Intra-renal transfection of heat shock protein 90 alpha or beta (Hsp90  or Hsp90 ) protects against ischemia/reperfusion injury

Barrera‐Chimal, Jonatan; Pérez‐Villalva, Rosalba; Ortega, Juan Antonio; Uribe, Norma; Gamba, Gerardo; Cortés‐González, Cesar; Bobadilla, Norma A.

doi:10.1093/ndt/gft415

Cited by 17 publications

(21 citation statements)

References 58 publications

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“…The intrarenal transfection of HSP90 protects against the renal damage induced by ischemia/reperfusion. Rats subjected to ischemia/reperfusion and transfected with HSP90 showed preservation of the tubular epithelium and no reduction in renal blood flow and abnormal proteinuria (Barrera-Chimal et al 2014). Tanaka et al (2013) showed that HSP90 inhibitor 17dimethylaminoethylaminogeldanamycin (17-DMAG) significantly suppressed the proliferation of human aortic endothelial cells induced by anti-HLA IgG.…”

Section: Prospects Of Hsp Therapymentioning

confidence: 99%

Heat shock proteins and kidney disease: perspectives of HSP therapy

Chebotareva

Bobkova

Shilov

2017

Cell Stress and Chaperones

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Heat shock proteins (HSPs) mediate a diverse range of cellular functions, prominently including folding and regulatory processes of cellular repair. A major property of these remarkable proteins, dependent on intracellular or extracellular location, is their capacity for immunoregulation that optimizes immune activity while avoiding hyperactivated inflammation. In this review, recent investigations are described, which examine roles of HSPs in protection of kidney tissue from various traumatic influences and demonstrate their potential for clinical management of nephritic disease. The HSP70 class is particularly attractive in this respect due to its multiple protective effects. The review also summarizes current understanding of HSP bioactivity in the pathophysiology of various kidney diseases, including acute kidney injury, diabetic nephropathy, chronic glomerulonephritis, and lupus nephritis-along with other promising strategies for their remediation, such as DNA vaccination.

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Section: Prospects Of Hsp Therapymentioning

confidence: 99%

Heat shock proteins and kidney disease: perspectives of HSP therapy

Chebotareva

Bobkova

Shilov

2017

Cell Stress and Chaperones

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“…Among these transfection methods, naked plasmid DNA (pDNA) is safe and simple to use, but there are few transfection methods using pDNA because of the complexity of the renal structure and lack of specific ligands (Mukai et al, 2008;Barrera-Chimal et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Characterization of transgene expression and pDNA distribution of the suctioned kidney in mice

et al. 2017

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We have previously developed an efficient and safe transfection method for the kidney in mice: renal suction-mediated transfection. In this study, we verified the detailed characteristics of transgene expression and plasmid DNA (pDNA) in mice to develop therapeutic strategies and application to gene function analysis in the kidney. After naked pDNA was administered intravenously, the right kidney was immediately suctioned by a tissue suction device. We examined the spatial distribution of transgene expression and pDNA in the suctioned kidney using tissue clearing by CUBIC, Clear T2 , and Scale SQ reagents. Spatial distribution analysis showed that pDNA was transfected into extravascular cells and sufficiently delivered to the deep renal cortex. In addition, we revealed that transgene expression occurred mainly in peritubular fibroblasts of the suctioned kidney by tissue clearing and immunohistochemistry. Next, we confirmed the periods of pDNA uptake and activation of transcription factors nuclear factor-jB and activator protein 1 by luciferase assays. Moreover, the use of a pCpG-free plasmid enabled sustained transgene expression in the suctioned kidney. In conclusion, analyses of the spatial distribution and immunostaining of the section suggest that pDNA and transgene expression occurs mainly in peritubular fibroblasts of the suctioned kidney. In addition, we clarified some factors for efficient and/or sustained transgene expression in the suctioned kidney.ARTICLE HISTORY

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“…To date, the precise site of interaction with the G-protein subunits with HSP90 remains to be determined. In the normal kidney, HSP90 is expressed at a low level (Barrera-Chimal et al, 2014 ; Smithline et al, 2014 ), and can be detected in the distal tubule and collecting duct epithelial cells (Satoh et al, 1994 ), which are common sites of Gα 12 subunit localization (Zheng et al, 2003 ; Boucher et al, 2012 ). Under normal conditions, HSP90 acts as a surveillance system to ensure proper conformational protein production and function, and its expression is induced during cellular stress (Burrows et al, 2004 ; Whitesell and Lin, 2012 ).…”

Section: Types Of Accessory Proteins In the Normal Kidneymentioning

confidence: 99%

“…Pharmacological inhibition of HSP90 reduced the tubular epithelial cell damage following ischemia-reperfusion injury, and was associated with an induction of other heat shock protein 70 and 27, which can activate cytoprotective pathways (Harrison et al, 2008 ). Conversely, over-expression of HSP90α/β in the kidney was partially effective in reducing tubular epithelial cell injury following ischemia-reperfusion injury, which was associated with the re-establishment in the coupling of endothelial nitric oxide synthase (eNOS) (Barrera-Chimal et al, 2014 ). To date, the role by which G-protein signaling through the dimeric interaction between HSP90 and Gα 12 or Gβγ subunits to control epithelial cell damage and recovery following AKI needs further investigation.…”

Section: Accessory Proteins In Kidney Injury and Diseasementioning

confidence: 99%

Accessory proteins for heterotrimeric G-proteins in the kidney

Park

2015

Front. Physiol.

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Heterotrimeric G-proteins play a fundamentally important role in regulating signal transduction pathways in the kidney. Accessory proteins are being identified as direct binding partners for heterotrimeric G-protein α or βγ subunits to promote more diverse mechanisms by which G-protein signaling is controlled. In some instances, accessory proteins can modulate the signaling magnitude, localization, and duration following the activation of cell membrane-associated receptors. Alternatively, accessory proteins complexed with their G-protein α or βγ subunits can promote non-canonical models of signaling activity within the cell. In this review, we will highlight the expression profile, localization and functional importance of these newly identified accessory proteins to control the function of select G-protein subunits under normal and various disease conditions observed in the kidney.

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Intra-renal transfection of heat shock protein 90 alpha or beta (Hsp90 or Hsp90 ) protects against ischemia/reperfusion injury

Abstract: Here we showed that eNOS-Hsp90 uncoupling plays a critical role in promoting NO reduction during IR. This effect was effectively reversed through Hsp90α or Hsp90β intra-renal transfection, suggesting their implication in regulating NO/eNOS pathway and the renal vascular tone.

Cited by 17 publications

References 58 publications

Heat shock proteins and kidney disease: perspectives of HSP therapy

Heat shock proteins and kidney disease: perspectives of HSP therapy

Characterization of transgene expression and pDNA distribution of the suctioned kidney in mice

Accessory proteins for heterotrimeric G-proteins in the kidney

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