Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 한기환 | * |
dc.date.accessioned | 2016-08-28T10:08:45Z | - |
dc.date.available | 2016-08-28T10:08:45Z | - |
dc.date.issued | 2013 | * |
dc.identifier.issn | 0363-6127 | * |
dc.identifier.other | OAK-9954 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/223607 | - |
dc.description.abstract | It has been reported that several proteins [heat shock protein 70 (Hsp70 and Hsc70), annexin II, and tropomyosin 5b] interact with the Ser256 residue on the COOH terminus of aquaporin-2 (AQP2), where vasopressin-induced phosphorylation occurs for mediating AQP2 trafficking. However, it remains unknown whether these proteins, particularly Hsp70, play a role in AQP2 trafficking. Semiquantitative immunoblotting revealed that renal expression of AQP2 and Hsp70 was significantly increased in water-restricted or dDAVP-infused rats. In silico analysis of the 5′-flanking regions of AQP2, Hsp70-1, and Hsp70-2 genes revealed that transcriptional regulator binding elements associated with cAMP response were identified at both the Hsp70-1 and Hsp70-2 promoter regions, in addition to AQP2. Luciferase reporter assay demonstrated the significant increase of luminescence after dDAVP stimulation (10-8 M, 6 h) in the LLC-PK1 cells transfected with luciferase vector containing 1 kb of the 5′-flanking region of Hsp70-2 gene. Hsp70-2 protein expression was also increased in mpkCCDc14 cells treated by dDAVP in a concentration-dependent manner. Cell surface biotinylation analysis demonstrated that forskolin (10-5 M, 15 min)-induced AQP2 targeting to the apical plasma membrane was significantly attenuated in the mpkCCDc14 cells with Hsp70-2 knockdown. Moreover, forskolin-induced AQP2 phosphorylation (Ser256) was not significantly induced in the mpkCCDc14 cells with Hsp70-2 knockdown. In contrast, Hsp70-2 knockdown did not affect the dDAVP-induced AQP2 abundance. In addition, siRNA-directed knockdown of Hsp70 significantly decreased cell viability. The results suggest that Hsp70 is likely to play a role in AQP2 trafficking to the apical plasma membrane, partly through affecting AQP2 phosphorylation at Ser256 and cell viability. © 2013 the American Physiological Society. | * |
dc.language | English | * |
dc.title | The role of 70-kDa heat shock protein in dDAVP-induced AQP2 trafficking in kidney collecting duct cells | * |
dc.type | Article | * |
dc.relation.issue | 7 | * |
dc.relation.volume | 304 | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | F958 | * |
dc.relation.lastpage | F971 | * |
dc.relation.journaltitle | American Journal of Physiology - Renal Physiology | * |
dc.identifier.doi | 10.1152/ajprenal.00469.2012 | * |
dc.identifier.wosid | WOS:000317003200013 | * |
dc.identifier.scopusid | 2-s2.0-84878236750 | * |
dc.author.google | Park E.-J. | * |
dc.author.google | Lim J.-S. | * |
dc.author.google | Jung H.J. | * |
dc.author.google | Kim E. | * |
dc.author.google | Han K.-H. | * |
dc.author.google | Kwon T.-H. | * |
dc.contributor.scopusid | 한기환(14622504200) | * |
dc.date.modifydate | 20240123095704 | * |