國家衛生研究院 NHRI:Item 3990099045/9681
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    题名: Distal M domain of cobra ADAM-like metalloproteinase mediates the binding of positively charged cysteine-rich domain to alphavbeta3 integrin in the suppression of cell migration
    其它题名: Distal M domain of cobra ADAM-like metalloproteinase mediates the binding of positively charged cysteine-rich domain to αvβ3 integrin in the suppression of cell migration
    作者: Wu, PL;Lin, CC;Lin, TH;Lee, MS;Wu, WG
    贡献者: Division of Infectious Diseases
    摘要: We have previously identified two new P-III type ADAM-like snake venom metalloproteinases (SVMPs), i.e., atragin and kaouthiagin-like, from Taiwan cobra venom and determined their 3D structures with a distinct C- and I-shaped metalloproteinase/disintegrin-like/cysteine-rich (MDC) modular architecture. Herein, we investigated their functional targets to elucidate the role of cobra SVMPs in perturbing wound healing in snakebite victims. We showed that the non-RGD (Arg-Gly-Asp) C-shaped SVMP atragin binds about ten-fold stronger than the RGD-containing I-shaped SVMP kaouthiagin-like to alphavbeta3 integrin in the surface-immobilized form. Atragin binds to alphavbeta3 integrin through a novel interaction mode involving distal M and C domains via the RRN sequence motif in the hyper variable loop. In a cell adhesion assay, the adhesion of fibroblasts to atragin was mediated by alphavbeta3 integrin. Furthermore, atragin inhibited wound healing and suppressed cell migration in a alphavbeta3 integrin-dependent manner. These results, together with our previous demonstration of non-cytotoxic cobra CTX A5 in targeting alphavbeta3 integrin, suggest that cobra venom consists of several non-RGD toxins with integrin-binding specificity that could perturb wound healing in snakebite victims.
    日期: 2016-08
    關聯: Toxicon. 2016 Aug;118:1-12.
    Link to: http://dx.doi.org/10.1016/j.toxicon.2016.04.034
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0041-0101&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000380594700001
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84963820155
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