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Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases.

Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Research Abstract Details 

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  • Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Abstract Text:

    t chenT Chen,m o'rourkeM O'rourke,j mckennaJ McKenna,d g hirstD G Hirst,c shawC Shaw,

    Maximakinin is an N-terminally extended bradykinin (DLPKINRKGPRPPGFSPFR) from the venom of a Chinese toad (Bombina maxima) that displays highly selective activity at mammalian arterial smooth muscle receptors. In this study, we report that incubation of maximakinin with either kallikrein or human saliva generates catabolites with enhanced bioactivity that retain the tissue selective effects of the parent molecule. In addition, we have observed that kallikrein rapidly cleaves the C-terminal arginyl residue of both maximakinin and bradykinin - a cleavage hitherto considered to be performed by a carboxypeptidase that facilitates selective bradykinin receptor targeting. Maximakinin has thus evolved as a 'smart' defensive weapon in the toad with inherent resistance to the signal-terminating protease hardware in the potential predator. Thus, natural selection of amphibian skin peptides for antipredator defence, through interspecies delivery by an exogenous secretory mode, produces subtle structural stabilization modifications that can potentially provide new insights for the design of orally active and selectively targeted peptide therapeutics.

    Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Publishing Authors By Initials

    t chenT Chen,m o'rourkeM O'rourke,j mckennaJ McKenna,dg hirstDG Hirst,c shawC Shaw,

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    Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: The journal of peptide research : official journal

    VOLUME: 66 Suppl 1

    Page Numbers: 106-13

    Journal Abbreviation: J. Pept. Res.

    ISSN: 1397-002X

    DAY: 2

    MONTH: Dec

    YEAR: 2005

    Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Information

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    LANGUAGE: eng

    NlmUniqueID: 9707067

    Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Keywords Mesh Terms:

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    Chemical & Substance for Abstract: Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases. Information

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    Grant and Affiliation Information for Biotransformation of maximakinin, a bradykinin-related nonadecapeptide from toad venom, by mammalian kallikrein and salivary proteases.

    AFFILIATION: School of Biomedical Sciences, University of Ulster, Cromore Road, Coleraine BT52 1SA, UK.

    Country: Denmark

    Denmark Research PublicationDenmark Research Publication

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    MEDLINETA: J Pept Res

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