Mercury, cadmium, and arsenite enhance heat shock protein synthesis in chick embryos prior to embryotoxicity

Papaconstantinou, Andriana D.; Brown, Ken M.; Noren, Bradley T.; Mcalister, Terence; Fisher, Benjamin R.; Goering, Peter L.

doi:10.1002/bdrb.10044

Cited by 53 publications

(29 citation statements)

References 45 publications

(54 reference statements)

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“…For example, it is known that in the chick embryo, the induced protein expression patterns are depending on the kind of heavy metal used for the assay [36]. In the sea urchin embryo subacute/sublethal cadmium concentrations are also able to enhance the expression of the metallothionein gene, as demonstrated in our previous paper [19].…”

Section: Discussionmentioning

confidence: 79%

Cadmium induces the expression of specific stress proteins in sea urchin embryos

Roccheri

Agnello

Bonaventura

et al. 2004

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 79%

Cadmium induces the expression of specific stress proteins in sea urchin embryos

Roccheri

Agnello

Bonaventura

et al. 2004

Biochemical and Biophysical Research Communications

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“…In mammalian systems, Cd exposure has been found to induce stress proteins of 72 and 90·kDa in human keratinocytes and in fibroblasts, 70 and 90·kDa in primary rat hepatocytes, and 32, 72, 90 and 110·kDa in human melanoma cells (Bauman et al, 1993;Madden et al, 2002;Urani et al, 2005). In chick embryos, exposure to Cd enhanced de novo synthesis of HSP70, whereas HSP24 and HSP90 were unaffected (Papaconstantinou et al, 2003). Data for the Cd-induced chaperone response in aquatic organisms are limited.…”

Section: Discussionmentioning

confidence: 99%

Effects of cadmium on cellular protein and glutathione synthesis and expression of stress proteins in eastern oysters, Crassostrea virginica Gmelin

Ivanina

Cherkasov

Sokolova

2008

Journal of Experimental Biology

134

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SUMMARYCadmium (Cd) is an important toxicant in estuarine and coastal environments that can strongly affect energy balance of aquatic organisms by increasing the organismʼs basal energy demand and reducing its aerobic capacity. Mechanisms of cadmiuminduced increase in basal metabolic costs are not well understood and may involve elevated detoxification costs due to the synthesis of cellular protective proteins and glutathione. We studied the short-term effects of cadmium exposure (4·h) on protein and glutathione (GSH) synthesis and expression of stress proteins (heat shock proteins HSP60, HSP70 and HSP90) and metallothioneins in isolated gill and hepatopancreas cells of the eastern oyster, Crassostrea virginica. Our study showed that exposure to cadmium resulted in a dose-dependent increase in the rate of protein synthesis in oyster cells, which reached 150% of the control at the highest tested Cd level (2000·mol·l -1 ). GSH synthesis was significantly inhibited by the highest Cd concentrations, especially in hepatopancreas, which resulted in a slight but significant decrease in the total GSH concentrations. Elevated protein synthesis was associated with the increased expression of metallothioneins and heat shock proteins. Interestingly, stress protein response differed considerably between gill and hepatopancreas cells. In hepatopancreas, expression of metallothionein mRNA (measured by real-time PCR) increased 2-8-fold in response to Cd exposure, whereas no significant increase in metallothionein expression was found in Cd-exposed gill cells. By contrast, HSP60 and HSP70 protein levels increased significantly in Cd-exposed gill cells (by 1.5-2-fold) but not in hepatopancreas. No change in HSP90 expression was detected in response to Cd exposure in oyster cells. These data indicate that metallothionein expression may provide sufficient protection against Cd-induced damage to intracellular proteins in hepatopancreas, alleviating the need for overexpression of molecular chaperones. By contrast, Cd detoxification mechanisms such as inducible metallothioneins and GSH appear to be insufficient to fully prevent protein damage in gill cells, thus necessitating induction of HSPs as a secondary line of cellular defense. Therefore, gills are likely to be among the most Cd-sensitive tissues in oysters, which may have important implications for impaired oxygen uptake contributing to energy misbalance and reduced aerobic scope in Cd-exposed oysters.

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“…Tab. 1 lists the members of each family, their locations, and functions in the cell [20][21][22][23].…”

Section: Heat Shock Proteinsmentioning

confidence: 99%

Inducible heat shock protein 70 kD and inducible nitric oxide synthase in hemorrhage/resuscitation-induced injury

Kiang

2004

Cell Res

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Inducible heat shock protein 70 kD (HSP-70i) has been shown to protect cells, tissues, and organs from harmful assaults in in vivo and in vitro experimental models. Hemorrhagic shock followed by resuscitation is the principal cause of death among trauma patients and soldiers in the battlefield. Although the underlying mechanisms are still not fully understood, it has been shown that nitric oxide (NO) overproduction and inducible nitric oxide synthase (iNOS) overexpression play important roles in producing injury caused by hemorrhagic shock including increases in polymorphonuclear neutrophils (PMN) infiltration to injured tissues and leukotriene B 4 (LTB 4 ) generation. Moreover, transcription factors responsible for iNOS expression are also altered by hemorrhage and resuscitation. It has been evident that either up-regulation of HSP-70i or down-regulation of iNOS can limit tissue injury caused by ischemia/reperfusion or hemorrhage/resuscitation. In our laboratory, geldanamycin, a member of ansamycin family, has been shown to induce HSP70i overexpression and then subsequently to inhibit iNOS expression, to reduce cellular caspase-3 activity, and to preserve cellular ATP levels. HSP-70i is found to couple to iNOS and its transcription factor. Therefore, the complex formation between HSP-70i and iNOS may be a novel mechanism for protection from hemorrhage/resuscitation-induced injury.

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Mercury, cadmium, and arsenite enhance heat shock protein synthesis in chick embryos prior to embryotoxicity

Abstract: The data support metal-induced developmental abnormalities, which are preceded by synthesis of stress proteins.

Cited by 53 publications

References 45 publications

Cadmium induces the expression of specific stress proteins in sea urchin embryos

Cadmium induces the expression of specific stress proteins in sea urchin embryos

Effects of cadmium on cellular protein and glutathione synthesis and expression of stress proteins in eastern oysters, Crassostrea virginica Gmelin

Inducible heat shock protein 70 kD and inducible nitric oxide synthase in hemorrhage/resuscitation-induced injury

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