Relevant bibliographies by topics / Wnt genes. Wnt proteins

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Academic literature on the topic 'Wnt genes. Wnt proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 February 2022

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Journal articles on the topic "Wnt genes. Wnt proteins"

1

Krauss, S., V. Korzh, A. Fjose, and T. Johansen. "Expression of four zebrafish wnt-related genes during embryogenesis." Development 116, no. 1 (September 1, 1992): 249–59. http://dx.doi.org/10.1242/dev.116.1.249.

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The wnt gene family codes for a group of cysteine-rich, secreted proteins, which are differentially expressed in the developing embryo and are possibly involved in cellular communication. Here, we describe the polymerase chain reaction based cloning and embryonic expression patterns of four zebrafish wnt-related sequences; wnt[a], wnt[b], wnt[c] and wnt[d]. One of these genes, wnt[a], is a potential homologue of murine Wnt-3, while the other three genes most likely represent new members of the vertebrate wnt gene family. In zebrafish embryos, transcripts of wnt[a] are confined to the dorsal diencephalon, the dorsal midbrain, the rhombic lips and the dorsal portions of the spinal cord. wnt[b] is expressed in the tail bud and at considerably lower levels in the mesoderm of the head. wnt[c] transcripts are present within the diencephalon and the posterior midbrain whereas wnt[d] shows a surprisingly similar expression pattern to zebrafish wnt-1. By analogy to wnt-1, it is likely that the members of the zebrafish wnt gene family play an important role in cell-to-cell signalling during pattern formation in the neural tube and the tail bud.
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Caspi, Elanite, and Rina Rosin-Arbesfeld. "A Novel Functional Screen in Human Cells Identifies MOCA as a Negative Regulator of Wnt Signaling." Molecular Biology of the Cell 19, no. 11 (November 2008): 4660–74. http://dx.doi.org/10.1091/mbc.e07-10-1046.

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Aberrant Wnt signal transduction is involved in many human diseases such as cancer and neurodegenerative disorders. The key effector protein of the canonical Wnt pathway is β-catenin, which functions with T-cell factor/lymphoid enhancer factor (TCF/LEF) to activate gene transcription that leads to expression of Wnt target genes. In this study we provide results obtained from a novel functional screen of a human brain cDNA library used to identify 63 genes that are putative negative Wnt regulators. These genes were divided into eight functional groups that include known canonical and noncanonical Wnt pathway components and genes that had not yet been assigned to the Wnt pathway. One of the groups, the presenilin-binding proteins, contains the modifier of cell adhesion (MOCA) gene. We show that MOCA is a novel inhibitor of Wnt/β-catenin signaling. MOCA forms a complex with β-catenin and inhibits transcription of known Wnt target genes. Epistasis experiments indicate that MOCA acts to reduce the levels of nuclear β-catenin, increase the levels of membrane-bound β-catenin, and enhances cell–cell adhesion. Therefore, our data indicate that MOCA is a novel Wnt negative regulator and demonstrate that this screening approach can be a rapid means for isolation of new Wnt regulators.
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Khan, Naveed I., Kenneth Francis Bradstock, and Linda J. Bendall. "The Wnt Pathway Modulates Expression of Growth and Survival Genes in Acute Lymphoblastic Leukemia Cells." Blood 108, no. 11 (November 16, 2006): 1850. http://dx.doi.org/10.1182/blood.v108.11.1850.1850.

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Abstract Wnt proteins are important bone marrow-derived growth factors known to support normal hematopoietic progenitor and stem cell development. Here we report that B cell progenitor acute lymphoblastic leukemia (pre-B ALL) cells express Wnt proteins, including Wnt-2b in 33%, Wnt-5a in 42%, Wnt-10b in 58% and Wnt-16b in 25% of cases. The Wnt receptors, Frizzled (Fz)-7 and -8 were also expressed in most cases while Fz-3, -4 and -9 were occasionally detected. Stimulation of pre-B ALL cells with Wnt-3a activated canonical Wnt signaling with increased expression and nuclear translocation of β-catenin. This resulted in a 1.7 to 5.3-fold increase in cell proliferation, which was associated with enhanced cell cycle entry. Wnt-3a also significantly increased the survival of pre-B ALL cells under conditions of serum deprivation. To determine the mechanisms involved we examined the effects of Wnt-3a on gene expression using the leukemic pre-B ALL cell line NALM6 and a cancer specific microarray (GEArray® OHS-802), which contains 440 known cancer genes. Expression of 83 genes (19%) could be detected on the array. Exposure to Wnt-3a for 24 hours resulted in increased (>1.5 fold) expression of 29 genes and reduced (<50% of control) expression of 3 genes. The most highly regulated genes in response to Wnt-3a were MYBL2, E2F1, CD10, VDAC1, CDC25B (upregulated) and TRAIL-R2 (downregulated). Using qRT-PCR, we confirmed regulation of these genes in NALM6 cells and/or in another leukemic cell line LK63. These genes play important roles in the control of cell cycle (MYBL2, E2F1 and CDC25B), apoptosis (VDAC1 and TRAIL-R2) and motility (CD10) in cancer cells. Our results suggest that Wnt signalling regulates cell growth and proliferation in leukemic cells by modulating the expression of a number of genes. To our knowledge this is the first study examining the gene expression profile following Wnt stimulation in leukemic cells and potentially identifies new therapeutic targets for treatment.
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Gerlach, Jan P., Ingrid Jordens, Daniele V. F. Tauriello, Ineke van ‘t Land-Kuper, Jeroen M. Bugter, Ivar Noordstra, Johanneke van der Kooij, et al. "TMEM59 potentiates Wnt signaling by promoting signalosome formation." Proceedings of the National Academy of Sciences 115, no. 17 (April 9, 2018): E3996—E4005. http://dx.doi.org/10.1073/pnas.1721321115.

