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Article ; Online: The role of Niemann-Pick type C2 in zebrafish embryonic development.

Tseng, Wei-Chia / Johnson Escauriza, Ana J / Tsai-Morris, Chon-Hwa / Feldman, Benjamin / Dale, Ryan K / Wassif, Christopher A / Porter, Forbes D

Development (Cambridge, England)

2021 Volume 148, Issue 7

Abstract: Niemann-Pick disease type C (NPC) is a rare, fatal, neurodegenerative lysosomal disease caused by mutations of either NPC1 or NPC2. NPC2 is a soluble lysosomal protein that functions in coordination with NPC1 to efflux cholesterol from the lysosomal ... ...

Abstract	Niemann-Pick disease type C (NPC) is a rare, fatal, neurodegenerative lysosomal disease caused by mutations of either NPC1 or NPC2. NPC2 is a soluble lysosomal protein that functions in coordination with NPC1 to efflux cholesterol from the lysosomal compartment. Mutations of either gene result in the accumulation of unesterified cholesterol and other lipids in the late endosome/lysosome, and reduction of cellular cholesterol bioavailability. Zygotic null npc2m/m zebrafish showed significant unesterified cholesterol accumulation at larval stages, a reduction in body size, and motor and balance defects in adulthood. However, the phenotype at embryonic stages was milder than expected, suggesting a possible role of maternal Npc2 in embryonic development. Maternal-zygotic npc2m/m zebrafish exhibited significant developmental defects, including defective otic vesicle development/absent otoliths, abnormal head/brain development, curved/twisted body axes and no circulating blood cells, and died by 72 hpf. RNA-seq analysis conducted on 30 hpf npc2+/m and MZnpc2m/m embryos revealed a significant reduction in the expression of notch3 and other downstream genes in the Notch signaling pathway, suggesting that impaired Notch3 signaling underlies aspects of the developmental defects observed in MZnpc2m/m zebrafish.
MeSH term(s)	Animals ; Biological Transport ; Cholesterol/metabolism ; Embryonic Development ; Endosomes/metabolism ; Gene Expression Regulation, Developmental ; Larva/anatomy & histology ; Lysosomes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Niemann-Pick Disease, Type C/genetics ; Niemann-Pick Disease, Type C/metabolism ; Receptor, Notch3/genetics ; Receptor, Notch3/metabolism ; Zebrafish/anatomy & histology ; Zebrafish/embryology ; Zebrafish/genetics ; Zebrafish/metabolism ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism
Chemical Substances	Membrane Proteins ; Notch3 protein, zebrafish ; Receptor, Notch3 ; Zebrafish Proteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2021-04-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.194258
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Zs.MG 91: Show issues

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Article ; Online: Targeted knock-in mice with a human mutation in GRTH/DDX25 reveals the essential role of phosphorylated GRTH in spermatid development during spermatogenesis.

Kavarthapu, Raghuveer / Anbazhagan, Rajakumar / Raju, Murugananthkumar / Morris, Chon-Hwa Tsai / Pickel, James / Dufau, Maria L

Human molecular genetics

2019 Volume 28, Issue 15, Page(s) 2561–2572

Abstract: Gonadotropin-regulated testicular RNA helicase (GRTH/DDX25) is a testis specific member of the DEAD-box family of RNA helicases expressed in meiotic and haploid germ cells which plays an essential role in spermatogenesis. There are two species of GRTH ... ...

