Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration

Itoh, Hideaki; Komatsuda, Atsushi; Oda, Hiroshi; Wakui, Hideki; Imai, Hirokazu; Sawada, Kenichi; Otaka, Michiro; Ogura, Mariko; Suzuki, Akira; Hamada, Fumio

doi:10.1046/j.1432-1033.2002.03317.x

Cited by 100 publications

(68 citation statements)

References 28 publications

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“…They were then cut into small pieces and homogenized with protein extraction buffer. Subcellular fractions were extracted as described elsewhere (Itoh et al 2002).…”

Section: Subcellular Fractionationsmentioning

confidence: 99%

Localization of the Sulphonylurea Receptor Subunits, SUR2A and SUR2B, in Rat Renal Tubular Epithelium

Zhou

Tanaka

et al. 2008

Tohoku J. Exp. Med.

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ATP-sensitive K + (K ATP ) channels in the kidney are considered to play roles in regulating membrane potential according to changes in the intracellular ATP concentration. They are composed of two types of subunits; the pore subunits (Kir6.1, Kir6.2), which are members of the inwardly rectifying K + channel family, and the regulatory subunits, the sulphonylurea receptors, which belong to the ATP-binding cassette (ABC) superfamily. The sulphonylurea receptors (SURs) are receptors of sulphonylureas widely used for the treatment of type 2 diabetes mellitus. The SURs are divided into two isoforms, SUR1 and SUR2, the latter was further divided into SUR2A and SUR2B. In the present study, we have investigated the mRNA expression by RT-PCR assay, and protein expression profi les by immunoblotting, immunohistochemistry, and immunoelectron microscopy with anti SUR2A and anti SUR2B antibodies. RT-PCR detected the presence of mRNA transcripts of the SUR2A and SUR2B, while SUR1 mRNA was barely detected. In immunoblotting, SUR2A protein was detected distinctly in the microsomal fraction, weakly in the mitochondrial fraction and at negligible level in the cell membrane fraction. In contrast, the SUR2B protein was detected intensely in the microsomal fraction, with a low level in the mitochondrial fraction and scarcely in the cell membrane fraction. In immunohistochemistry SUR2A and SUR2B proteins were widely distributed in renal tubular epithelial cells, glomerular mesangial cells, and the endothelium and the smooth muscle of blood vessels. In immunoelectron microscopy, the immunoreactivity was localized in the endoplasmic reticulum and mitochondria throughout the epithelial cells for SUR2A, and dominantly in the apical cytoplasm of the cells for SUR2B. In conclusion, the regulatory subunits of the K ATP channel in the rat kidney are SUR2A and SUR2B; they also are candidate regulatory subunits for the mitochondrial K ATP channel.ATP-sensitive K + channel; sulphonylurea receptor; immunohistochemistry; immunoelectron microscopy; kidney.Tohoku

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“…They were then cut into small pieces and homogenized with protein extraction buffer. Subcellular fractions were extracted as described elsewhere (Itoh et al 2002).…”

Section: Subcellular Fractionationsmentioning

confidence: 99%

Localization of the Sulphonylurea Receptor Subunits, SUR2A and SUR2B, in Rat Renal Tubular Epithelium

Zhou

Tanaka

et al. 2008

Tohoku J. Exp. Med.

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“…In these cells we analyzed the expression of two heat shock protein genes, HSP60 and HSP75, at both basal and heat stress conditions. HSP60 (Cpn60) and HSP75 (TRAP1) are mitochondrial chaperones that assist, in both stressed and non-stressed cells, in the folding, unfolding, or disaggregating of proteins either imported from the cytosol or synthesized within mitochondria (HSP60) (Cheng et al 1989;Frydman 2001;Itoh et al 2002;Saibil 2008) and in the reallocation of cytosolic protein into mitochondria (HSP75) (Felts et al 2000;Mokranjac and Neupert 2005). In addition to its chaperone activity, HSP60 has welldocumented anti-or pro-apoptotic roles (Arya et al 2007;Chandra et al 2007) as well as immunoregulatory properties (Habich and Burkart 2007;Pockley et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial DNA variability modulates mRNA and intra-mitochondrial protein levels of HSP60 and HSP75: experimental evidence from cybrid lines

