Tissue-Specific Differences in Accumulation of Stress Proteins in Mytilus edulis Exposed to a Range of Copper Concentrations

Sanders, Brenda Μ.; Martin, Leigh R.; Howe, Stavros; Nelson, William G.; Hegre, Erling S.; Phelps, Donald K.

doi:10.1006/taap.1994.1066

Cited by 54 publications

(20 citation statements)

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“…It has also been previously reported that differences in the accumulation of Hsp70 and other stress proteins might be useful in identifying tissues that are particularly vulnerable to damage by a specific stressor (Sanders et al, 1994). Our results are in accordance with those described by Chapple et al (1997), who also reported that hyperthermia induces in gills the largest increase in Hsp70 levels, compared with the mantle and the adductor muscle of Mytilus edulis.…”

Section: Discussionsupporting

confidence: 92%

Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.)

Kefaloyianni

Gourgou

Ferle

et al. 2005

Journal of Experimental Biology

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SUMMARY We investigated the effects of various heavy metals such as copper, zinc and cadmium, as well as acute thermal stress, on the signalling mechanisms involved in the protection and/or apoptosis of Mytilus galloprovincialis mantle and gill tissues. The results of our studies revealed that mantle and gill tissues differentially respond to the stressful stimuli examined. In the mantle tissue, 1 μmol l–1Cu2+ and 50 μmol l–1 Zn2+ induced a transient p38-MAPK activation, whereas 1 μmol l–1Cd2+ induced a biphasic profile of the kinase phosphorylation with maximal values at 15 and 120 min of treatment, respectively. Furthermore, 1μmol l–1 SB203580 abolished the Cu2+-induced kinase phosphorylation. In gills, both Cu2+ and Zn2+induced a considerably higher p38-MAPK activation, which remained elevated for at least 60 min, whereas Cd2+ induced a maximal kinase activation within 60 min of treatment. Hypothermia (4°C) induced a moderate kinase phosphorylation (maximised at 30 min), whereas hyperthermia (30°C) induced a rapid (within 15 min) p38-MAPK phosphorylation that remained considerably above basal levels for at least 2 h. Our studies on the synergistic effect of hyperthermia and Cu2+ revealed that these two stressful stimuli are additive in the mantle tissue, inducing an almost double p38-MAPK activation. Further studies on the involvement of the p38-MAPK signalling pathway in tissue-specific pro- or anti-apoptotic events revealed that identical stressful stimuli possibly lead to apoptotic death via the caspase-3 activation in the mantle tissue and to anti-apoptotic events possibly via the induction of Hsp70 overexpression in the gill tissue.

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Section: Discussionsupporting

confidence: 92%

Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.)

Kefaloyianni

Gourgou

Ferle

et al. 2005

Journal of Experimental Biology

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“…These results might suggest that the oyster digestive glands are scarcely affected by heat and possibly that Hsp70 only acts as a constitutive molecular chaperone in this tissue. Different tissue specificity and temporal patterns of Hsp induction have therefore been observed in O edulis, in agreement with similar observations reported for other organisms in response to stress (Sanders et al 1994;Smith et al 1999). As observed by other authors (Hofmann and Somero 1995), different constitutive members of the Hsp70 family are present in the gills of unstressed Mitilidae; in our experimental conditions, the exposure to temperatures Ն32ЊC provoked the overexpression of such proteins, without transient enhancement of any inducible isoform.…”

Section: Figsupporting

confidence: 92%

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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“…Tissue-specific expression of HSP70 has been reported in gill and heart tissues of Fundulus heteroclitus (a teleost), but not in liver, muscle or brain (Koban et al 1991). Sanders et al (1994) have suggested that the differences in the accumulation of stress proteins are useful in identifying tissues, which are particularly vulnerable to damage by a specific stressor. No expression was observed in fish fed intermediate and highest phosphorus diets in any tissues.…”

Section: Discussionmentioning

confidence: 99%

Haemato-biochemical responses and induction of HSP70 to dietary phosphorus in Catla catla (Hamilton) fingerlings

Sukumaran

Pal

Sahu

et al. 2007

Fish Physiol Biochem

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A feeding trial of 120 days was conducted to study the effect of graded levels of dietary phosphorus on haematology, serum protein concentrations and HSP70 expression in fingerlings of the Indian major carp, Catla (Catla catla). Eight isonitrogenous and isoenergetic purified diets were formulated to contain graded levels of dietary phosphorus (dP), i.e., T(1), 0.1%; T(2), 0.3%; T(3), 0.5%; T(4), 0.7%; T(5), 0.9%; T(6), 1.1%; T(7), 1.3%; or T(8), 1.5%. Four hundred and eighty fish (average weight 4.23 +/- 0.016 g) were equally distributed into 24 tanks forming eight treatments with three replicates each. The fish were fed daily at the rate of 3.5% body weight in two instalments. At the end of feeding trial fish were sampled to study total RBC and WBC count, haemoglobin, serum lysozyme activity, serum total protein, albumin (A), globulin (G) concentration and HSP70 expression. Total RBC count, haemoglobin concentration and serum lysozyme activity did not vary significantly in response to different dietary phosphorus concentrations. Total WBC count was found to be significantly (P < 0.05) higher in T(1 )relative to all other treatments. Serum albumin and A/G ratio was found to be significantly lower in fish of T(1) and T(2) in relation to T(7) group (P < 0.05). Serum globulin and total protein levels remained unaffected by variations in dietary phosphorus. HSP70 expression was observed in T(1) group (0.1% dP) in gills and brain tissue, but not in liver and muscle tissues. No HSP70 expression was observed in fish of T(4) (0.7% dP) and T(8) (1.5% dP) treatments. These prima facie results suggest that dietary phosphorus had only minor influence on the haemato-biochemical parameters studied; however dietary phosphorus deficiency caused organ specific induction of HSP70 in catla fingerlings.

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Tissue-Specific Differences in Accumulation of Stress Proteins in Mytilus edulis Exposed to a Range of Copper Concentrations

Cited by 54 publications

References 0 publications

Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.)

Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.)

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

Haemato-biochemical responses and induction of HSP70 to dietary phosphorus in Catla catla (Hamilton) fingerlings

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