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    Intracellular delivery of bioactive peptides to RBL-2H3 cells induces beta-hexosaminidase secretion and phospholipase D activation.

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    Authors
    Howl, John D.
    Jones, Sarah
    Farquhar, Michelle
    Issue Date
    2003
    
    Metadata
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    Abstract
    This investigation compared the secretory efficacies of a series of peptides delivered to the cytoplasm of RBL-2H3 mast cells. Mimetic peptides, designed to target intracellular proteins that regulate cell signalling and membrane fusion, were synthesised as transportan 10 (TP10) chimeras for efficient plasma membrane translocation. Exocytosis of beta-hexosaminidase, a secretory lysosomal marker, indicated that peptides presenting sequences derived from protein kinase C (PKC; C1 H-CRRLSVEIWDWDL-NH(2)) and the CB(1) cannabinoid receptor (C3 H-RSKDLRHAFRSMFPSCE-NH(2)) induced beta-hexosaminidase secretion. Other peptide cargoes, including a Rab3A-derived sequence and a homologue of C3, were inactive in similar assays. Translocated C1 also activated phospholipase D (PLD), an enzyme intimately involved in the regulated secretory response of RBL-2H3 cells, but C1-induced secretion was not dependent upon phosphatidate synthesis. Neither down-regulation of Ca(2+)-sensitive isoforms of PKC nor the application of a selective PKC inhibitor attenuated the secretory efficacy of C1. These observations indicate that the molecular target of C1 is a protein involved in the regulated secretory pathway that is upstream of PLD but is not a PKC isoform. This study also confirmed that TP10 is a relatively inert cell-penetrating vector and is, therefore, widely suitable for studies in cells that are sensitive to peptidyl secretagogues.
    Citation
    ChemBioChem, 4(12): 1312-1316
    Publisher
    Wiley InterScience
    Journal
    ChemBioChem
    URI
    http://hdl.handle.net/2436/29936
    DOI
    10.1002/cbic.200300694
    PubMed ID
    14661273
    Additional Links
    https://onlinelibrary.wiley.com/doi/full/10.1002/cbic.200300694
    Type
    Journal article
    Language
    en
    ISSN
    1439-4227
    ae974a485f413a2113503eed53cd6c53
    10.1002/cbic.200300694
    Scopus Count
    Collections
    Research Institute in Healthcare Science

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