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Wnt/β-catenin signaling controls development and adult tissue homeostasis by regulating cell proliferation and cell fate decisions. Wnt binding to its receptors Frizzled (FZD) and low-density lipoprotein-related 6 (LRP6) at the cell surface initiates a signaling cascade that leads to the transcription of Wnt target genes. Upon Wnt binding, the receptors assemble into large complexes called signalosomes that provide a platform for interactions with downstream effector proteins. The molecular basis of signalosome formation and regulation remains elusive, largely due to the lack of tools to analyze its endogenous components. Here, we use internally tagged Wnt3a proteins to isolate and characterize activated, endogenous Wnt receptor complexes by mass spectrometry-based proteomics. We identify the single-span membrane protein TMEM59 as an interactor of FZD and LRP6 and a positive regulator of Wnt signaling. Mechanistically, TMEM59 promotes the formation of multimeric Wnt–FZD assemblies via intramembrane interactions. Subsequently, these Wnt–FZD–TMEM59 clusters merge with LRP6 to form mature Wnt signalosomes. We conclude that the assembly of multiprotein Wnt signalosomes proceeds along well-ordered steps that involve regulated intramembrane interactions.
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Wöhrle, Simon, Britta Wallmen, and Andreas Hecht. "Differential Control of Wnt Target Genes Involves Epigenetic Mechanisms and Selective Promoter Occupancy by T-Cell Factors." Molecular and Cellular Biology 27, no. 23 (October 8, 2007): 8164–77. http://dx.doi.org/10.1128/mcb.00555-07.

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ABSTRACT Canonical Wnt signaling and its nuclear effectors, β-catenin and the family of T-cell factor (TCF) DNA-binding proteins, belong to the small number of regulatory systems which are repeatedly used for context-dependent control of distinct genetic programs. The apparent ability to elicit a large variety of transcriptional responses necessitates that β-catenin and TCFs distinguish precisely between genes to be activated and genes to remain silent in a specific context. How this is achieved is unclear. Here, we examined patterns of Wnt target gene activation and promoter occupancy by TCFs in different mouse cell culture models. Remarkably, within a given cell type only Wnt-responsive promoters are bound by specific subsets of TCFs, whereas nonresponsive Wnt target promoters remain unoccupied. Wnt-responsive, TCF-bound states correlate with DNA hypomethylation, histone H3 hyperacetylation, and H3K4 trimethylation. Inactive, nonresponsive promoter chromatin shows DNA hypermethylation, is devoid of active histone marks, and additionally can show repressive H3K27 trimethylation. Furthermore, chromatin structural states appear to be independent of Wnt pathway activity. Apparently, cell-type-specific regulation of Wnt target genes comprises multilayered control systems. These involve epigenetic modifications of promoter chromatin and differential promoter occupancy by functionally distinct TCF proteins, which together determine susceptibility to Wnt signaling.
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Eisenberg, Leonard M., and Carol A. Eisenberg. "Evaluating the Role of Wnt Signal Transduction in Promoting the Development of the Heart." Scientific World JOURNAL 7 (2007): 161–76. http://dx.doi.org/10.1100/tsw.2007.71.

