear hormone receptors which recognize thyroid and steroid hormones, vitamen D and retinoic acid and which are characterized by their ability to bind both ligands and the genes which respond to them.
