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10.1038/srep43612 http://scihub22266oqcxt.onion/10.1038/srep43612 C5333632!5333632!28252668     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28252668&cmd=llinks): Failed to open stream: HTTP request failed! 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Aggretin Venom Polypeptide as a Novel Anti-angiogenesis Agent by Targeting Integrin alpha2beta1 |pdf=|usr=}}{{28252668}} gab.com Text Aggretin Venom Polypeptide as a Novel Anti-angiogenesis Agent by Targeting Integrin alpha2beta1 JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28252668 #FOAvip VEGF and VEGFR antibodies have been used as a therapeutic strategy to inhibit angiogenesis in many diseases; however, frequent and repeated administration of these antibodies to patients induces immunogenicity. In previous studies, we demonstrated that aggretin, a heterodimeric snake venom C-type lectin, exhibits pro-angiogenic activities via integrin ?2?1 ligation. We hypothesised that small-mass aggretin fragments may bind integrin ?2?1 and act as antagonists of angiogenesis. In this study, the anti-angiogenic efficacy of a synthesised aggretin ?-chain C-terminus (AACT, residue 106?136) was evaluated in both in vitro and in vivo angiogenesis models. The AACT demonstrated inhibitory effects on collagen-induced platelet aggregation and HUVEC adhesion to immobilised collagen. These results indicated that AACT may block integrin ?2?1?collagen interaction. AACT also inhibited HUVEC migration and tube formation. Aortic ring sprouting and Matrigel implant models demonstrated that AACT markedly inhibited VEGF-induced neovascularisation. In addition, induction of FAK/PI3K/ERK1/2 tyrosine phosphorylation and talin 1/2 associated with integrin ?1 which are induced by VEGF were blocked by AACT. Similarly, tyrosine phosphorylation of VEFGR2 and ERK1/2 induced by VEGF was diminished in integrin ?2-silenced endothelial cells. Our results demonstrate that AACT is a potential therapeutic candidate for angiogenesis related-diseases via integrin ?2?1 blockade. Twit Text FOAVip Aggretin Venom Polypeptide as a Novel Anti-angiogenesis Agent by Targeting Integrin alpha2beta1 ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28252668 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28252668 #FOAvip English Wikipedia <ref>{{Cite pmid|28252668}}</ref> Aggretin Venom Polypeptide as a Novel Anti-angiogenesis Agent by Targeting Integrin alpha2beta1 #MMPMID28252668 Chung CH; Chang CH; Hsu CC; Lin KT; Peng HC; Huang TF Sci Rep 2017[]; 7 (ä): ä PMID28252668show ga VEGF and VEGFR antibodies have been used as a therapeutic strategy to inhibit angiogenesis in many diseases; however, frequent and repeated administration of these antibodies to patients induces immunogenicity. In previous studies, we demonstrated that aggretin, a heterodimeric snake venom C-type lectin, exhibits pro-angiogenic activities via integrin ?2?1 ligation. We hypothesised that small-mass aggretin fragments may bind integrin ?2?1 and act as antagonists of angiogenesis. In this study, the anti-angiogenic efficacy of a synthesised aggretin ?-chain C-terminus (AACT, residue 106?136) was evaluated in both in vitro and in vivo angiogenesis models. The AACT demonstrated inhibitory effects on collagen-induced platelet aggregation and HUVEC adhesion to immobilised collagen. These results indicated that AACT may block integrin ?2?1?collagen interaction. AACT also inhibited HUVEC migration and tube formation. Aortic ring sprouting and Matrigel implant models demonstrated that AACT markedly inhibited VEGF-induced neovascularisation. In addition, induction of FAK/PI3K/ERK1/2 tyrosine phosphorylation and talin 1/2 associated with integrin ?1 which are induced by VEGF were blocked by AACT. Similarly, tyrosine phosphorylation of VEFGR2 and ERK1/2 induced by VEGF was diminished in integrin ?2-silenced endothelial cells. Our results demonstrate that AACT is a potential therapeutic candidate for angiogenesis related-diseases via integrin ?2?1 blockade. äAggretin Venom Polypeptide as a Novel Anti-angiogenesis Agent by Targe(epmc).pdf DeepDyve Pubget Overpricing