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Wnts are a family of secreted signaling proteins that are encoded by 19 distinct genes in the vertebrate genome. These molecules initiate several signal transduction pathways: the canonical Wnt, Wnt/Ca2+, and Wnt/planar cell polarity pathways. Wnt proteins have major impact on embryonic development, tumor progression, and stem cell differentiation. Wnt signal transduction also influences the formation of the heart, yet many issues concerning the involvement of Wnt regulation in initiating cardiac development remain unresolved. In this review, we will examine the published record to discern (a) what has been shown by experimental studies on the participation of Wnt signaling in cardiogenesis, and (b) what are the important questions that need to be addressed to understand the importance and function of Wnt signal transduction in facilitating the development of the heart.
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Zhang, Shu, Tolga Çagatay, Manami Amanai, Mei Zhang, Janine Kline, Diego H. Castrillon, Raheela Ashfaq, Orhan K. Öz, and Keith A. Wharton. "Viable Mice with Compound Mutations in the Wnt/Dvl Pathway Antagonists nkd1 and nkd2." Molecular and Cellular Biology 27, no. 12 (April 16, 2007): 4454–64. http://dx.doi.org/10.1128/mcb.00133-07.

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ABSTRACT Gradients of Wnt/β-catenin signaling coordinate development and physiological homeostasis in metazoan animals. Proper embryonic development of the fruit fly Drosophila melanogaster requires the Naked cuticle (Nkd) protein to attenuate a gradient of Wnt/β-catenin signaling across each segmental anlage. Nkd inhibits Wnt signaling by binding the intracellular protein Dishevelled (Dsh). Mice and humans have two nkd homologs, nkd1 and nkd2, whose encoded proteins can bind Dsh homologs (the Dvl proteins) and inhibit Wnt signaling. To determine whether nkd genes are necessary for murine development, we replaced nkd exons that encode Dvl-binding sequences with IRES-lacZ/neomycin cassettes. Mutants homozygous for each nkd lacZ allele are viable with slightly reduced mean litter sizes. Surprisingly, double-knockout mice are viable, with subtle alterations in cranial bone morphology that are reminiscent of mutation in another Wnt/β-catenin antagonist, axin2. Our data show that nkd function in the mouse is dispensable for embryonic development.
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Ploper, Diego, Vincent F. Taelman, Lidia Robert, Brian S. Perez, Björn Titz, Hsiao-Wang Chen, Thomas G. Graeber, Erika von Euw, Antoni Ribas, and Edward M. De Robertis. "MITF drives endolysosomal biogenesis and potentiates Wnt signaling in melanoma cells." Proceedings of the National Academy of Sciences 112, no. 5 (January 20, 2015): E420—E429. http://dx.doi.org/10.1073/pnas.1424576112.

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Canonical Wnt signaling plays an important role in development and disease, regulating transcription of target genes and stabilizing many proteins phosphorylated by glycogen synthase kinase 3 (GSK3). We observed that the MiT family of transcription factors, which includes the melanoma oncogene MITF (micropthalmia-associated transcription factor) and the lysosomal master regulator TFEB, had the highest phylogenetic conservation of three consecutive putative GSK3 phosphorylation sites in animal proteomes. This finding prompted us to examine the relationship between MITF, endolysosomal biogenesis, and Wnt signaling. Here we report that MITF expression levels correlated with the expression of a large subset of lysosomal genes in melanoma cell lines. MITF expression in the tetracycline-inducible C32 melanoma model caused a marked increase in vesicular structures, and increased expression of late endosomal proteins, such as Rab7, LAMP1, and CD63. These late endosomes were not functional lysosomes as they were less active in proteolysis, yet were able to concentrate Axin1, phospho-LRP6, phospho-β-catenin, and GSK3 in the presence of Wnt ligands. This relocalization significantly enhanced Wnt signaling by increasing the number of multivesicular bodies into which the Wnt signalosome/destruction complex becomes localized upon Wnt signaling. We also show that the MITF protein was stabilized by Wnt signaling, through the novel C-terminal GSK3 phosphorylations identified here. MITF stabilization caused an increase in multivesicular body biosynthesis, which in turn increased Wnt signaling, generating a positive-feedback loop that may function during the proliferative stages of melanoma. The results underscore the importance of misregulated endolysosomal biogenesis in Wnt signaling and cancer.
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Ye, Mittag, Schmidt, Simm, Horstkorte, and Huber. "Wnt Glycation Inhibits Canonical Signaling." Cells 8, no. 11 (October 25, 2019): 1320. http://dx.doi.org/10.3390/cells8111320.

