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10.1016/j.tox.2018.01.006 http://scihub22266oqcxt.onion/10.1016/j.tox.2018.01.006 29355601!ä!29355601 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       Toxicology 2018 ; 395 (ä): 45-53 Nephropedia Template TP {{tp|p=29355601|t=2018. Nickel ions bind to HSP90beta and enhance HIF-1alpha-mediated IL-8 expression |pdf=|usr=}}{{29355601}} gab.com Text Nickel ions bind to HSP90beta and enhance HIF-1alpha-mediated IL-8 expression JO: Toxicology http://www.kidney.de/pget.php?&tw=1&pmid=29355601 #FOAvip Nickel ions (Ni(2+)) eluted from biomedical devices cause inflammation and Ni allergy. Although Ni(2+) and Co(2+) elicit common effects, Ni(2+) induces a generally stronger inflammatory reaction. However, the molecular mechanism by which Ni(2+) and Co(2+) induce such different responses remains to be elucidated. In the present study, we compared the effects of Ni(2+) and Co(2+) on the expression of interleukin (IL)-8 in human monocyte THP-1 cells. We report that NiCl(2) but not CoCl(2) induced the expression of IL-8; in contrast, CoCl(2) elicited a higher expression of hypoxia-inducible factor-1alpha (HIF-1alpha). The NiCl(2)-induced expression of IL-8 in late phase was blocked by a HIF-1alpha inhibitor, PX-478, indicating that NiCl(2) targets additional factors responsible for activating HIF-1alpha. To identify such targets, proteins that bound preferentially to Ni-NTA beads were analyzed by LC/MS/MS. The analysis yielded heat shock protein 90beta (HSP90beta) as a possible candidate. Furthermore, Ni(2+) reduced the interaction of HSP90beta with HIF-1alpha, and instead promoted the interaction between HIF-1alpha and HIF-1beta, as well as the nuclear localization of HIF-1alpha. Using various deletion variants, we showed that Ni(2+) could bind to the linker domain on HSP90beta. These results suggest that HSP90beta plays important roles in Ni(2+)-induced production of IL-8 and could be a potential target for the regulation of Ni(2+)-induced inflammation. Twit Text FOAVip Nickel ions bind to HSP90beta and enhance HIF-1alpha-mediated IL-8 expression ????Toxicology http://www.kidney.de/pget.php?&tw=1&pmid=29355601 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29355601 #FOAvip English Wikipedia <ref>{{Cite pmid|29355601}}</ref> Nickel ions bind to HSP90beta and enhance HIF-1alpha-mediated IL-8 expression #MMPMID29355601 Asakawa S; Onodera R; Kasai K; Kishimoto Y; Sato T; Segawa R; Mizuno N; Ogasawara K; Moriya T; Hiratsuka M; Hirasawa N Toxicology 2018[Feb]; 395 (ä): 45-53 PMID29355601show ga Nickel ions (Ni(2+)) eluted from biomedical devices cause inflammation and Ni allergy. Although Ni(2+) and Co(2+) elicit common effects, Ni(2+) induces a generally stronger inflammatory reaction. However, the molecular mechanism by which Ni(2+) and Co(2+) induce such different responses remains to be elucidated. In the present study, we compared the effects of Ni(2+) and Co(2+) on the expression of interleukin (IL)-8 in human monocyte THP-1 cells. We report that NiCl(2) but not CoCl(2) induced the expression of IL-8; in contrast, CoCl(2) elicited a higher expression of hypoxia-inducible factor-1alpha (HIF-1alpha). The NiCl(2)-induced expression of IL-8 in late phase was blocked by a HIF-1alpha inhibitor, PX-478, indicating that NiCl(2) targets additional factors responsible for activating HIF-1alpha. To identify such targets, proteins that bound preferentially to Ni-NTA beads were analyzed by LC/MS/MS. The analysis yielded heat shock protein 90beta (HSP90beta) as a possible candidate. Furthermore, Ni(2+) reduced the interaction of HSP90beta with HIF-1alpha, and instead promoted the interaction between HIF-1alpha and HIF-1beta, as well as the nuclear localization of HIF-1alpha. Using various deletion variants, we showed that Ni(2+) could bind to the linker domain on HSP90beta. These results suggest that HSP90beta plays important roles in Ni(2+)-induced production of IL-8 and could be a potential target for the regulation of Ni(2+)-induced inflammation. |Cell Line[MESH] |Cell Nucleus/drug effects/metabolism[MESH] |Cobalt/metabolism/pharmacology[MESH] |HSP90 Heat-Shock Proteins/drug effects/*metabolism[MESH] |Humans[MESH] |Hypoxia-Inducible Factor 1, alpha Subunit/antagonists & inhibitors/drug effects/*metabolism[MESH] |Interleukin-8/*biosynthesis[MESH] |Monocytes/metabolism[MESH] |Mustard Compounds/pharmacology[MESH] |Nickel/*metabolism/*pharmacology[MESH] |Phenylpropionates/pharmacology[MESH] |Protein Binding[MESH]Nickel ions bind to HSP90beta and enhance HIF-1alpha-mediated IL-8 exp(epmc).pdf DeepDyve Pubget Overpricing