Abstract	Gonadotropin-regulated testicular RNA helicase (GRTH/DDX25) is a testis specific member of the DEAD-box family of RNA helicases expressed in meiotic and haploid germ cells which plays an essential role in spermatogenesis. There are two species of GRTH the 56 kDa non-phospho and 61 kDa phospho forms. Our early studies revealed a missense mutation (R242H) of GRTH in azoospermic men that when expressed in COS1-cells lack the phospho-form of GRTH. To investigate the role of the phospho-GRTH species in spermatogenesis, we generated a GRTH knock-in (KI) transgenic mice with the R242H mutation. GRTH-KI mice are sterile with reduced testis size, lack sperm with spermatogenic arrest at round spermatid stage and loss of the cytoplasmic phospho-GRTH species. Electron microscopy studies revealed reduction in the size of chromatoid bodies (CB) of round spermatids (RS) and germ cell apoptosis. We observed absence of phospho-GRTH in the CB of RS. Complete loss of chromatin remodeling and related proteins such as TP2, PRM2, TSSK6 and marked reduction of their respective mRNAs and half-lives were observed in GRTH-KI mice. We showed that phospho-GRTH has a role in TP2 translation and revealed its occurrence in a 3' UTR dependent manner. These findings demonstrate the relevance of phospho-GRTH in the structure of the chromatoid body, spermatid development and completion of spermatogenesis and provide an avenue for the development of a male contraceptive.
MeSH term(s)	Animals ; Aspermia/genetics ; Aspermia/metabolism ; Aspermia/physiopathology ; Chromatin Assembly and Disassembly ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; DEAD-box RNA Helicases/physiology ; Gene Expression Regulation ; Infertility, Male/genetics ; Infertility, Male/metabolism ; Infertility, Male/physiopathology ; Male ; Mice ; Mice, Knockout ; Mutation, Missense ; Phosphorylation ; Protamines/genetics ; Protein Processing, Post-Translational ; Protein-Serine-Threonine Kinases/genetics ; Spermatids/metabolism ; Spermatids/pathology ; Spermatids/physiology ; Spermatogenesis
Chemical Substances	Protamines ; protamine 2 ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Tssk6 protein, mouse (EC 2.7.11.1) ; DDX25 protein, human (EC 3.6.1.-) ; Ddx25 protein, mouse (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2019-04-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddz079
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Article ; Online: Elucidation of RNA binding regions of gonadotropin-regulated testicular RNA helicase (GRTH/DDX25) to transcripts of a chromatin remodeling protein essential for spermatogenesis.

Yang, Ruifeng / Tsai-Morris, Chon-Hwa / Kang, Jung Hoon / Dufau, Maria L

Hormone molecular biology and clinical investigation

2015 Volume 22, Issue 3, Page(s) 119–130

Abstract: Background: Gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific member of the DEAD-box family of RNA helicases present in Leydig and germ cells. It is a transport protein of mRNAs from nucleus to cytoplasmic sites and is essential ...

Abstract	Background: Gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific member of the DEAD-box family of RNA helicases present in Leydig and germ cells. It is a transport protein of mRNAs from nucleus to cytoplasmic sites and is essential for posttranscriptional regulation and completion of spermatogenesis. Transition protein 2 (Tp2), which associates with GRTH and is required for spermatid elongation, failed to express in GRTH null mice with impaired mRNA nuclear export. The present study determines GRTH binding motifs/regions that associate with Tp2 mRNA transcripts. Materials and methods: RNA-protein interaction was analyzed using biotin-labeled electrophoretic mobility gel shift assays (EMSA). 3'-biotin-labeled RNA (Tp2) was incubated with mGRTH protein (full length/sequential deletion of specific and conserved RNA helicase motifs of GRTH) expressed from in vitro TNT coupled reticulocyte lysate system. Binding specificity was further elucidated by mutagenesis and antibody supershift analysis. Results: RNA-EMSA revealed that the 3' UTR of Tp2 RNA (127 nt from TGA) was retarded in presence of full length GRTH. Nucleotide sequences downstream of TGA of the Tp2 transcript (1-47 and 78-127 nt) are important for binding to GRTH. Sequential deletions/point mutations in GRTH revealed region(s) of conserved binding motifs of RNA helicases (Ia and V) essential for GRTH binding to Tp2 mRNA. Conclusions: Our studies provide insights into the association of Tp2 expression via binding to the conserved RNA binding motifs of GRTH protein and the basis for understanding GRTH in the regulation of the genes essential for germ cell elongation and completion of spermatogenesis.
MeSH term(s)	3' Untranslated Regions ; Animals ; Chromatin Assembly and Disassembly ; DEAD-box RNA Helicases/metabolism ; Electrophoretic Mobility Shift Assay ; Germ Cells/metabolism ; Mice ; Nuclear Proteins/metabolism ; RNA, Messenger/metabolism ; Spermatogenesis
Chemical Substances	3' Untranslated Regions ; Nuclear Proteins ; RNA, Messenger ; Tnp2 protein, mouse ; Ddx25 protein, mouse (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2015-06
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2536635-X
ISSN	1868-1891 ; 1868-1883
ISSN (online)	1868-1891
ISSN	1868-1883
DOI	10.1515/hmbci-2015-0004
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Article: Relevance of gonadotropin-regulated testicular RNA helicase (GRTH/DDX25) in the structural integrity of the chromatoid body during spermatogenesis.