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Glycation occurs as a non-enzymatic reaction between amino and thiol groups of proteins, lipids, and nucleotides with reducing sugars or -dicarbonyl metabolites. The chemical reaction underlying is the Maillard reaction leading to the formation of a heterogeneous group of compounds named advanced glycation end products (AGEs). Deleterious effects have been observed to accompany glycation such as alterations of protein structure and function resulting in crosslinking and accumulation of insoluble protein aggregates. A substantial body of evidence associates glycation with aging. Wnt signaling plays a fundamental role in stem cell biology as well as in regeneration and repair mechanisms. Emerging evidence implicates that changes in Wnt/-catenin pathway activity contribute to the aging process. Here, we investigated the effect of glycation of Wnt3a on its signaling activity. Methods: Glycation was induced by treatment of Wnt3a-conditioned medium (CM) with glyoxal (GO). Effects on Wnt3a signaling activity were analyzed by Topflash/Fopflash reporter gene assay, co-immunoprecipitation, and quantitative RT-PCR. Results: Our data show that GO-treatment results in glycation of Wnt3a. Glycated Wnt3a suppresses -catenin transcriptional activity in reporter gene assays, reduced binding of -catenin to T-cell factor 4 (TCF-4) and extenuated transcription of Wnt/-catenin target genes. Conclusions: GO-induced glycation impairs Wnt3a signaling function.
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Blache, Philippe, Marc van de Wetering, Isabelle Duluc, Claire Domon, Philippe Berta, Jean-Noël Freund, Hans Clevers, and Philippe Jay. "SOX9 is an intestine crypt transcription factor, is regulated by the Wnt pathway, and represses the CDX2 and MUC2 genes." Journal of Cell Biology 166, no. 1 (July 5, 2004): 37–47. http://dx.doi.org/10.1083/jcb.200311021.

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TCF and SOX proteins belong to the high mobility group box transcription factor family. Whereas TCFs, the transcriptional effectors of the Wnt pathway, have been widely implicated in the development, homeostasis and disease of the intestine epithelium, little is known about the function of the SOX proteins in this tissue. Here, we identified SOX9 in a SOX expression screening in the mouse fetal intestine. We report that the SOX9 protein is expressed in the intestinal epithelium in a pattern characteristic of Wnt targets. We provide in vitro and in vivo evidence that a bipartite β-catenin/TCF4 transcription factor, the effector of the Wnt signaling pathway, is required for SOX9 expression in epithelial cells. Finally, in colon epithelium-derived cells, SOX9 transcriptionally represses the CDX2 and MUC2 genes, normally expressed in the mature villus cells of the intestinal epithelium, and may therefore contribute to the Wnt-dependent maintenance of a progenitor cell phenotype.
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Dissertations / Theses on the topic "Wnt genes. Wnt proteins"

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Nambiar, Roopa. "Zebrafish hdac1 reciprocally regulates the canonical and non-canonical Wnt pathways." Columbus, Ohio : Ohio State University, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1150313622.

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Chow, Hei-man, and 周熙文. "Hormonal, chemical, and transcriptional regulations of Wnt/{221}-catenin signaling in mammary carcinogensis." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2010. http://hub.hku.hk/bib/B4589100X.

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Ng, Chun-laam, and 吳圳嵐. "Wnt inhibitory factor 1 (Wif-1) coordinates Shh and Wnt signaling activities in urorectal development." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hub.hku.hk/bib/B48329629.

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In vertebrates, the urogenital sinus and the hindgut are connected at a hollow region called cloaca. A midline mesenchymal structure known as urorectal septum (urs) descends from the ventral body wall to separate the urogenital sinus from the hindgut before the formation of an anal opening. Subsequent cloaca membrane regression at the ventral midline of the genital tubercle (GT) is crucial for the formation of an anal opening. These two events are important during cloaca septation in urorectal development. Mice with defective Shh or Wnt signaling displayed similar urorectal defects such as GT agenesis, un-partitioned cloaca (persistent cloaca) and proximal urethral opening that are attributable to increased cell apoptosis. Furthermore, Shh and Wnt signal transduction coordinate with each other and regulate cell survival of the developing urorectum. However, the molecular mechanisms by which these two signaling pathways coordinate in urorectal development remain unclear. We previously identified Wnt inhibitory factor1 (Wif1) from Affymetrix array analysis for genes/pathways that is implicated in urorectal development. Wif1 is a secreted protein that binds directly to Wnt ligands preventing Wnts from binding to receptors. This leads to -catenin degradation and thereby inhibits their activities. It is known that Wif1 binds to Wnt3a and Wnt5a with high affinity and deletion of Wnt3a, Wnt5a and -catenin in mice caused GT agenesis, persistent cloaca and proximal hypospadias. Using ETU-induced anorectal malformations model, I found out that Wif1 is ectopically expressed in the un-tubularized and un-septated urorectum. Wif1 is mainly expressed at the fusing endoderm that associates with programmed cell death during cloaca septation. Exogenous addition of Wif1 protein in urorectum culture also caused cloaca membrane disintegration, and proximal urethral opening that may be due to aberrant apoptosis. Shh and Wif1 are differentially expressed at the cloaca endoderm. In normal mice, Shh is highly expressed at the cloaca endoderm except those Wif1-expressing endodermal cells. Blockage of Shh pathway by cyclopamine in urorectum culture induced ectopic expression of Wif1, concomitant with genital tubercle hypoplasia and un-septated cloaca. More importantly, deletion of Shh in mice hastened Wif1 expression at the cloaca membrane endoderm and elicited increased cell death in the Wif1 expressing endoderm. Wif1-/- embryos display urorectal defects including delayed genital outgrowth and proximal hypospadias. Therefore, disruption of spatiotemporal expression of Wif1 could lead to defective Wnt signaling and contributes to abnormal urorectal development in Shh-/- mutant. Current study revealed that Wif1 is involved in urorectal development and is implicated in urorectal defects. It may function as a pro-apoptotic factor to regulate endodermal cell death which is essential for the septation process. Its specific expression is restricted at the midline cloaca endoderm by Shh signaling to inhibit local Wnt--catenin activities during cloaca septation. I proposed novel hypothetical models to explain (1) the significance of the tempo-spatial expression of Wif1; (2) the significance of cell death; and (3) the molecular mechanism that Shh signaling regulates Wnt signaling activities through Wif1 in urorectal development.
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Surgery
Doctoral
Doctor of Philosophy
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4

