國家衛生研究院 NHRI:Item 3990099045/9681

NHRI > National Institute of Infectious Diseases and Vaccinology > Min-Shi Lee > Periodical Articles > Item 3990099045/9681

Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/9681

Title:	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
Other Titles:	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
Authors:	Wu, PL;Lin, CC;Lin, TH;Lee, MS;Wu, WG
Contributors:	Division of Infectious Diseases
Abstract:	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.
Date:	2016-08
Relation:	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
Appears in Collections:	[Min-Shi Lee] Periodical Articles

Files in This Item:

File	Description	Size	Format
PUB27090013.pdf		2237Kb	Adobe PDF	473	View/Open

Loading...