• Admin Login
    View Item 
    •   Home
    • Research Institute in Healthcare Science
    • Research Institute in Healthcare Science
    • View Item
    •   Home
    • Research Institute in Healthcare Science
    • Research Institute in Healthcare Science
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of WIRECommunitiesTitleAuthorsIssue DateSubmit DateSubjectsTypesJournalDepartmentPublisherThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsTypesJournalDepartmentPublisher

    Administrators

    Admin Login

    Local Links

    AboutThe University LibraryOpen Access Publications PolicyDeposit LicenceCOREWIRE Copyright and Reuse Information

    Statistics

    Display statistics

    Novel mastoparan analogs induce differential secretion from mast cells.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    Publisher version
    View Source
    Access full-text PDFOpen Access
    View Source
    Check access options
    Check access options
    Authors
    Farquhar, Michelle
    Soomets, Ursel
    Bates, Ruth L.
    Martin, Ashley
    Langel, Ulo
    Howl, John D.
    Issue Date
    2002
    
    Metadata
    Show full item record
    Abstract
    Cationic amphiphilic peptides stimulate secretion via a receptor-independent action upon G proteins. We have previously utilized chimeric analogs of mastoparan (MP), including galparan (galanin(1-13)-MP ), as molecular probes of secretion. Here, we further resolve the structure-activity relationship of peptidyl secretagogs, including rationally designed chimeric MP analogs. The secretory efficacies of 10 MP analogs were significantly higher than 45 unrelated basic peptides. Comparative studies identified MP analogs that are differential secretagogs for 5-hydroxytryptamine (5-HT) and beta-hexosaminidase. Peptide-induced activation of phospholipase D (PLD), an enzyme intimately involved in regulated exocytosis [5], correlated with the secretion of beta-hexosaminidase but not 5-HT. Thus, these data indicate that different mechanisms are responsible for the exocytosis of 5-HT and beta-hexosaminidase, respectively. Moreover, mastoparan analogs are novel tools for probing the molecular details of exocytosis and other biological phenomena.
    Citation
    Chemistry & Biology, 9(1): 63-70
    Publisher
    Elsevier Science B.V
    URI
    http://hdl.handle.net/2436/14646
    DOI
    10.1016/S1074-5521(01)00098-9
    Additional Links
    http://direct.bl.uk/bld/PlaceOrder.do?UIN=108952570&ETOC=RN&from=searchenginehttp://www.ingentaconnect.com/content/els/10745521/2002/00000009/00000001/art00098
    Type
    Journal article
    Language
    en
    Description
    Metadata only
    ISSN
    10745521
    ae974a485f413a2113503eed53cd6c53
    10.1016/S1074-5521(01)00098-9
    Scopus Count
    Collections
    Research Institute in Healthcare Science

    entitlement

     
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Contact Us
    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.