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10.1158/0008-5472.CAN-14-1017 http://scihub22266oqcxt.onion/10.1158/0008-5472.CAN-14-1017 C4315623!4315623!25297628     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cancer+Res 2014 ; 74 (23): 7125-36 Nephropedia Template TP {{tp|p=25297628|t=2014. HSP90 Supports Tumor Growth and Angiogenesis through PRKD2 Protein Stabilization |pdf=|usr=}}{{25297628}} gab.com Text HSP90 Supports Tumor Growth and Angiogenesis through PRKD2 Protein Stabilization JO: Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=25297628 #FOAvip The kinase PRKD2 (protein kinase D) is a crucial regulator of tumor cell-endothelial cell communication in gastrointestinal tumors and glioblastomas, but its mechanistic contributions to malignant development are not understood. Here, we report that the oncogenic chaperone HSP90 binds to and stabilizes PRKD2 in human cancer cells. Pharmacologic inhibition of HSP90 with structurally divergent small molecules currently in clinical development triggered proteasome-dependent degradation of PRKD2, augmenting apoptosis in human cancer cells of various tissue origins. Conversely, ectopic expression of PRKD2 protected cancer cells from the apoptotic effects of HSP90 abrogation, restoring blood vessel formation in two preclinical models of solid tumors. Mechanistic studies revealed that PRKD2 is essential for hypoxia-induced accumulation of hypoxia-inducible factor-1? (HIF1?) and activation of NF-?B in tumor cells. Notably, ectopic expression of PRKD2 was able to partially restore HIF1? and secreted VEGF-A levels in hypoxic cancer cells treated with HSP90 inhibitors. Taken together, our findings indicate that signals from hypoxia and HSP90 pathways are interconnected and funneled by PRKD2 into the NF-?B/VEGF-A signaling axis to promote tumor angiogenesis and tumor growth. Twit Text FOAVip HSP90 Supports Tumor Growth and Angiogenesis through PRKD2 Protein Stabilization ????Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=25297628 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25297628 #FOAvip English Wikipedia <ref>{{Cite pmid|25297628}}</ref> HSP90 Supports Tumor Growth and Angiogenesis through PRKD2 Protein Stabilization #MMPMID25297628 Azoitei N; Diepold K; Brunner C; Rouhi A; Genze F; Becher A; Kestler H; van Lint J; Chiosis G; Koren J; Fröhling S; Scholl C; Seufferlein T Cancer Res 2014[Dec]; 74 (23): 7125-36 PMID25297628show ga The kinase PRKD2 (protein kinase D) is a crucial regulator of tumor cell-endothelial cell communication in gastrointestinal tumors and glioblastomas, but its mechanistic contributions to malignant development are not understood. Here, we report that the oncogenic chaperone HSP90 binds to and stabilizes PRKD2 in human cancer cells. Pharmacologic inhibition of HSP90 with structurally divergent small molecules currently in clinical development triggered proteasome-dependent degradation of PRKD2, augmenting apoptosis in human cancer cells of various tissue origins. Conversely, ectopic expression of PRKD2 protected cancer cells from the apoptotic effects of HSP90 abrogation, restoring blood vessel formation in two preclinical models of solid tumors. Mechanistic studies revealed that PRKD2 is essential for hypoxia-induced accumulation of hypoxia-inducible factor-1? (HIF1?) and activation of NF-?B in tumor cells. Notably, ectopic expression of PRKD2 was able to partially restore HIF1? and secreted VEGF-A levels in hypoxic cancer cells treated with HSP90 inhibitors. Taken together, our findings indicate that signals from hypoxia and HSP90 pathways are interconnected and funneled by PRKD2 into the NF-?B/VEGF-A signaling axis to promote tumor angiogenesis and tumor growth. äHSP90 Supports Tumor Growth and Angiogenesis through PRKD2 Protein Sta(epmc).pdf DeepDyve Pubget Overpricing