JavaScript is disabled for your browser. Some features of this site may not work without it.
  • About K
  • Academics
  • Admission
  • Alumni Relations
  • Giving to K
  • News & Events
  • Student Life
  • HORNET HIVE
  • ATHLETICS
  • SITEMAP
  • WEBMAIL
    • Login
    View Item 
    •   CACHE Homepage
    • Academic Departments, Programs, and SIPs
    • Biology
    • Diebold Symposium Posters and Schedules
    • View Item
    •   CACHE Homepage
    • Academic Departments, Programs, and SIPs
    • Biology
    • Diebold Symposium Posters and Schedules
    • View Item

    Expression of Mutant Epitope-Tagged TACE Constructs in TACE Knockout Fibroblasts and the Importance of TACE Cytoplasmic Domain in PKC-Mediated Phosphorylation

    Thumbnail
    View/Open
    poster/ Kalamazoo College only (925.5Kb)
    Date
    2005
    Author
    Januszewski, Jacob
    Metadata
    Show full item record
    Abstract
    Alzheimer's disease (AD) is its most common form of dementia affecting the elderly population. It is speculated that one of the essential upstream mediators of AD is the accumulation of amyloid beta (Aβ)-containing plaques in the brain. Ab is derived from the cleavage of the amyloid precursor protein (APP) by β-and γ-secretases. On the contrary, there exists a competing pathway to that of the β-and y-secretases, in which another enzyme called α-secretase cleaves APP within the Aβ region. The result of this cleavage precludes plaque formation in the brain, and produces a non-pathogenic sAPPα fragment. TACE (TNF-α Converting Enzyme) is a well known a-secretase that competes with the AD-causing β-and γ-secretase pathway. Thus, elucidating the mechanism of TACE regulation will potentially play an important role in understanding ways to reduce the amount of Ab produced in disease states. Recent in vitro studies have shown that protein kinase C (PKC) is directly involved in the phosphorylation of the TACE cytoplasmic domain. In order to determine if the cytoplasmic domain of TACE plays a significant role in in vivo PKC-mediated phosphorylation, several mutant versions of the TACE cytoplasmic domain were produced for transfection into TACE knockout fibroblasts. Since this lab has not yet shown if the TACE knockout fibroblasts are transfectable, this became an important factor in the experiment. Here we show that TACE knockout fibroblasts are transfectable, and that cellular detection of equivalent levels of epitope-tagged TACE constructs is possible. Experiments are ongoing to determine if our mutant TACE constructs will produce altered levels of sAPPα. Wild type or mutant TACE constructs will be expressed and then stimulated with PMA to determine if the mutant version of TACE reduces the amount of sAPPα produced.
    URI
    http://hdl.handle.net/10920/8045
    Collections
    • Diebold Symposium Posters and Schedules [479]

    Browse

    All of CACHECommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    Login

    DSpace software copyright © 2002-2023  DuraSpace
    DSpace Express is a service operated by 
    Atmire NV
    Logo

    Kalamazoo College
    1200 Academy Street
    Kalamazoo Michigan 49006-3295
    USA
    Info 269-337-7000
    Admission 1-800-253-3602

    About K
    Academics
    Admission
    Alumni Relations
    Giving to K
    News & Events
    Student Life
    Sitemap
    Map & Directions
    Contacts
    Directories
    Nondiscrimination Policy
    Consumer Information
    Official disclaimer
    Search this site


    Academic Calendars
    Apply
    Bookstore
    Crisis Response
    Employment
    Library
    Registrar
    DSpace Express is a service operated by 
    Atmire NV