Ho, Sze-hang, and 何思恆. "Differential expression of Wnt inhibitors Dickkopf-1 (Dkk-1) and Wnt inhibitory factor-1 (Wif1) in the regulation of urorectal development." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2014. http://hdl.handle.net/10722/207999.

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In mammals, the external genitalia, urinary tract and anorectal tract are developed from a common embryonic primordium, the urorectum. Cloaca is the hollow space inside the urorectum that connects the hindgut and the urogenital sinus. During the urorectal development, the external genitalia is formed from the outgrowth of genital tubercle (GT) protruding from the urorectum, while the future urinary tract and anorectal tract are formed by the partition of cloaca during cloacal septation. GT outgrowth and cloacal septation are important developmental events for the formation of genitourinary and anorectal system. In human, dysregulation of these developmental events results in congenital anorectal malformations (ARM). Wnt signaling is one of the key signaling pathways that regulates urorectal development. The activity of Wnt signaling is initiated by the binding of Wnt ligands to cell surface receptors, which can be antagonized by secretory Wnt inhibitors. Dickkopf1 (Dkk1) and Wnt inhibitory factor 1 (Wif1) are secretory Wnt inhibitors implicated in urorectal development. However, the functions of other secretory Wnt inhibitors during urorectal developments remain to be elucidated. In this study, expression analyses showed that Dkk1, Dickkopf2 (Dkk2), Dickkopf4 (Dkk4), Secreted Frizzled-related Protein 1 (Sfrp1) and Wif1 were expressed in the developing urorectum. The dynamic, overlapping and restricted expression patterns of these Wnt inhibitors were closely associated with the GT outgrowth and the cloacal septation events, implying that these Wnt inhibitors functioned in a coordinated manner in defining the field of Wnt signaling activities in the developing urorectum. Wif1 knockout mice (〖Wif1〗^(-/-)) was used as the model to investigate the functions of and the interplay between secretory Wnt inhibitors in urorectal development. GT outgrowth and cloacal septation defects were observed in 〖Wif1〗^(-/-) embryos. Most of the 〖Wif1〗^(-/-) embryos displayed varying degrees of GT outgrowth defects, while septation defects were only occasionally observed. This suggested that GT outgrowth and cloacal septation were regulated by Wif1 via different regulatory mechanisms. In the urorectum of 〖Wif1〗^(-/-) embryos, Dkk1 was significantly upregulated in the peri-cloacal mesenchyme. Further expression analysis suggested that Dkk1 was sufficient to rescue cloacal septation defects but not GT outgrowth defects in 〖Wif1〗^(-/-)embryos. In the 〖Wif1〗^(-/-) embryos with severe GT outgrowth defects, the Fgf8-expressing distal urethral epithelium, the signaling center in the urorectum, was absent, suggesting that the GT outgrowth defects could be contributed by the loss of dUE-expressing signals such as Fgf8. This study demonstrated the importance of secretory Wnt inhibitors in the GT outgrowth and cloacal septation and suggested that secretory Wnt inhibitors played partially overlapping roles in urorectal development. A rescue mechanism for cloacal septation performed by Dkk1 upon Wif1 deletion was proposed. Such auto-regulatory mechanism within the Wnt signaling pathway indicated that Wnt inhibitors play essential regulatory roles in the urorectal development and a balanced Wnt signaling activity modulated by Wnt inhibitors is crucial to the development of urorectum.
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Surgery
Master
Master of Philosophy
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5

Kwan, Hoi-tung, and 關愷彤. "AMPK activators inhibit cervical cancer cell growth through reduction of Dvl3 in Wnt/{221}-catenin signaling." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B46936087.

