Cellular responses to oxidative and osmotic stress

Mager, Willem H.; Boer, Albertus H. de; Siderius, Marco; Voss, Hans–Peter

doi:10.1379/1466-1268(2000)005<0073:crtoao>2.0.co;2

Cited by 43 publications

(24 citation statements)

References 7 publications

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“…One of the numerous classes of Hsps (named according to their apparent molecular mass) identified so far is Hsp70 with its members either constitutively expressed (Hsc70) or existing as stress-inducible forms (Hsp70) (Hartl and Hayer-Hartl, 2002). Hsp70 transcriptional upregulation is elicited primarily by heat (Scharf et al, 1998) but also by other stimuli including osmotic (Tirard et al, 1997) and oxidative stress (Mager et al, 2000) as well as metal ion concentration (Ryan and Hightower, 1994). Another family of proteins known to be induced by adverse environmental conditions (i.e.…”

Section: Introductionmentioning

confidence: 99%

Hyperthermia-induced Hsp70 and MT20 transcriptional upregulation are mediated by p38-MAPK and JNKs inMytilus galloprovincialis(Lamarck); a pro-survival response

Gourgou

Aggeli

Beis

et al. 2010

Journal of Experimental Biology

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SUMMARYIn the present study we investigated the signal transduction cascades triggered by acute thermal stress in Mytilus galloprovincialis gills. This particular species has been reported to exhibit a significant tolerance to high temperatures; thus, it was intriguing to examine the molecular mechanisms responsible for this extraordinary trait. In particular, exposure to 30°C was found to cause a significant and sustained stimulation of p38-MAPK phosphorylation while the activation profile of JNKs was transient and relatively moderate. We also observed that hyperthermia induced apoptosis as a delayed response, with both MAPK subfamilies rapidly translocating to the nucleus. The phosphorylation of cJun, ATF2 and NFB was detected next. Using selective inhibitors, phosphorylation of these transcription factors was established to be dependent on p38-MAPK or JNKs. Subsequently, potential changes in gene expression were assessed. In this context, hyperthermia resulted in the transcriptional upregulation of Hsp70 and MT20 genes with a widely known salutary effect, preserving mussel fitness and performance under adverse environmental conditions. Interestingly, p38-MAPK and JNKs were found to mediate the hyperthermia-induced Hsp70 and MT20 upregulation as well as the delayed induction of apoptosis under the interventions studied. Overall this is, to our knowledge, the first time that an insight into the compensatory survival 'programme' initiated in Mytilus galloprovincialis gills, contributing to this organism's exceptional tolerance to thermal stress, has been gained. In particular, we provide evidence demonstrating the principal role of p38-MAPK and JNKs in transducing the stress signal via mobilization of specific transcription factors and the transcriptional upregulation of cytoprotective genes.

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Section: Introductionmentioning

confidence: 99%

Hyperthermia-induced Hsp70 and MT20 transcriptional upregulation are mediated by p38-MAPK and JNKs inMytilus galloprovincialis(Lamarck); a pro-survival response

Gourgou

Aggeli

Beis

et al. 2010

Journal of Experimental Biology

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“…Stress factors include heat shock but also a number of chemical and physical stressors such as osmotic changes, oxygen radicals, anoxia, toxicants, etc., that are able to affect the tertiary structure of proteins with detrimental effects on cell homeostasis (Mager et al, 2000;Snyder et al, 2001). HSPs are classified into major families according to their molecular weight, e.g., HSP100, HSP90, HSP70, HSP27, etc.…”

Section: Introductionmentioning

confidence: 99%

Sequencing and expression pattern of inducible heat shock gene products in the European flat oyster, Ostrea edulis

Piano

Franzellitti

Tinti

et al. 2005

Gene

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“…The discovery of Hsps was consequent to heat exposure (Lindquist and Craig 1988), and heat does remain the prototypical stimulus eliciting their expression (Scharf et al 1998); however, many other stimuli are known to alter Hsp biosynthesis, such as osmotic (Tirard et al 1997) and oxidative stress (Mager et al 2000), hypoxia (Chang et al 2000), magnetic field (Lin et al 1997), and a number of other physical or chemical stressors (Snyder et al 2001). All these disturbances are known to affect the tertiary structure of proteins, and, therefore, are detrimental to cell homeostasis.…”

Section: Introductionmentioning

confidence: 99%

Expression of cytoprotective proteins, heat shock protein 70and metallothioneins, in tissues ofOstrea edulis exposed to heat andheavy metals

2004

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Heat shock proteins (Hsps) are constitutively expressed in cells and involved in protein folding, assembly, degradation, intracellular localization, etc, acting as molecular chaperones. However, their overexpression represents a ubiquitous molecular mechanism to cope with stress. Hsps are classified into families, and among them the Hsp70 family appears to be the most evolutionary preserved and distributed in animals. In this study, the expression of Hsp70 and the related messenger ribonucleic acid (mRNA) has been studied in Ostrea edulis after exposure to heat and heavy metals; moreover, levels of metallothioneins (MTs), another class of stress-induced proteins, have contemporaneously been assessed in the same animals. Thermal stress caused the expression of a 69-kDa inducible isoform in gills of O edulis but not in the digestive gland. Northern dot blot analysis confirmed that the transcription of Hsp69-mRNA occurs within 3 hours of stress recovery after oyster exposure at 32 and 35ЊC. Hsp69-mRNA transcripts were not present in the gills of animals exposed to 38ЊC after 3 hours of poststress recovery, but they were detected after 24 hours. The expression of the 69-kDa protein in O edulis exposed to 38ЊC was rather low or totally absent, suggesting that the biochemical machinery at the base of the heat shock response is compromised. Together with the expected increase in MT content, the oysters exposed to Cd showed a significant enhancement of Hsp70, although there was no clear appearance of Hsp69. Interestingly, the levels of MT were significantly increased in the tissues of individuals exposed to thermal stress. Unlike oysters, heat did not provoke the expression of inducible Hsp isoforms in Mytilus galloprovincialis, Tapes philippinarum, and Scapharca inaequivalvis, although it significantly enhanced the expression of constitutive proteins of the 70-kDa family. The expression of newly synthesized Hsp70 isoforms does not seem therefore a common feature in bivalves exposed to thermal stress.

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Cellular responses to oxidative and osmotic stress

Cited by 43 publications

References 7 publications

Hyperthermia-induced Hsp70 and MT20 transcriptional upregulation are mediated by p38-MAPK and JNKs inMytilus galloprovincialis(Lamarck); a pro-survival response

Hyperthermia-induced Hsp70 and MT20 transcriptional upregulation are mediated by p38-MAPK and JNKs inMytilus galloprovincialis(Lamarck); a pro-survival response

Sequencing and expression pattern of inducible heat shock gene products in the European flat oyster, Ostrea edulis

Expression of cytoprotective proteins, heat shock protein 70and metallothioneins, in tissues ofOstrea edulis exposed to heat andheavy metals

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