Molecular characterization, gene expression and transcriptional regulation of cytosolic HSP90 genes in the flatfish Senegalese sole (Solea senegalensis Kaup)

Manchado, Manuel; Salas-Leiton, Emilio; Infante, Carlos; Ponce, Marian; Asensio, Esther; Crespo, Aniela; Zuasti, Eugenia; Cañavate, José Pedro

doi:10.1016/j.gene.2008.03.007

Cited by 95 publications

(52 citation statements)

References 44 publications

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“…Scale bar 400 μm hsp90 in planarianssituations. The transcriptional up-regulation of Djhsp90 is consistent with that observed in a variety of organisms after exposition to different stressors (Farcy et al 2007;Gao et al 2007;Lei et al 2009;Li et al 2009a;Manchado et al 2008;Tokalov et al 2007;Zhang et al 2009) and indicates that this gene encodes an inducible HSP90 form. To assess the function of Djhsp90 in intestinal cells, we used RNA interference (RNAi).…”

Section: Characterization Of Djhsp90supporting

confidence: 83%

Expression of hsp90 mediates cytoprotective effects in the gastrodermis of planarians

Conte

Isolani

Deri

et al. 2011

Cell Stress and Chaperones

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Heat shock proteins (HSPs) play a crucial role in the protection of cells. In the present study, we have identified an hsp90-related gene (Djhsp90) encoding a cytosolic form of HSP90 that is primarily expressed in gastrodermis of the planarian Dugesia japonica. Djhsp90 becomes significantly induced after traumatic amputation or other stress stimuli, such as exposure to X-ray or ultraviolet radiations, heat shock, or prolonged starvation. When Djhsp90 is silenced by ribonucleic acid interference (RNAi), planarians dramatically decrease in size, becoming unable to eat, and die in a few weeks. Our results indicate that this gene plays an essential cytoprotective role in the gastrodermis of planarians and suggest that this chaperone can be involved in autophagic processes that are activated by this tissue.

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Section: Characterization Of Djhsp90supporting

confidence: 83%

Expression of hsp90 mediates cytoprotective effects in the gastrodermis of planarians

Conte

Isolani

Deri

et al. 2011

Cell Stress and Chaperones

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“…Heat shock proteins are often used as biomarkers in environmental toxicology (Ryan and Hightower, 1996), and HSP90 has been considered as a useful biomarker to assess the nutritional stress in early life stages of fish and as a defense mechanism against a great diversity of stressors such as heat shock, infections, or starvation (Cara et al, 2005;Manchado et al, 2008;Li et al, 2012). The possible biological function of MaHSP90 under stress response was further understood by investigating mRNA expression at different time points after acute nitrite exposure.…”

Section: Discussionmentioning

confidence: 99%

“…As an important member of the HSP family, HSP90 has recently received considerable attention in aquaculture research. To date, several HSP90s have been reported, and the expression level of the HSP90 gene has been investigated in fish species, such as miiuy croaker (Wei et al, 2013), mountain minnow , carp (Hermesz et al, 2001), senegalese sole (Manchado et al, 2008), and rainbow trout (Cara et al, 2005). However, investigations on the response of HSP90 gene at the functional level in teleost fish are lacking.…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression analysis of a heat shock protein 90 β isoform gene from the gills of Wuchang bream (Megalobrama amblycephala Yih) subjected to nitrite stress