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Yang, Xuesong, and 楊雪松. "Identification of epigenetic biomarkers for diagnosis of nasopharyngeal carcinoma and determination of WIF1 functional relevance." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2014. http://hdl.handle.net/10722/209492.

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Nasopharyngeal carcinoma (NPC) is closely associated with Epstein-Barr Virus (EBV).Early diagnosis of NPC will improve the overall survival. However, traditional EBV markers do not perform well in high-risk individuals or for early detection of NPC. Aberrant promoter hypermethylation of tumor suppressor genes (TSGs) is an important epigenetic change in early tumorigenesis. This study identified a promising panel of methylation markers for early detection of NPC and assessed the clinical usefulness of these markers using nasopharyngeal (NP) brushing and blood specimens. Methylation-sensitive high resolution melting (MS-HRM) assays were carried out to assess the methylation status of a selected panel of four TSGs (RASSF1A, WIF1, DAPK1, RAR2)in biopsies, NP brushings and cell-free plasma from NPC patients. NP brushing and blood samples from high-risk and cancer-free groups were used as controls. The DNA methylation panel showed higher sensitivity and specificity than the EBV DNA markerincell-free plasma for early stage (Iand II) NPC (sensitivity: 64.6% vs. 51.2% and specificity: 96.0% vs. 88.0%, respectively). In combination with plasma EBV DNA, testing for DNA methylation in plasma and NP brushings using the four-gene MS-HRM test significantly increased the detection rate for all stages of NPC(94.1% for stages I-II, 98.4% for stages III-IV) as well as recurrence(93.5%). Aberrant activation of the Wnt signaling pathway is a common mechanism for cell transformation and tumor development in a variety of human cancers. A high frequency of promoter hypermethylation of WIF1was observed in NPC cell lines (100%), primary tumor biopsies(89.7%), NP brushings (80.2%), and cell-free plasma (51.8%),with no significant correlation with NPC stage. Simultaneously, expression of WIF1 was completely silenced in NPC cell lines (HONE1, HK1, HNE1, SUNE1, CNE1, CNE2, and C666),but not in immortalized NP epithelial cells (NP460 and NP69). These together suggested an important role of WIF1 in NPC development. In vitro and in vivo functional assays revealed a tumor suppressive role of WIF1in NPC. Restoration of WIF1expression in NPC cells significantly suppressed anchorage-independent growth, in vivo tumorigenicity, invasion, migration, and angiogenesis of NPC cells. A number of important angiogenesis-related genes were down-regulated by WIF1expression, including IL6,IL8,VEGF165,VEGFA, PDGFB, and MCP1. There is inhibition of the Wnt/β-catenin signaling pathway, manifested as decreased β-catenin expression and TCF/LEF Wnt promoter activity. These data indicated the important regulatory role of Wnt signaling pathway in NPC tumorigenicity, invasion, migration, and angiogenesis, by interacting with the complex signaling network in NPC cells. To conclude, the MS-HRM assay on the selected gene panel in combination with the EBV DNA test, increases the sensitivity for NPC detection at an early stage and detection of recurrence and has great potential to become a non-invasive test for early diagnosis and disease monitoring after treatment. Collectively, results from this study reveal that WIF1is not only a sensitive biomarker, but also a tumor suppressor gene in NPC. Understanding the molecular regulatory role ofWIF1in NPC will facilitate the diagnosis of NPC, and development of novel NPC therapeutic strategy.
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Clinical Oncology
Doctoral
Doctor of Philosophy
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7

Wong, Yin-chi Betty. "Significance of LRP6 coreceptor upregulation in the aberrant activation of Wnt signaling in hepatocellular carcinoma." Click to view the E-thesis via HKUTO, 2008. http://sunzi.lib.hku.hk/hkuto/record/B41757865.

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8

Chan, Lai Sheung. "Therapeutic potential of a Wnt modulator ICG-001 on nasopharyngeal carcinoma." HKBU Institutional Repository, 2017. https://repository.hkbu.edu.hk/etd_oa/410.

