Stress proteins as molecular biomarkers for environmental toxicology

Ryan, J. A.; Hightower, Lawrence E.

doi:10.1007/978-3-0348-9088-5_28

Cited by 92 publications

(68 citation statements)

References 16 publications

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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%

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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Section: Discussionmentioning

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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“…Of all the hsps, the hsp70 family has been most widely studied as a biomarker of stress because of its rapid and significant increase during cellular disruption (Ryan & Hightower 1996). One of the major inducing factors for hsp70 upregulation in the cell is the occurrence of damaged cellular proteins (Ananthan et al 1986) and the key role of hsp70 is to repair such proteins (Gething & Sambrook 1992).…”

Section: Discussionmentioning

confidence: 99%

“…Presently there is a paucity of data concerning the effect of pathogenic stress on hsps in fish and in this study the concerted expression profiles of the key hsp families, hsp90, hsp70 and hsp60, in fish infected with a pathogenic strain of V. alginolyticus is reported. Also, a comparison of effects of live V. alginolyticus and its ECP was studied.Of all the hsps, the hsp70 family has been most widely studied as a biomarker of stress because of its rapid and significant increase during cellular disruption (Ryan & Hightower 1996). One of the major inducing factors for hsp70 upregulation in the cell is the occurrence of damaged cellular proteins (Ananthan et al 1986) and the key role of hsp70 is to repair such proteins (Gething & Sambrook 1992).…”

mentioning

confidence: 99%

Modulated heat shock protein expression during pathogenic Vibrio alginolyticus stress of sea bream

Deane

Li²,

Woo³

2004

Dis. Aquat. Org.

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The effects of infective Vibrio alginolyticus and its extracellular product (ECP) on host fish function are not well understood. In this study a partial biochemical characterization of the ECP from an infective strain of V. alginolyticus isolated from diseased silver sea bream Sparus sarba was achieved and the effects of live V. alginolyticus and ECP on hepatic heat shock protein (hsp) expression was compared. The ECP fraction was found to contain several hydrolytic enzymes including both haemolytic and proteolytic activities. Intramuscular administration of ECP to sea bream resulted in vibriosis with similar pathological signs as those observed with live V. alginolyticus administration. Using quantitative immunoassays we assessed the levels of the major hsp families, hsp90, hsp70 and hsp60, in hepatic tissue of diseased sea bream between 12 and 48 h post-infection. Throughout the infective period, live V. alginolyticus did not alter hsp90 whereas ECP significantly reduced hepatic hsp90 during the late stages of acute infection. The levels of hsp70 were found to be rapidly and drastically increased with both live V. alginolyticus and ECP. The transcript levels of both gene members of the hsp70 family (hsc70 and hsp70) were significantly increased with both live V. alginolyticus and ECP. The levels of hsp60 remained unchanged with both live V. alginolyticus and ECP. The data presented in this study is the first report describing an effect of both live V. alginolytus and ECP on hsp expression in diseased fish.KEY WORDS: Fish · Disease · Vibrio · Heat shock protein · hsp90 · hsp70 · hsp60 Resale or republication not permitted without written consent of the publisherDis Aquat Org 62: [205][206][207][208][209][210][211][212][213][214][215] 2004 When normal cellular processes are adversely affected the synthesis of a group of proteins belonging to the heat shock protein (hsp) families (hsp90, hsp70 and hsp60) are rapidly increased. Members of these different hsp families play different roles in the cell; for example, the hsp90 family is involved in steroid receptor formation and protein folding (Smith & Toft 1993, Pratt 1997, the hsp70 family is necessary for protein synthesis, translocation and protein folding (Gething & Sambrook 1992), and mitochon-drial bound hsp60 is defined as being involved in protein stability and folding (Cheng et al. 1989, Ostermann et al. 1989, Martin et al. 1992. Indeed all of these groups of hsps have been demonstrated to be upregulated in fish during abiotic stress (Iwama et al. 1998). Evidence from mammalian studies has suggested that hsps are important during disease as they may play critical roles in immune function and protection (Jacquier-Sarlin et al. 1994), antigen presentation (DeNagel & Pierce 1993) and non-specific immune responses (Guzik et al. 1999). Although strong evidence exists for an important role of hsps in disease responses for mammals, much less is known about pathogenic stress and its effect on hsp90, 70 and 60 expression in fish. A better understanding...

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“…Extensive studies in this field revealed that virtually every other nonthermal stress could induce Hsps [31][32][33]. Owing to their responsiveness to diverse forms of stress, the stress proteins have undergone widespread application in biomonitoring and environmental toxicology [5,[34][35][36][37][38][39][40][41]. As members of the Hsp70 are often the prominent proteins to be expressed following environmental insults, these stress proteins are, therefore, very useful indicators of cellular aggression, and have been used to monitor the impact of environmental factors on various animal species [42][43][44][45] as well as in in vitro models [28,37,41,46,47].…”

Section: Hsp70 In Environmental Monitoringmentioning

confidence: 99%

“…A few studies in recent years have correlated the expression of hsp70 with known toxicological endpoints [51][52][53]. The efficiency of hsp70 expression as biomarker of environmental pollution has been advocated by many researchers [36,51,[54][55][56][57][58][59]. Recently a number of studies have been made to include more and more environmental pollutants to validate the above hypothesis.…”

Section: Hsp70 In Environmental Monitoringmentioning

confidence: 99%

Heat shock response: hsp70 in environmental monitoring

Mukhopadhyay

Nazir

Saxena

et al. 2003

J Biochem & Molecular Tox

146

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Heat shock proteins (Hsps) are a ubiquitous feature of cells in which these proteins cope with stress-induced denaturation of other proteins. Among the different families of Hsps, the 70 kDa family (hsp70) is the most highly conserved and has been most extensively studied. Apart from their primary role in cellular defense under stress condition, a number of studies in recent years have shown the immense potential of hsp70 in pollution monitoring using even transgenic approach both in vivo and in vitro. This article reviews the recent developments in the widespread application of hsp70 in environmental risk assessment. C

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Stress proteins as molecular biomarkers for environmental toxicology

Cited by 92 publications

References 16 publications

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

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

Modulated heat shock protein expression during pathogenic Vibrio alginolyticus stress of sea bream

Heat shock response: hsp70 in environmental monitoring

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