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10.1172/JCI88696 http://scihub22266oqcxt.onion/10.1172/JCI88696 C5490773!5490773!28530637     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Clin+Invest ä ; 127 (7): 2541-54 Nephropedia Template TP {{tp|p=28530637|t=ä. Cell-penetrating peptides selectively targeting SMAD3 inhibit profibrotic TGF-? signaling |pdf=|usr=}}{{28530637}} gab.com Text Cell-penetrating peptides selectively targeting SMAD3 inhibit profibrotic TGF- signaling JO: J Clin Invest http://www.kidney.de/pget.php?&tw=1&pmid=28530637 #FOAvip TGF-? is considered a master switch in the pathogenesis of organ fibrosis. The primary mediators of this activity are the SMAD proteins, particularly SMAD3. In the current study, we have developed a cell-penetrating peptide (CPP) conjugate of the HIV TAT protein that is fused to an aminoterminal sequence of sorting nexin 9 (SNX9), which was previously shown to bind phosphorylated SMAD3 (pSMAD3). We determined that specifically preventing the nuclear import of pSMAD3 using the TAT-SNX9 peptide inhibited profibrotic TGF-? activity in murine cells and human lung fibroblasts as well as in vivo with no demonstrable toxicity. TGF-? signaling mediated by pSMAD2, bone morphogenetic protein 4 (BMP4), EGF, or PDGF was unaffected by the TAT-SNX9 peptide. Furthermore, while the TAT-SNX9 peptide prevented TGF-??s profibrotic activity in vitro as well as in 2 murine treatment models of pulmonary fibrosis, a 3?amino acid point mutant that was unable to bind pSMAD3 proved ineffective. These findings indicate that specifically targeting pSMAD3 can ameliorate both the direct and indirect fibroproliferative actions of TGF-?. Twit Text FOAVip Cell-penetrating peptides selectively targeting SMAD3 inhibit profibrotic TGF- signaling ????J Clin Invest http://www.kidney.de/pget.php?&tw=1&pmid=28530637 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28530637 #FOAvip English Wikipedia <ref>{{Cite pmid|28530637}}</ref> Cell-penetrating peptides selectively targeting SMAD3 inhibit profibrotic TGF-? signaling #MMPMID28530637 Kang JH; Jung MY; Yin X; Andrianifahanana M; Hernandez DM; Leof EB J Clin Invest ä[]; 127 (7): 2541-54 PMID28530637show ga TGF-? is considered a master switch in the pathogenesis of organ fibrosis. The primary mediators of this activity are the SMAD proteins, particularly SMAD3. In the current study, we have developed a cell-penetrating peptide (CPP) conjugate of the HIV TAT protein that is fused to an aminoterminal sequence of sorting nexin 9 (SNX9), which was previously shown to bind phosphorylated SMAD3 (pSMAD3). We determined that specifically preventing the nuclear import of pSMAD3 using the TAT-SNX9 peptide inhibited profibrotic TGF-? activity in murine cells and human lung fibroblasts as well as in vivo with no demonstrable toxicity. TGF-? signaling mediated by pSMAD2, bone morphogenetic protein 4 (BMP4), EGF, or PDGF was unaffected by the TAT-SNX9 peptide. Furthermore, while the TAT-SNX9 peptide prevented TGF-??s profibrotic activity in vitro as well as in 2 murine treatment models of pulmonary fibrosis, a 3?amino acid point mutant that was unable to bind pSMAD3 proved ineffective. These findings indicate that specifically targeting pSMAD3 can ameliorate both the direct and indirect fibroproliferative actions of TGF-?. äCell-penetrating peptides selectively targeting SMAD3 inhibit profibro(epmc).pdf DeepDyve Pubget Overpricing