Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos

Lang, Lisa; Miskovic, Dragana; Lo, Maisie; Heikkila, John J.

doi:10.1379/1466-1268(2000)005<0036:sitseo>2.0.co;2

Cited by 42 publications

(20 citation statements)

References 39 publications

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“…In this case, an increase of the molecular chaperone, the HSP70 protein, might play a role in preventing lens proteins such as crystallins from aggregation. This idea is supported by reports that heat shock and UV-A irradiation, known to cause aggregation of lens proteins (Blondin and Taylor, 1987;Wong et al, 1978), caused an increase in the hsp70 expression in lens (Lang et al, 2000;Weinreb et al, 2001). The similar response of hsp70 and ␣A-crystallin to ⌬g is probably due to similar properties of their protein products in lens.…”

Section: Microgravity Vs Hypergravitymentioning

confidence: 64%

Changes in gravitational force cause changes in gene expression in the lens of developing zebrafish

Shimada

Moorman

2006

Developmental Dynamics

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Gravity has been a constant physical factor during the evolution and development of life on Earth. We have been studying effects of simulated microgravity on gene expression in transgenic zebrafish embryos expressing gfp under the influence of gene-specific promoters. In this study, we assessed the effect of microgravity on the expression of the heat shock protein 70 (hsp70) gene in lens during development using transgenic zebrafish embryos expressing gfp under the control of hsp70 promoter/enhancer. Hsp70:gfp expression was up-regulated (45%) compared with controls during the developmental period that included the lens differentiation stage. This increase was lens specific, because the entire embryo showed only a 4% increase in gfp expression. Northern blot and in situ hybridization analysis indicated that the hsp70:gfp expression recapitulated endogenous hsp70 mRNA expression. Hypergravity exposure also increased hsp70 expression during the same period. In situ hybridization analysis for two lens-specific crystallin genes revealed that neither micro-nor hypergravity affected the expression level of ␤B1-crystallin, a non-hsp gene used as a marker for lens differentiation. However, hypergravity changed the expression level of ␣A-crystallin, a member of the small hsp gene family. Terminal deoxynucleotidyl transferase-mediated deoxyuridinetriphosphate nick end-labeling (TUNEL) assay analysis showed that altered-gravity (⌬g) decreased apoptosis in lens during the same period and the decrease correlated with the up-regulation of hsp70 expression, suggesting that elimination of nuclei from differentiating lens fiber cells was suppressed probably through hsp70 up-regulation. These results support the idea that ⌬g influences hsp70 expression and differentiation in lens-specific and developmental period specific manners and that hsp family genes play a specific role in the response to ⌬g.

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Section: Microgravity Vs Hypergravitymentioning

confidence: 64%

Changes in gravitational force cause changes in gene expression in the lens of developing zebrafish

Shimada

Moorman

2006

Developmental Dynamics

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“…message was not detectable until after MBT in Xenopus embryos, and beyond this stage, hsp70 gene expression was developmentally and spatially regulated (Heikkila et al, 1987;Krone and Heikkila, 1988;1989;Lang et al, 2000). Hsp70 mRNA was detected in the head region, the lens placode, the cement gland, proctodeum, and somitic regions of heat shocked tailbud embryos (Lang et al, 2000).…”

Section: Xenopus Hsp70 Developmental Regulationmentioning

confidence: 98%

“…In a study of hsc70 mRNA accumulation in Xenopus embryos, Lang et al (2000) observed that this message was present in unfertilized eggs, indicative of its maternal origin. Hsc70 mRNA was detected at all stages of development with increasing relative levels at neurula and late tailbud stages.…”

Section: Developmental Expression Of Hsp Genes In Xenopusmentioning

confidence: 99%

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Examination of the expression of the heat shock protein gene, hsp110, in Xenopus laevis cultured cells and embryos

Gauley

Heikkila

2006

Comparative Biochemistry and Physiology Part A: Molecular &

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Prokaryotic and eukaryotic organisms respond to various stressors with the production of heat shock proteins (HSPs). HSP110 is a large molecular mass HSP that is constitutively expressed in most adult mammalian tissues. In the present study, we have examined for the first time the expression of the hsp110 gene in Xenopus laevis cultured cells and embryos. The Xenopus hsp110 cDNA encodes an 854 amino acid protein, which shares 74% identity with mice and humans. In Xenopus A6 kidney epithelial cells hsp110 mRNA was detected constitutively and was heat inducible. Enhanced hsp110 mRNA levels were detected within 1 h, and remained elevated for at least 6 h. A similar accumulation of hsp70 mRNA was observed, but only in response to stress. Treatment of A6 cells with sodium arsenite and cadmium chloride also induced hsp110 and hsp70 mRNA accumulation. However, while ethanol treatment resulted in the accumulation of hsp70 mRNA no effect was seen for hsp110.Similarly, HSP110 and HSP70 protein increased after a 2 h heat shock and 12 h sodium arsenite treatment. The elevation in HSP110 and HSP70 protein in response to heat was detectable for up to 6 h. Recent studies with mice suggest an important role for HSP110 during development. Analysis of Xenopus embryos revealed that hsp110 mRNA was present in unfertilized eggs, indicating that it is a maternal mRNA, unlike the hsp70 message which was only detectable in response to heat shock. Heat shock-induced hsp110 mRNA accumulation was developmentally regulated, similar to hsp70, since it was not detectable until after the midblastula stage of development. Enhanced hsp110 mRNA accumulation was evident with heat shock at the blastula stage, and levels continued to increase reaching a maximum at the late tailbud stage. Message for the small heat shock protein, hsp27, was not detectable until the early tailbud stage, indicating that this hsp was not present maternally and was developmentally regulated. In situ hybridization analysis revealed that hsp110 mRNA was present in control embryos in the lens placode, spinal cord and somites, but increased upon heat shock in the anterior and posterior region, the lens placode, as well as in the somites and spinal cord. A similar iv distribution was observed for the hsp27 message, although it was not detectable until the early tailbud stage in control or heat-shocked embryos. The intracellular localization of HSP110 protein in response to stress was also investigated. HSP110 was detected predominantly in the cytoplasm in either a diffuse pattern or in long spindle-shaped fibres. Additionally, HSP110 was present in the nucleus. In heat shocked Xenopus A6 cells, HSP110 localized in distinct patterns surrounding the nucleus and was enhanced in the nucleus after prolonged heat stress. Sodium arsenite-treated cells displayed a similar pattern in which HSP110 localized on opposite ends of the nucleus. In contrast, in response to stress HSP30 was homogeneously distributed in the cytoplasm, moving into the nucleus only upon intense stress. ...

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“…It was already reported that heat shock proteins are rapidly synthesized within stressed cells after exposure to environmental stressors (Bendena et al 1991;Lang et al 2000). HSPs can be induced by a variety of environmental factors including heat (Schlesinger 1990;Currie and Tuftsal.…”

Section: Introductionmentioning

confidence: 99%

Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia

Luan

Zhang

et al. 2009

Cell Stress and Chaperones

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Heat shock protein 90 (HSP90) works as a multifunctional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25°C to 35°C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.

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Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos

Cited by 42 publications

References 39 publications

Changes in gravitational force cause changes in gene expression in the lens of developing zebrafish

Changes in gravitational force cause changes in gene expression in the lens of developing zebrafish

Examination of the expression of the heat shock protein gene, hsp110, in Xenopus laevis cultured cells and embryos

Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia

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