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10.1016/j.yexcr.2017.02.004 http://scihub22266oqcxt.onion/10.1016/j.yexcr.2017.02.004 28185835!ä!28185835 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Exp+Cell+Res 2017 ; 352 (2): 225-233 Nephropedia Template TP {{tp|p=28185835|t=2017. Requirement of Hsp105 in CoCl(2)-induced HIF-1alpha accumulation and transcriptional activation |pdf=|usr=}}{{28185835}} gab.com Text Requirement of Hsp105 in CoCl(2)-induced HIF-1alpha accumulation and transcriptional activation JO: Exp Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=28185835 #FOAvip The mammalian stress protein Hsp105alpha protects cells from stress conditions. Several studies have indicated that Hsp105alpha is overexpressed in many types of solid tumors, which contain hypoxic microenvironments. However, the role of Hsp105alpha in hypoxic tumors remains largely unknown. We herein demonstrated the involvement of Hsp105alpha in HIF-1 functions induced by the hypoxia-mimetic agent CoCl(2). While Hsp105alpha is mainly localized in the cytoplasm under normal conditions, a treatment with CoCl(2) induces the nuclear localization of Hsp105alpha, which correlated with HIF-1alpha expression levels. The overexpression of degradation-resistant HIF-1alpha enhances the nuclear localization of Hsp105alpha without the CoCl(2) treatment. The CoCl(2)-dependent transcriptional activation of HIF-1, which is measured using a reporter gene containing a HIF-responsive element, is reduced by the knockdown of Hsp105alpha. Furthermore, the CoCl(2)-induced accumulation of HIF-1alpha is enhanced by heat shock, which results in the nuclear localization of Hsp105, and is suppressed by the knockdown of Hsp105. Hsp105 associates with HIF-1alpha in CoCl(2)-treated cells. These results suggest that Hsp105alpha plays an important role in the functions of HIF-1 under hypoxic conditions, in which Hsp105alpha enhances the accumulation and transcriptional activity of HIF-1 through the HIF-1alpha-mediated nuclear localization of Hsp105alpha. Twit Text FOAVip Requirement of Hsp105 in CoCl(2)-induced HIF-1alpha accumulation and transcriptional activation ????Exp Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=28185835 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28185835 #FOAvip English Wikipedia <ref>{{Cite pmid|28185835}}</ref> Requirement of Hsp105 in CoCl(2)-induced HIF-1alpha accumulation and transcriptional activation #MMPMID28185835 Mikami H; Saito Y; Okamoto N; Kakihana A; Kuga T; Nakayama Y Exp Cell Res 2017[Mar]; 352 (2): 225-233 PMID28185835show ga The mammalian stress protein Hsp105alpha protects cells from stress conditions. Several studies have indicated that Hsp105alpha is overexpressed in many types of solid tumors, which contain hypoxic microenvironments. However, the role of Hsp105alpha in hypoxic tumors remains largely unknown. We herein demonstrated the involvement of Hsp105alpha in HIF-1 functions induced by the hypoxia-mimetic agent CoCl(2). While Hsp105alpha is mainly localized in the cytoplasm under normal conditions, a treatment with CoCl(2) induces the nuclear localization of Hsp105alpha, which correlated with HIF-1alpha expression levels. The overexpression of degradation-resistant HIF-1alpha enhances the nuclear localization of Hsp105alpha without the CoCl(2) treatment. The CoCl(2)-dependent transcriptional activation of HIF-1, which is measured using a reporter gene containing a HIF-responsive element, is reduced by the knockdown of Hsp105alpha. Furthermore, the CoCl(2)-induced accumulation of HIF-1alpha is enhanced by heat shock, which results in the nuclear localization of Hsp105, and is suppressed by the knockdown of Hsp105. Hsp105 associates with HIF-1alpha in CoCl(2)-treated cells. These results suggest that Hsp105alpha plays an important role in the functions of HIF-1 under hypoxic conditions, in which Hsp105alpha enhances the accumulation and transcriptional activity of HIF-1 through the HIF-1alpha-mediated nuclear localization of Hsp105alpha. |*Transcriptional Activation[MESH] |Active Transport, Cell Nucleus[MESH] |Cell Hypoxia[MESH] |Cell Nucleus/*metabolism[MESH] |Cobalt/*toxicity[MESH] |HEK293 Cells[MESH] |HSP110 Heat-Shock Proteins/genetics/*metabolism[MESH] |HeLa Cells[MESH] |Heat-Shock Response[MESH] |Humans[MESH] |Hypoxia-Inducible Factor 1, alpha Subunit/genetics/*metabolism[MESH] |Protein Binding[MESH]Requirement of Hsp105 in CoCl(2)-induced HIF-1alpha accumulation and t(epmc).pdf DeepDyve Pubget Overpricing