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According to the cancer stem cells (CSCs) hypothesis, CSCs are responsible for the treatment failures. CSCs are a subset of cells possessing stemness properties within the heterogeneous tumor mass. Therapeutic intervention on Wnt signaling is of our great interest because an aberrant Wnt signaling is an important driver to maintain the potency of CSCs. In nasopharyngeal carcinoma (NPC), deregulated expression of the Wnt signaling components is frequently observed. ICG-001 is a selective Wnt modulator (CBP antagonist) that specifically interrupts the interaction between β-catenin and CBP, thereby encourages the interaction between β-catenin and p300 and the subsequent differentiation and reduction of the CSCs subset. For this reason, the present study aimed to evaluate the therapeutic potential of ICG-001 in NPC. Results showed that ICG-001 inhibited both the migration of the NPC cells and the formation of tumor spheres. In the first part of the mechanistic studies (Chapter 3), ICG-001 was found to restore the expression of miR-150 in NPC cells. MiR-150 was further found to directly reduce CD44 expression and inhibit NPC cell migration. In the second part of the mechanistic studies (Chapter 4), ICG-001 was found to reduce the expression of Evi1 in NPC cells. The effect was accompanied with the inhibition of both the NPC cells migration and the tumor spheres formation. Two molecular axes, namely miR-96/Evi1/miR-449a and survivin/Evi1/miR-449a, were found to be involved in the inhibition of the tumor cell migration and spheroids formation. The therapeutic potential of using this CBP antagonist (ICG-001) in NPC, namely the in vitro and in vivo efficacy of ICG-001 combined with cisplatin, was examined (Chapter 5). Concurrent treatment of ICG-001 and cisplatin exhibited a synergistic inhibition on the in vitro growth and the tumor sphere forming capacity of NPC cells as well as the growth of NPC xenografts. Taken together, results presented in this thesis suggested that ICG-001 (PRI-724 is the analog of ICG-001 currently used in clinical trials) has a therapeutic potential in NPC.
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9

Chamorro, Mario Narciso. "Characterization of different aspects of Wnt signaling : in human and mouse tumors /." Access full-text from WCMC, 2009. http://proquest.umi.com/pqdweb?did=1619205751&sid=2&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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10

Brown, Jeffrey D. "Mechanisms and functions of Wnt signaling in Xenopus development /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/5013.

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Books on the topic "Wnt genes. Wnt proteins"

1

Wnt signaling in development. Georgetown, Tex: Landes Bioscience/Eurekah.com, 2003.

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Kühl, Michael. Wnt signaling in development. Georgetown, Tex: Landes Bioscience, 2003.

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Kahn, Michael. Targeting the Wnt pathway in cancer. New York: Springer, 2011.

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Nusse, Roel, Xi He, and Renee van Amerongen. Wnt signaling: A subject collection from Cold Spring harbor perspectives in biology. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory Press, 2012.

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Hagens, Olivier. An investigation of two novel genes associated with Wnt signalling in Drosophila melanogaster. Brighton, UK: University of Sussex, 2000.

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Elizabeth, Vincan, ed. Wnt signaling. New York, NY: Humana Press, 2008.

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Wnt signaling in embryonic development. Amsterdam: Elsevier, 2007.

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Sokol, Sergei. Wnt Signaling in Embryonic Development, Volume 17 (Advances in Developmental). Elsevier Science, 2007.

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Wnt Signaling in Development and Disease: Molecular Mechanisms and Biological Functions. Wiley-Blackwell, 2014.

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Hoppler, Stefan P., and Randall T. Moon. Wnt Signaling in Development and Disease: Molecular Mechanisms and Biological Functions. Wiley & Sons, Incorporated, John, 2014.

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Book chapters on the topic "Wnt genes. Wnt proteins"

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Bergstein, Ivan, and Anthony M. C. Brown. "WNT Genes and Breast Cancer." In Breast Cancer, 181–98. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-456-6_8.

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Sun, Zijie, and Suk Hyung Lee. "Androgen Action, Wnt Signaling, and Prostate Tumorigenesis." In Androgen-Responsive Genes in Prostate Cancer, 101–16. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-6182-1_7.

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Willert, Karl H. "Isolation and Application of Bioactive Wnt Proteins." In Methods in Molecular Biology, 17–29. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-249-6_2.

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James, Richard G., William H. Conrad, and Randall T. Moon. "β-Catenin-Independent Wnt Pathways: Signals, Core Proteins, and Effectors." In Methods in Molecular Biology, 131–44. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-249-6_10.

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Wolf, Vladimir, Yoshimi Endo, and Jeffrey S. Rubin. "Purification and Wnt-Inhibitory Activities of Secreted Frizzled-Related Proteins." In Methods in Molecular Biology, 31–44. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-249-6_3.

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Bryant, J. "Introduction: Part II–Genomes, genes and proteins." In WIT Transactions on State-of-the-art in Science and Engineering, 13–27. Southampton UK: WIT Press, 2006. http://dx.doi.org/10.2495/978-1-85312-853-0/02.

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Sharma, Manisha, Michael Johnson, Mariana Brocardo, Cara Jamieson, and Beric R. Henderson. "Wnt Signaling Proteins Associate with the Nuclear Pore Complex: Implications for Cancer." In Cancer Biology and the Nuclear Envelope, 353–72. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_16.

