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  • 2000-2004  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 85 (2003), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Vanilloid receptor I (TRPV1) is an integral membrane protein that integrates thermal and chemical stimuli. This molecular device is at the essence of cellular signalling at peripheral nerve terminals where it plays a central role in nociception. As expected, channel dysfunction is critically involved in pain transduction, specially in inflammatory pain. This notion is supported by genetic and pharmacological knock out data. As other ion channels, TRPV1 is a component of supramolecular assemblies that configure intraneuronal protein networks essential for signal transduction. As a result, a tremendous effort is being invested to identify the molecular components of the ion channel complex, and to validate them as therapeutic targets for better analgesic drugs. Current advances and discoveries in this exciting field will be highlighted, along with their implications for efficient and selective pain management.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science, Ltd
    International journal of cosmetic science 24 (2002), S. 0 
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Botulinum neurotoxins (BoNTs) represent a revolution in cosmetic science because of their remarkable and long-lasting antiwrinkle activity. However, their high neurotoxicity seriously limits their use. Thus, there is a need to design and validate non-toxic molecules that mimic the action of BoNTs. The hexapeptide Ac-EEMQRR-NH2 (coined Argireline) was identified as a result of a rational design programme. Noteworthy, skin topography analysis of an oil/water (O/W) emulsion containing 10% of the hexapeptide on healthy women volunteers reduced wrinkle depth up to 30% upon 30 days treatment. Analysis of the mechanism of action showed that Argireline significantly inhibited neurotransmitter release with a potency similar to that of BoNT A, although as expected, it displayed much lower efficacy than the neurotoxin. Inhibition of neurotransmitter release was due to the interference of the hexapeptide with the formation and/or stability of the protein complex that is required to drive Ca2+-dependent exocytosis, namely the vesicular fusion (known as SNARE) complex. Notably, this peptide did not exhibit in vivo oral toxicity nor primary irritation at high doses. Taken together, these findings demonstrate that Argireline is a non-toxic, antiwrinkle peptide that emulates the action of currently used BoNTs. Therefore, this hexapetide represents a biosafe alternative to BoNTs in cosmetics.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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