• Login
    View Item 
    •   Home
    • Faculty/ Researcher Works
    • Faculty/ Researcher Works
    • View Item
    •   Home
    • Faculty/ Researcher Works
    • Faculty/ Researcher Works
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of TUScholarShareCommunitiesDateAuthorsTitlesSubjectsGenresThis CollectionDateAuthorsTitlesSubjectsGenres

    My Account

    LoginRegister

    Help

    AboutPeoplePoliciesHelp for DepositorsData DepositFAQs

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Mutations in the C-terminus of the X protein of hepatitis B virus regulate Wnt-5a expression in hepatoma Huh7 cells: cDNA microarray and proteomic analyses

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    Mutations in the C-terminus of ...
    Size:
    608.3Kb
    Format:
    PDF
    Download
    Genre
    Journal Article
    Date
    2008-06-01
    Author
    Liu, X
    Wang, L
    Zhang, S
    Lin, J
    Zhang, S
    Feitelson, MA
    Gao, H
    Zhu, M
    Subject
    Blotting, Western
    Carcinoma, Hepatocellular
    Cell Line, Tumor
    Electrophoresis, Gel, Two-Dimensional
    Gene Expression
    Humans
    Immunohistochemistry
    Liver Neoplasms
    Mutation
    Oligonucleotide Array Sequence Analysis
    Proteomics
    Proto-Oncogene Proteins
    Reverse Transcriptase Polymerase Chain Reaction
    Trans-Activators
    Transfection
    Viral Regulatory and Accessory Proteins
    Wnt Proteins
    Wnt-5a Protein
    Show allShow less
    Permanent link to this record
    http://hdl.handle.net/20.500.12613/5608
    
    Metadata
    Show full item record
    DOI
    10.1093/carcin/bgn111
    Abstract
    Background: The hepatitis B virus x gene (HBx) is a promiscuous transactivator implicated in the development of hepatocellular carcinoma (HCC). The present study was designed to investigate the molecular events regulated by HBx. Methods: Genomic and proteomic expression profiling was performed in Huh7 HCC cells transfected with HBx mutants with a C-terminal deletion. The gene and protein expression of wingless-type murine-mammary-tumour virus (MMTV) integration site family, member 5A (Wnt-5a) was validated by analyses of reverse transcription-polymerase chain reaction (RT-PCR), real-time RT-PCR, western blot and immunohistochemistry. Results: Differentially expressed genes and proteins were found in the transfected Huh7 HCC cells; most of them were involved in transcriptional regulation, although others including oncogenes or tumor suppressor genes, and molecules involved in cell junctions, signal transduction pathways, metabolism or the immune response were also observed. The expression of the Wnt-5a gene was elevated >10-fold in Huh7 cells transfected with the HBx 3′-30 amino acid deletion mutant. However, the expression was downregulated by the transfection with the HBx 3′-40 amino acid deletion mutant. The changes in Wnt-5a expression were also observed in human HCC tissues, compared with corresponding non-cancerous liver tissues. A negative correlation was found between the expression of Wnt-5a and HBx COOH mutations in HCC tissues. Conclusions: HBx mutants may participate in the development and progression of HCC, at least in part through the Wnt-5a pathway. © The Author 2008. Published by Oxford University Press. All rights reserved.
    Citation to related work
    Oxford University Press (OUP)
    Has part
    Carcinogenesis
    ADA compliance
    For Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/5590
    Scopus Count
    Collections
    Faculty/ Researcher Works

    entitlement

     

    Related items

    Showing items related by title, author, creator and subject.

    • Thumbnail

      Quantifying Nucleoporin Stoichiometry Inside Single Nuclear Pore Complexes In vivo

      Mi, L; Goryaynov, A; Lindquist, A; Rexach, M; Yang, W; Yang, Weidong|0000-0002-3554-3035 (2015-01-01)
      © 2015, Nature Publishing Group. All rights reserved. The nuclear pore complex (NPC) is one of the largest supramolecular structures in eukaryotic cells. Its octagonal ring-scaffold perforates the nuclear envelope and features a unique molecular machinery that regulates nucleocytoplasmic transport. NPCs are composed of ∼30 different nucleoporins (Nups), averaged at 8, 16 or 32 copies per NPC. This estimate has not been confirmed for individual NPCs in living cells due to the inherent difficulty of counting proteins inside single supramolecular complexes. Here we used single-molecule SPEED microscopy to directly count the copy-number of twenty-four different Nups within individual NPCs of live yeast, and found agreement as well as significant deviation from previous estimates. As expected, we counted 8 copies of four peripheral Nups and 16 copies of fourteen scaffold Nups. Unexpectedly, we counted a maximum of 16 copies of Nsp1 and Nic96, rather than 32 as previously estimated; and found only 10-15 copies of six other Nups, rather than 8 or 16 copies as expected. This in situ molecular-counting technology can test structure-function models of NPCs and other supramolecular structures in cells.
    • Thumbnail

      A Spiroligomer α-Helix Mimic That Binds HDM2, Penetrates Human Cells and Stabilizes HDM2 in Cell Culture

      Brown, ZZ; Akula, K; Arzumanyan, A; Alleva, J; Jackson, M; Bichenkov, E; Sheffield, JB; Feitelson, MA; Schafmeister, CE (2012-10-18)
      We demonstrate functionalized spiroligomers that mimic the HDM2-bound conformation of the p53 activation domain. Spiroligomers are stereochemically defined, functionalized, spirocyclic monomers coupled through pairs of amide bonds to create spiro-ladder oligomers [1]. Two series of spiroligomers were synthesized, one of structural analogs and one of stereochemical analogs, from which we identified compound 1, that binds HDM2 with a Kd value of 400 nM. The spiroligomer 1 penetrates human liver cancer cells through passive diffusion and in a dose-dependent and time-dependent manner increases the levels of HDM2 more than 30-fold in Huh7 cells in which the p53/HDM2 negative feed-back loop is inoperative. This is a biological effect that is not seen with the HDM2 ligand nutlin-3a. We propose that compound 1 modulates the levels of HDM2 by stabilizing it to proteolysis, allowing it to accumulate in the absence of a p53/HDM2 feedback loop. © 2012 Brown et al.
    • Thumbnail

      The retinoblastoma family: Twins or distant cousins?

      Claudio, PP; Tonini, T; Giordano, A; Giordano, Antonio|0000-0002-5959-016X (2002-09-23)
      The destiny of a cell - whether it undergoes division, differentiation or death - results from an intricate balance of many regulators, including oncoproteins, tumor-suppressor proteins and cell-cycle-associated proteins. One of the better-studied tumor suppressors is the retinoblastoma protein, known as pRb or p105. Two recently identified proteins, pRb2/p130 and p107, show structural and functional similarities to pRb, and these proteins and their orthologs make up the retinoblastoma (Rb) family. Members of the family have been found in animals and plants, and a related protein is known in the alga Chlamydomonas. Members of the Rb family are bound and inactivated by viral proteins and, in turn, bind cellular transcription factors and repress their function, and can also form complexes with cyclins and cyclin-dependent kinases and with histone deacetylases. The are found in the nucleus and their subnuclear localization depends on binding to the nuclear matrix. Members of the family form part of a signal-transduction pathway called the Rb pathway, which is important in cell-cycle regulation and have roles in growth suppression, differentiation and apoptosis in different organisms and cell types.
    DSpace software (copyright © 2002 - 2022)  DuraSpace
    Temple University Libraries | 1900 N. 13th Street | Philadelphia, PA 19122
    (215) 204-8212 | scholarshare@temple.edu
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.