Shared more. Cited more. Safe forever.
    • advanced search
    • submit works
    • about
    • help
    • contact us
    • login
    View Item 
    •   MOspace Home
    • University of Missouri-Columbia
    • Health Sciences Research Day (MU)
    • 2009 Health Sciences Research Day (MU)
    • View Item
    •   MOspace Home
    • University of Missouri-Columbia
    • Health Sciences Research Day (MU)
    • 2009 Health Sciences Research Day (MU)
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.
    advanced searchsubmit worksabouthelpcontact us

    Browse

    All of MOspaceCommunities & CollectionsDate IssuedAuthor/ContributorTitleIdentifierThesis DepartmentThesis AdvisorThesis SemesterThis CollectionDate IssuedAuthor/ContributorTitleIdentifierThesis DepartmentThesis AdvisorThesis Semester

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular AuthorsStatistics by Referrer

    Targeting the guanylate cyclase c receptor with an agonist peptide from enterotoxegenic Y. Enterocolitica [abstract]

    Loethen, Troy J.
    Liu, Dijie
    View/Open
    [PDF] TargetingGuanylateCyclaseCReceptor[abstract].pdf (22.89Kb)
    Date
    2010-03
    Contributor
    University of Missouri--Columbia. School of Medicine
    Format
    Abstract
    Metadata
    [+] Show full item record
    Abstract
    Heat-stable enterotoxin peptides (ST's) are expressed by enterotoxigenic strains of bacteria in order to co-opt an endogenous ligand-receptor system that regulates fluid homeostasis within the gut. Bacteria such as E. coli, V. Cholerae, and Y. enterocolitica have evolved ST's which mimic native guanylin/uroguanylin peptides by activating guanylate cyclase C (GC-C), yet possess increased resistance to heat/enzymatic degradation as well as superagonist activity by virtue of a third disulfide bond. We have previously utilized ST peptides derived from an E. coli isolate, as well as analogs of the endogenous peptide hormone uroguanylin, as imaging and therapeutic agents for GC-C-expressing colorectal cancers. In this work, we have compared the ability of these peptides to target GC-C and engender production of cGMP with that of an ST analog derived from Yersinia enterocolitica.Previous results had suggested that the Y. enterocolitica sequence may elicit higher cyclase activity than other peptides in this class. We have generated the peptide GENDWDWCCELCCNPACFGC both with and without an N-terminal DOTA chelating moiety and characterized its receptor binding affinity and ability to stimulate cGMP production in comparison to other peptides in this class. Our findings indicate that the Yersinia peptide possesses receptor binding affinity and cyclase stimulating activity intermediate between known E. coli ST analogs and human uroguanylin. However, in vivo biodistribution results obtained using the 64Cu-labeled DOTA-peptide demonstrated normal tissue distributions substantially different from E. coli-derived peptides, and more akin to those obtained with radiolabeled uroguanylin peptides.
    URI
    http://hdl.handle.net/10355/6494
    Rights
    OpenAccess.
    This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License.
    Collections
    • 2009 Health Sciences Research Day (MU)

    Send Feedback
    hosted by University of Missouri Library Systems
     

     


    Send Feedback
    hosted by University of Missouri Library Systems