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Wolverhampton Intellectual Repository and E-Theses > Research Institutes > Research Institute in Healthcare Science > Molecular Pharmacology Research Group > Intracellular delivery of bioactive peptides to RBL-2H3 cells induces beta-hexosaminidase secretion and phospholipase D activation.

Please use this identifier to cite or link to this item: http://hdl.handle.net/2436/29936
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Title: Intracellular delivery of bioactive peptides to RBL-2H3 cells induces beta-hexosaminidase secretion and phospholipase D activation.
Authors: Howl, John D.
Jones, Sarah
Farquhar, Michelle
Citation: ChemBioChem, 4(12): 1312-1316
Publisher: Wiley InterScience
Journal: ChemBioChem
Issue Date: 2003
URI: http://hdl.handle.net/2436/29936
DOI: 10.1002/cbic.200300694
PubMed ID: 14661273
Additional Links: http://www3.interscience.wiley.com/journal/106567337/abstract
http://direct.bl.uk/bld/PlaceOrder.do?UIN=142527065&ETOC=RN&from=searchengine
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.
Type: Article
Language: en
Keywords: Molecular Biology
Chimerism
secretion
MeSH: Amino Acid Sequence
Animals
Cell Line, Tumor
Dose-Response Relationship, Drug
Enzyme Activation
Glycerophospholipids
Mast Cells
Molecular Sequence Data
Peptides
Phospholipase D
Protein Kinase C
Rats
Receptor, Cannabinoid, CB1
Recombinant Fusion Proteins
beta-N-Acetylhexosaminidases
rab3A GTP-Binding Protein
ISSN: 1439-4227
Appears in Collections: Molecular Pharmacology Research Group

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