Sun¹,

Zhu²,

Ge³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. Heat shock protein 90 (HSP90), a highly conserved and multi-functional molecular chaperone, plays an essential role in cellular metabolism and stress response. In this study, HSP90 cDNA named MaHSP90 was cloned from Wuchang bream (Megalobrama amblycephala) gills by using rapid amplification of cDNA ends. The fulllength MaHSP90 cDNA is 2674 bp and consists of a 3',5'-untranslated region and a 2250-bp open reading frame encoding a 750-amino acid long protein. Identity analysis revealed that the amino acid sequence of MaHSP90 is highly conserved. Homology analysis and structure comparison further indicated that MaHSP90 should be the β isoform member of the HSP90 family. MaHSP90 mRNA was ubiquitously expressed in the liver, heart, muscle, gill, intestine, kidney, and brain. The MaHSP90 mRNA levels under nitrite stress were analyzed using real-time quantitative reverse transcriptase-polymerase chain reaction (qRT-PCR); the mRNA levels significantly increased at 3, 6, and 12 h after nitrite exposure in the gills and then stabilized between 24 and 48 h. Furthermore, a similar relationship between mRNA expression (qRT-PCR) and HSP90 protein levels (densitometric band analysis) was found. Transcriptional analysis of caspase-8 and caspase-9 expression in the gills of juvenile M. amblycephala after a 48-h exposure to nitrite suggested that MaHSP90 expression is related positively with nitriteinduced apoptosis. Fish exposed to nitrite also showed gill damage. Our results suggest that MaHSP90 mRNA is constitutively expressed in various tissues and inducible in the gills under nitrite stress, suggesting its important role in nitrite stress response.

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“…Riba 2004;Costa et al 2009a, b;Oliva et al 2010). In addition, some successful attempts using ''omic'' approaches can already been found, although most also relate to aquaculture, such as transcription analysis by cDNA microarrays and PCR techniques (Manchado et al 2008;Osuna-Jiménez et al 2009;Prieto-Á lamo et al 2009 and a few others) and proteomics (Forné et al 2009;Salas-Leiton et al 2009;Costa et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Transcriptomic analyses in a benthic fish exposed to contaminated estuarine sediments through laboratory and in situ bioassays

et al. 2011

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The transcription of contaminant response-related genes was investigated in juvenile Senegalese soles exposed to sediments from three distinct sites (a reference plus two contaminated) of a Portuguese estuary (the Sado, W Portugal) through simultaneous 28-day laboratory and in situ bioassays. Transcription of cytochrome P450 1A (CYP1A), metallothionein 1 (MT1), glutathione peroxidase (GPx), catalase (CAT), caspase 3 (CASP3) and 90 kDa heat-shock protein alpha (HSP90AA) was surveyed in the liver by real-time PCR. CASP3 transcription analysis was complemented by surveying apoptosis through the TUNEL reaction. After 14 days of exposure, relative transcription was either reduced or decreased in fish exposed to the contaminated sediments, revealing a disturbance stress phase during which animals failed to respond to insult. After 28 days of exposure all genes' transcription responded to contamination but laboratory and in situ assays depicted distinct patterns of regulation. Although sediments revealed a combination of organic and inorganic toxicants, transcription of the CYP1A gene was consistently correlated to organic contaminants. Metallothionein regulation was found correlated to metallic and organic xenobiotic contamination in the laboratory and in situ, respectively. The transcription of oxidative stress-related genes can be a good indicator of general stress but caution is mandatory when interpreting the results since regulation may be influenced by multiple factors. As for MT1, HSP90 up-regulation has potential to be a good indicator for total contamination, as well as the CASP3 gene, even though hepatocyte apoptosis depicted values inconsistent with sediment contamination, showing that programmed cell death did not directly depend on caspase transcription alone.

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Molecular characterization, gene expression and transcriptional regulation of cytosolic HSP90 genes in the flatfish Senegalese sole (Solea senegalensis Kaup)

Cited by 95 publications

References 44 publications

Expression of hsp90 mediates cytoprotective effects in the gastrodermis of planarians

Expression of hsp90 mediates cytoprotective effects in the gastrodermis of planarians

Cloning and expression analysis of a heat shock protein 90 β isoform gene from the gills of Wuchang bream (Megalobrama amblycephala Yih) subjected to nitrite stress

Transcriptomic analyses in a benthic fish exposed to contaminated estuarine sediments through laboratory and in situ bioassays

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