Sato, Hisashi / Tsai-Morris, Chon-Hwa / Dufau, Maria L

Biochimica et biophysica acta

2010 Volume 1803, Issue 5, Page(s) 534–543

Abstract: Gonadotropin-regulated testicular RNA helicase (GRTH/DDX25), a multifunctional protein and a component of ribonucleoprotein complexes, is essential for the completion of spermatogenesis. We investigated the nuclear/cytoplasmic shuttling of GRTH in germ ... ...

Abstract	Gonadotropin-regulated testicular RNA helicase (GRTH/DDX25), a multifunctional protein and a component of ribonucleoprotein complexes, is essential for the completion of spermatogenesis. We investigated the nuclear/cytoplasmic shuttling of GRTH in germ cells and its impact on the chromatoid body (CB)-a perinuclear organelle viewed as a storage/processing site of mRNAs. GRTH resides in the nucleus, cytoplasm and CB of round spermatids. Treatment of these cells with inhibitors of nuclear export or RNA synthesis caused nuclear retention of GRTH and its absence in the cytoplasm and CB. The nuclear levels of GRTH bound RNA messages were significantly enhanced and major reduction was observed in the cytoplasm. This indicated GRTH main transport function of mRNAs to the cytoplasm and CB. MVH, a germ cell helicase, and MIWI, a component of the RNA-induced-silencing complex (RISC), confined to the CB/cytoplasm, were absent in the CB and accumulated in the cytoplasm upon treatment. This also occurred in spermatids of GRTH-KO mice. The CB changed from lobular-filamentous to a small condensed structure after treatment resembling the CB of GRTH-KO. No interaction of GRTH with MVH or RISC members in both protein and RNA were observed. Besides of participating in the transport of messages of relevant spermatogenic genes, GRTH was found to transport its own message to cytoplasmic sites. Our studies suggest that GRTH through its export/transport function as a component of mRNP is essential to govern the CB structure in spermatids and to maintain systems that may participate in mRNA storage and their processing during spermatogenesis.
MeSH term(s)	Animals ; Blotting, Western ; Cell Nucleus/enzymology ; Chromatids/enzymology ; Chromatids/ultrastructure ; Cytoplasm/enzymology ; DEAD-box RNA Helicases/physiology ; Fluorescent Antibody Technique ; Immunoprecipitation ; Male ; Mice ; Mice, Knockout ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Spermatids/enzymology ; Spermatids/ultrastructure ; Spermatogenesis/physiology ; Testis
Chemical Substances	RNA, Messenger ; Ddx25 protein, mouse (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2010-02-20
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2010.02.004
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Article ; Online: Role of gonadotropin regulated testicular RNA helicase (GRTH/Ddx25) on polysomal associated mRNAs in mouse testis.

Tsai-Morris, Chon-Hwa / Sato, Hisashi / Gutti, Ravi / Dufau, Maria L

PloS one

2012 Volume 7, Issue 3, Page(s) e32470

Abstract: Gonadotropin Regulated Testicular RNA Helicase (GRTH/Ddx25) is a testis-specific multifunctional RNA helicase and an essential post-transcriptional regulator of spermatogenesis. GRTH transports relevant mRNAs from nucleus to cytoplasmic sites of meiotic ... ...

