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Activation of cathepsin L by the cathelin-like domain of protegrin-3.

Activation of cathepsin L by the cathelin-like domain of protegrin-3. Research Abstract Details 

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  • Activation of cathepsin L by the cathelin-like domain of protegrin-3. Abstract Text:

    shunyi zhuShunyi Zhu,liang weiLiang Wei,kenshi yamasakiKenshi Yamasaki,richard l galloRichard L Gallo,

    The cathelin-like domain (CLD) of the antimicrobial cathelicidin family constitutes a unique protein family with structural similarity to cystatins, the cysteine protease inhibitors. CLDs are derived from the processed amino-terminal prosequence of the cathelicidin precursors with conservation across the vertebrate lineage ranging from fish to human. Initial attempt to characterize a possible inhibitory activity of protegrin-3 (PG3) CLD protein (a member of the multigene family of porcine cathelicidins) against several proteases led to an unexpected finding that PG3 CLD efficiently activated rather than inhibited human cathepsin L. Partial deletion of the L2 loop of PG3 CLD, a structurally equivalent region important in interaction of cystatins with proteases, significantly decreased its activating effect on cathepsin L. A complex model based on this functional loop was proposed to explain this unexpected effect, in which evolutionary emergence of completely opposite biological activity could be associated with structural discrepancies of the loop due to sequence variations between pig and human. Our results provide new insights into deeper understanding of the immune-related biological activity of this so-called pro-domain of the cathelicidin family.

    Activation of cathepsin L by the cathelin-like domain of protegrin-3. Publishing Authors By Initials

    s zhuS Zhu,l weiL Wei,k yamasakiK Yamasaki,rl galloRL Gallo,

    For similar abstracts research abstracts see: abstracts research

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    Activation of cathepsin L by the cathelin-like domain of protegrin-3. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Molecular immunology

    VOLUME: 45

    Page Numbers: 2531-6

    Journal Abbreviation: Mol. Immunol.

    ISSN: 0161-5890

    DAY: 4

    MONTH: 03

    YEAR: 2008

    Activation of cathepsin L by the cathelin-like domain of protegrin-3. Information

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    LANGUAGE: eng

    NlmUniqueID: 7905289

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    Grant and Affiliation Information for Activation of cathepsin L by the cathelin-like domain of protegrin-3.

    AFFILIATION: Group of Animal Innate Immunity, State Key Laboratory of Integrated Management of Pest Insects & Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: Mol Immunol

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