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Bordet, Guillaume, and Vincent Bertrand. "Zic Genes in Nematodes: A Role in Nervous System Development and Wnt Signaling." In Advances in Experimental Medicine and Biology, 59–68. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-7311-3_4.

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Planutis, Kestutis, Marina Planutiene, and Randall F. Holcombe. "In Situ Hybridization to Evaluate the Expression of Wnt and Frizzled Genes in Mammalian Tissues." In Methods in Molecular Biology, 231–41. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-249-6_18.

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Edwards, Paul A. W., Clare Abram, Susan E. Hiby, Christina Niemeyer, Trevor C. Dale, and Jane M. Bradbury. "The Role of erbB-Family Genes and Wnt Genes in Normal and Preneoplastic Mammary Epithelium, Studied by Tissue Reconstitution." In Intercellular Signalling in the Mammary Gland, 57–66. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1973-7_6.

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Conference papers on the topic "Wnt genes. Wnt proteins"

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Fernández-Llamazares, Ana I., Kevin C. M. Hermans, Peter Timmerman, and W. Matthijs Blankesteijn. "Mimicking the Binding Sites of Wnt Proteins: Rational Design of Wnt/Fzd-Signaling Modulators." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.212.

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Konigshoff, M., EM Pfaff, N. Balsara, A. Gunther, and O. Eickelberg. "Dysregulation of the Wnt/beta-Catenin Pathway in Idiopathic Pulmonary Fibrosis: Epithelial-Derived Dickkopf Proteins Control Wnt-Induced Effects." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3454.

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Rehan, Virender K., Reiko Sakurai, Vijay Dhar, and John S. Torday. "Tracheal Aspirate Wnt-Related Proteins LEF-1 And ²-catenin, Novel Biomarkers Of Bronchopulmonary Dysplasia." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4131.

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Phillip, Cornel J., and Carlos S. Moreno. "Abstract 4932: Genistein Can Induce Demethylation Of Wnt Negative Regulatory Genes In Prostate Cancer Cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4932.

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Wang, Lihong, Yufang Ma, Ethan Lee, and Jialiang Wang. "Abstract 3529: BET bromodomain proteins regulate the canonical WNT signaling and drug resistance in colorectal cancer." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3529.

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Goodwin, Andrew, Liang Zheng, Ling Lin, Ivan O. Rosas, and Danielle Morse. "Small Proline Rich Repeat Protein 1A Protects Against Epithelial Apoptosis And Is A Downstream Target Of WNT Proteins." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5997.

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Bernabe-Dones, Raul D., Sharon C. Fonseca-Williams, Mercedes Y. Lacourt-Ventura, Cristina Muñoz, Maribel Tirado-Gomez, and Marcia R. Cruz-Correa. "Abstract 4783: Expression of genes panel related to WNT- signaling in colorectal cancer Human Papillomavirus-positive colorectal cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4783.

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Liu, H., X. Li, and J. Wang. "FRI0149 Inflammation intensity-dependent expression of osteoinductive wnt proteins is critical for ectopic new bone formation in ankylosing spondylitis." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.2570.

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Komatsu, Hisateru, Atsushi Niida, Masami Ueda, Hidenari Hirata, Ryutaro Uchi, Sho Nambara, Tomoko Saito, et al. "Abstract 1948: In silico screening for novel Wnt/β-catenin pathway target and regulator genes in human hepatocellular carcinoma." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1948.

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Ripple, Michael J., Amanda Struckhoff, Robin McGoey, and Luis Del Valle. "Abstract 4774: JC virus T-antigen-dependent activation of Wnt target genes and cell cycle progression in colon cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4774.

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Reports on the topic "Wnt genes. Wnt proteins"

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Kitajewski, Jan. WNT Proteins in Mammary Epithelial Cell Transformation. Fort Belvoir, VA: Defense Technical Information Center, July 1997. http://dx.doi.org/10.21236/ada329512.

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Kitajewski, Jan, Martin Julius, and Zhili Zheng. Wnt Proteins in Mammary Epithelial Cell Transformation. Fort Belvoir, VA: Defense Technical Information Center, June 1995. http://dx.doi.org/10.21236/ada297169.

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Kitajewski, Jan. WNT Proteins in Mammary Epithelial Cell Transformation. Fort Belvoir, VA: Defense Technical Information Center, July 1996. http://dx.doi.org/10.21236/ada314737.

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Kitajewski, Jan. WNT Proteins in Mammary Epithelial Cell Transformation. Fort Belvoir, VA: Defense Technical Information Center, June 1998. http://dx.doi.org/10.21236/ada358913.

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Wang, Xianshu. Analysis of Human AXIN2 and Other Wnt Signal Pathway Genes in Human Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2003. http://dx.doi.org/10.21236/ada415833.

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