Abstract	Gonadotropin Regulated Testicular RNA Helicase (GRTH/Ddx25) is a testis-specific multifunctional RNA helicase and an essential post-transcriptional regulator of spermatogenesis. GRTH transports relevant mRNAs from nucleus to cytoplasmic sites of meiotic and haploid germ cells and associates with actively translating polyribosomes. It is also a negative regulator of steroidogenesis in Leydig cells. To obtain a genome-wide perspective of GRTH regulated genes, in particularly those associated with polyribosomes, microarray differential gene expression analysis was performed using polysome-bound RNA isolated from testes of wild type (WT) and GRTH KO mice. 792 genes among the entire mouse genome were found to be polysomal GRTH-linked in WT. Among these 186 were down-regulated and 7 up-regulated genes in GRTH null mice. A similar analysis was performed using total RNA extracted from purified germ cell populations to address GRTH action in individual target cells. The down-regulation of known genes concerned with spermatogenesis at polysomal sites in GRTH KO and their association with GRTH in WT coupled with early findings of minor or unchanged total mRNAs and abolition of their protein expression in KO underscore the relevance of GRTH in translation. Ingenuity pathway analysis predicted association of GRTH bound polysome genes with the ubiquitin-proteasome-heat shock protein signaling network pathway and NFκB/TP53/TGFB1 signaling networks were derived from the differentially expressed gene analysis. This study has revealed known and unexplored factors in the genome and regulatory pathways underlying GRTH action in male reproduction.
MeSH term(s)	Animals ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Gene Regulatory Networks ; Leydig Cells/metabolism ; Male ; Mice ; Mice, Knockout ; Models, Genetic ; Polyribosomes/genetics ; Polyribosomes/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Spermatogenesis/genetics ; Testis/cytology ; Testis/growth & development ; Testis/metabolism ; Time Factors
Chemical Substances	RNA, Messenger ; Ddx25 protein, mouse (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2012-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0032470
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Article ; Online: Androgen-induced activation of gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) transcription: essential role of a nonclassical androgen response element half-site.

Villar, Joaquin / Tsai-Morris, Chon-Hwa / Dai, Lisheng / Dufau, Maria L

Molecular and cellular biology

2012 Volume 32, Issue 8, Page(s) 1566–1580

Abstract: GRTH, a testis-specific member of the DEAD-box family of RNA helicases essential for spermatogenesis, is present in Leydig cells (LC) and germ cells. In LC, it exerts an autocrine negative regulation on androgen production induced by gonadotropin. GRTH ... ...

Abstract	GRTH, a testis-specific member of the DEAD-box family of RNA helicases essential for spermatogenesis, is present in Leydig cells (LC) and germ cells. In LC, it exerts an autocrine negative regulation on androgen production induced by gonadotropin. GRTH is transcriptionally upregulated by gonadotropin via cyclic AMP/androgen through androgen receptors (AR). For studies of GRTH regulation by androgen in LC, we utilized in vitro/in vivo models. Androgen-induced GRTH expression was prevented by an AR antagonist. Two putative atypical ARE half-sites are present at bp -200 and -827 (ARE1 and ARE2). Point mutation of ARE2 prevented androgen-induced AR binding/function and upregulation of GRTH transcription. Chromatin immunoprecipitation (ChIP) assays showed recruitment of AR, SRC-1, Med-1, transcription factor IIB (TFIIB), and polymerase II (PolII) to GRTH ARE2 (bp -980/-702) and to the promoter region (bp -80/+63). ChIP3C assays revealed short-range chromosomal looping between AR/ARE2 and the core transcriptional machinery at the promoter. Knockdown of Med-1 and/or SRC-1 demonstrated the presence of a nonproductive complex which included AR, TFIIB, and PolII and the essential role of these coactivators in the transcriptional activation of GRTH. Our findings provide new insights into the molecular mechanism of androgen-regulated transcription in LC.
MeSH term(s)	Androgen Receptor Antagonists/pharmacology ; Androgens/metabolism ; Androgens/pharmacology ; Animals ; Cell Line ; Chromatin ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Leydig Cells/metabolism ; Male ; Mice ; Neurons/metabolism ; Promoter Regions, Genetic ; Receptors, Androgen/metabolism ; Transcriptional Activation/drug effects
Chemical Substances	Androgen Receptor Antagonists ; Androgens ; Chromatin ; Receptors, Androgen ; DDX25 protein, human (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2012-02-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.06002-11
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Zs.A 1666: Show issues

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Article ; Online: Prolactin induces up-regulation of its cognate receptor in breast cancer cells via transcriptional activation of its generic promoter by cross-talk between ERα and STAT5.

