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10.1007/s12079-013-0218-2 http://scihub22266oqcxt.onion/10.1007/s12079-013-0218-2 C4063992!4063992!24488697     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 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+Cell+Commun+Signal 2014 ; 8 (2): 135-46 Nephropedia Template TP {{tp|p=24488697|t=2014. The matricellular protein CCN5 regulates podosome function via interaction with integrin ?v?3 |pdf=|usr=}}{{24488697}} gab.com Text The matricellular protein CCN5 regulates podosome function via interaction with integrin v 3 JO: J Cell Commun Signal http://www.kidney.de/pget.php?&tw=1&pmid=24488697 #FOAvip CCN proteins play crucial roles in cell motility, matrix turnover, and proliferation. In particular, CCN5 plays a role in cell motility and proliferation in several cell types; however, no functional binding proteins for CCN5 have been identified. In this study we report that CCN5 binds to the cell surface receptor integrin ?v?3 in vascular smooth muscle cells. Furthermore, this interaction takes place in podosomes, organelles known to degrade matrix and mediate motility. We show that CCN5 regulates the ability of podosomes to degrade matrix, but does not affect podosome formation. The level of CCN5 present in a podosome negatively correlates with its ability to degrade matrix. Conversely, knockdown of CCN5 greatly enhances the matrix-degrading ability of podosomes. These findings suggest that the antimotility effects of CCN5 may be mediated through the direct interaction of CCN5 and integrin ?v?3 in podosomes and the concomitant suppression of matrix degradation that is required for cell migration. Twit Text FOAVip The matricellular protein CCN5 regulates podosome function via interaction with integrin v 3 ????J Cell Commun Signal http://www.kidney.de/pget.php?&tw=1&pmid=24488697 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24488697 #FOAvip English Wikipedia <ref>{{Cite pmid|24488697}}</ref> The matricellular protein CCN5 regulates podosome function via interaction with integrin ?v?3 #MMPMID24488697 Myers RB; Wei L; Castellot JJ J Cell Commun Signal 2014[Jun]; 8 (2): 135-46 PMID24488697show ga CCN proteins play crucial roles in cell motility, matrix turnover, and proliferation. In particular, CCN5 plays a role in cell motility and proliferation in several cell types; however, no functional binding proteins for CCN5 have been identified. In this study we report that CCN5 binds to the cell surface receptor integrin ?v?3 in vascular smooth muscle cells. Furthermore, this interaction takes place in podosomes, organelles known to degrade matrix and mediate motility. We show that CCN5 regulates the ability of podosomes to degrade matrix, but does not affect podosome formation. The level of CCN5 present in a podosome negatively correlates with its ability to degrade matrix. Conversely, knockdown of CCN5 greatly enhances the matrix-degrading ability of podosomes. These findings suggest that the antimotility effects of CCN5 may be mediated through the direct interaction of CCN5 and integrin ?v?3 in podosomes and the concomitant suppression of matrix degradation that is required for cell migration. äThe matricellular protein CCN5 regulates podosome function via interac(epmc).pdf DeepDyve Pubget Overpricing