Bellizzi

Taverna

D’Aquila

et al. 2009

Cell Stress and Chaperones

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To explore possible relationships between mitochondrial DNA (mtDNA) polymorphism and the expression levels of stress-responder nuclear genes we assembled five cybrid cell lines by repopulating 143B.TK − cells, depleted of their own mtDNA (Rho 0 cells), with foreign mitochondria with different mtDNA sequences (lines H, J, T, U, X). We evaluated, at both basal and under heat stress conditions, gene expression (mRNA) and intra-mitochondrial protein levels of HSP60 and HSP75, two key components in cellular stress response. At basal conditions, the levels of HSP60 and HSP75 mRNA were lower in one cybrid (H) than in the others (p=0.005 and p=0.001, respectively). Under stress conditions, the H line over-expressed both genes, so that the inter-cybrid difference was abolished. Moreover, the HSP60 intra-mitochondrial protein levels differed among the cybrid lines (p=0.001), with levels higher in H than in the other cybrid lines. On the whole, our results provide further experimental evidence that mtDNA variability influences the cell response to stressful conditions by modulating components involved in this response. Sentence summary of the article: the results reported in the present study provide important experimental evidence that in human cells mtDNA variability is able to influence the cellular response to heat stress by modulating both the transcription of genes involved in this response and their intra-mitochondrial protein levels.

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“…35 HSPD1 or HSP60 plays a key role in preventing apoptosis as well as immune response. 36 Expression of HSPD1 increases in dry eye. 37 Differential gene expression of HSPD1 in retinoblastoma compared to normal retina is reported.…”

Section: Discussionmentioning

confidence: 99%

Diabetic Retinopathy and Laser Therapy in Rats: A Protein-Protein Interaction Network Analysis

et al. 2017

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Introduction: Diabetic retinopathy (DR) is a serious microvascular complication of diabetes which can cause vision loss or blindness ultimately. Non enzymatic glycation of proteins leads to advanced glycation end products (AGEs) in DR. Since laser therapy is a well-established method, in this study, protein-protein interaction (PPI) network is applied for protein targets in DR disease in rats treated by laser. Methods: In this study, we focused on articles that investigated and compared the proteome profiles of DR rats with healthy control and also DR rats before and after laser therapy. The networks of related differentially expressed proteins were explored using Cytoscape version 3.3.0, the PPI analysis methods and ClueGO. Results: Analysis of PPI network of 37 related proteins to DR rats including 108 nodes, introduced 10 hub-bottleneck proteins and 5 concerned biochemical pathways. On the other hand, PPI analysis of related proteins to DR rats before and after laser therapy corresponded to 33 proteins and 2 biological pathways. Discussion: Centrality and cluster screening identified hub-bottelneck genes, including Aldoa, HSPD1, Pgam2, Mapk3, SLC2A4, Ctnnb1, Ywhab, HSPA8, GAPDH and Actb for DR rats versus healthy control and ENO1, Aldoa, GAPDH for DR samples after laser therapy. Conclusion: Gene expression analysis of the DR samples treated via laser therapy provides a molecular evidence in support of the therapeutic effect of laser.

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Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration

Cited by 100 publications

References 28 publications

Localization of the Sulphonylurea Receptor Subunits, SUR2A and SUR2B, in Rat Renal Tubular Epithelium

Localization of the Sulphonylurea Receptor Subunits, SUR2A and SUR2B, in Rat Renal Tubular Epithelium

Mitochondrial DNA variability modulates mRNA and intra-mitochondrial protein levels of HSP60 and HSP75: experimental evidence from cybrid lines

Diabetic Retinopathy and Laser Therapy in Rats: A Protein-Protein Interaction Network Analysis

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