Kavarthapu, Raghuveer / Tsai Morris, Chon-Hwa / Dufau, Maria L

Oncotarget

2014 Volume 5, Issue 19, Page(s) 9079–9091

Abstract: Prolactin (PRL) serves a critical role in breast cancer progression via activation of its cognate receptor. These studies reveal up-regulation of PRLR gene expression by PRL in absence of estradiol in MCF-7 and T47D breast cancer cells. PRL/PRLR via ... ...

Abstract	Prolactin (PRL) serves a critical role in breast cancer progression via activation of its cognate receptor. These studies reveal up-regulation of PRLR gene expression by PRL in absence of estradiol in MCF-7 and T47D breast cancer cells. PRL/PRLR via activation of STAT5 that binds a GAS-element in the PRLR gene and the participation of ERα stimulates PRLR transcription/expression. PRL/PRLR induces phosphorylation of ERα through the JAK2/PI3K/MAPK/ERK and JAK2/HER2 activated pathways. The increased recruitment of phospho-ERα, induced by PRL to Sp1 and C/EBPβ at PRLR promoter sites is essential for PRL-induced PRLR transcription. This recruitment is prevented by blockade of PRL expression using RNA interference or ERα phosphorylation using specific inhibitors of PI3K and ERK. Direct evidence is provided for local actions of PRL, independent of estradiol, in the up-regulation of PRLR transcription/expression by an activation-loop between STAT5 and the phospho-ERα/Sp1/C/EBPβ complex with requisite participation of signaling mechanisms. PRL's central role in the up-regulation of PRLR maximizes the action of the endogenous hormone. This study offers mechanistically rational basis for invasiveness fueled by prolactin in refractory states to adjuvant therapies in breast cancer.
MeSH term(s)	Binding Sites/genetics ; Breast Neoplasms/genetics ; Breast Neoplasms/pathology ; CCAAT-Enhancer-Binding Protein-beta/genetics ; CCAAT-Enhancer-Binding Protein-beta/metabolism ; Cell Line, Tumor ; Enzyme Activation ; Estradiol/metabolism ; Estrogen Receptor alpha/genetics ; Estrogen Receptor alpha/metabolism ; Extracellular Signal-Regulated MAP Kinases/antagonists & inhibitors ; Extracellular Signal-Regulated MAP Kinases/genetics ; Female ; Humans ; MAP Kinase Signaling System ; MCF-7 Cells ; Neoplasm Invasiveness/pathology ; Phosphatidylinositol 3-Kinases/genetics ; Phosphoinositide-3 Kinase Inhibitors ; Phosphorylation ; Prolactin/biosynthesis ; Prolactin/genetics ; Promoter Regions, Genetic/genetics ; RNA Interference ; RNA, Small Interfering ; Receptors, Prolactin/genetics ; Receptors, Prolactin/metabolism ; STAT5 Transcription Factor/genetics ; Sp1 Transcription Factor/genetics ; Sp1 Transcription Factor/metabolism ; Transcription, Genetic/genetics ; Tumor Suppressor Proteins/genetics ; Up-Regulation
Chemical Substances	CCAAT-Enhancer-Binding Protein-beta ; CEBPB protein, human ; Estrogen Receptor alpha ; Phosphoinositide-3 Kinase Inhibitors ; RNA, Small Interfering ; Receptors, Prolactin ; STAT5 Transcription Factor ; STAT5A protein, human ; STAT5B protein, human ; Sp1 Transcription Factor ; SP1 protein, human ; Tumor Suppressor Proteins ; Estradiol (4TI98Z838E) ; Prolactin (9002-62-4) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2014-09-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.2376
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Article: Gonadotropin-regulated testicular helicase (GRTH/DDX25): a master post-transcriptional regulator of spermatogenesis.

Dufau, Maria L / Sato, Hisashi / Gutti, Ravi / Tsai-Morris, Chon-Hwa

Advances in experimental medicine and biology

2011 Volume 707, Page(s) 23–29

MeSH term(s)	Animals ; Apoptosis/physiology ; DEAD-box RNA Helicases/metabolism ; DEAD-box RNA Helicases/physiology ; Leydig Cells/metabolism ; Male ; Polymorphism, Genetic ; RNA Processing, Post-Transcriptional/physiology ; Rats ; Spermatogenesis/physiology
Chemical Substances	Ddx25 protein, rat (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2011
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4419-8002-1_6
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Article ; Online: Differences in gonadotropin-regulated testicular helicase (GRTH/DDX25) single nucleotide polymorphism between Japanese and Chinese populations.

Tsai-Morris, Chon-Hwa / Koh, Eitetsu / Dufau, Maria L

Human reproduction (Oxford, England)

2008 Volume 23, Issue 11, Page(s) 2611–2613

MeSH term(s)	Alleles ; Azoospermia/ethnology ; Azoospermia/genetics ; China ; DEAD-box RNA Helicases/genetics ; Exons ; Genetic Variation ; Genotype ; Humans ; Japan ; Male ; Models, Statistical ; Oligospermia/ethnology ; Oligospermia/genetics ; Polymorphism, Single Nucleotide
Chemical Substances	DDX25 protein, human (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2008-11
Publishing country	England
Document type	Comment ; Letter
ZDB-ID	632776-x
ISSN	1460-2350 ; 0268-1161 ; 1477-741X
ISSN (online)	1460-2350
ISSN	0268-1161 ; 1477-741X
DOI	10.1093/humrep/den063
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Zs.B 2892: Show issues

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Article ; Online: Complex formation and interactions between transcription factors essential for human prolactin receptor gene transcription.

Kang, Jung-Hoon / Tsai-Morris, Chon-Hwa / Dufau, Maria L

Molecular and cellular biology

2011 Volume 31, Issue 16, Page(s) 3208–3222

Abstract: The protein association of estrogen receptor α ERα with DNA-bound SP1 and C/EBPβ is essential for the 17β-estradiol (E2)-induced activation of human prolactin receptor (hPRLR) gene transcription. Protein-protein interaction and complex formation at the ... ...

Abstract	The protein association of estrogen receptor α ERα with DNA-bound SP1 and C/EBPβ is essential for the 17β-estradiol (E2)-induced activation of human prolactin receptor (hPRLR) gene transcription. Protein-protein interaction and complex formation at the hPIII promoter of hPRLR was investigated. The basic region and leucine zipper (bZIP) of C/EBPβ, zinc finger (ZF) motifs of SP1, and the DNA binding domain of ERα were identified as regions responsible for the interactions between transfactors. The E2-induced interaction was confirmed by bioluminescence resonance energy transfer (BRET) assays of live cells. The combination of BRET/bimolecular luminescence complementation assay revealed that ERα exists as a constitutive homodimer, and E2 induced a change(s) in ERα homodimer conformation favorable for its association with C/EBPβ and SP1. Chromatin immunoprecipitation and small interfering RNA knockdown of members of the complex in breast cancer cells demonstrated the endogenous recruitment of components of the complex onto the hPIII promoter of the hPRLR gene. SP1 is the preferred transfactor for the recruitment of ERα to the complex that facilitates the C/EBPβ association. The E2/ERα-induced hPRLR transcription was demonstrated in ERα-negative breast cancer cells. This study indicates that the enhanced complex formation of ERα dimer with SP1 and C/EBPβ by E2 has an essential role in the transcriptional activation of the hPRLR gene.
MeSH term(s)	Binding Sites ; Breast Neoplasms/pathology ; CCAAT-Enhancer-Binding Protein-beta/metabolism ; Cell Line, Tumor ; Estradiol/metabolism ; Estradiol/pharmacology ; Female ; Humans ; Multiprotein Complexes/biosynthesis ; Promoter Regions, Genetic ; Protein Multimerization ; Receptors, Prolactin/genetics ; Sp1 Transcription Factor/metabolism ; Transcription Factors/metabolism ; Transcription, Genetic ; Transcriptional Activation
Chemical Substances	CCAAT-Enhancer-Binding Protein-beta ; Multiprotein Complexes ; Receptors, Prolactin ; Sp1 Transcription Factor ; Transcription Factors ; Estradiol (4TI98Z838E)
Language	English
Publishing date	2011-06-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.05337-11
Database	MEDical Literature Analysis and Retrieval System OnLINE

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