HSP110, caspase‐3 and ‐9 expression in physiological apoptosis and apoptosis induced by <i>in vivo</i> embryonic exposition to all‐trans retinoic acid or irradiation during early mouse eye development

Gashegu, Julien; Ladha, Reza; Vanmuylder, Nathalie; Philippson, C.; Bremer, F; Rooze, Marcel; Louryan, Stéphane

doi:10.1111/j.1469-7580.2007.00719.x

Cited by 9 publications

(9 citation statements)

References 52 publications

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“…Given this information, the authors hypothesized that HSP110 played a role in the early stages of apoptosis, but did not offer a mechanism. This study was supported by the findings of Gashegu et al (2007), who observed that HSP110 was expressed before caspase-3 during development of the mouse eye, and suggested a pro-apoptotic role for HSP110 in caspase activation. Although several studies agree that HSP110 is involved at some level in apoptosis in the developing embryo, its exact role has not yet been clarified.…”

Section: Hsp110/105 Developmental Regulation and Involvement In Apoptsupporting

confidence: 86%

“…A possible role in apoptosis was suggested for mouse HSP105 during early development since this protein was observed specifically in cells undergoing programmed cell death in the interdigital regions of the limb tissue (Hatayama et al, 1997). This proposed apoptotic role was supported by recent data linking HSP110 expression to caspase-3 expression during mouse development (Evrard et al, 1999;2000;Gashegu et al, 2007).…”

Section: Hsp110 Mrna Accumulation In A6 Cellsmentioning

confidence: 82%

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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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Section: Hsp110/105 Developmental Regulation and Involvement In Apoptsupporting

confidence: 86%

Section: Hsp110 Mrna Accumulation In A6 Cellsmentioning

confidence: 82%

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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“…HSP105 might have a similar, but stress-specific, role acting on proteins necessary for activation of caspase-3, such as through upstream molecules such as GSK3. It is interesting to note that elevated HSP105 previously was found to be associated with activated caspase-3 during development [46][47][48]. Alternatively, the finding that knockdown of HSP105 reduced caspase-3 activation could be interpreted as indicating that HSP105 does not facilitate caspase-3 activation but instead suppresses an alternative death pathway.…”

Section: Discussionmentioning

confidence: 91%

HSP105 interacts with GRP78 and GSK3 and promotes ER stress-induced caspase-3 activation

Meares

Zmijewska

Jope

2008

Cellular Signalling

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Stress of the endoplasmic reticulum (ER stress) is caused by the accumulation of misfolded proteins, which occurs in many neurodegenerative diseases. ER stress can lead to adaptive responses or apoptosis, both of which follow activation of the unfolded protein response (UPR). Heat shock proteins (HSP) support the folding and function of many proteins, and are important components of the ER stress response, but little is known about the role of one of the major large HSPs, HSP105. We identified several new partners of HSP105, including glycogen synthase-3 (GSK3), a promoter of ER stress-induced apoptosis, and GRP78, a key component of the UPR. Knockdown of HSP105 did not alter UPR signaling after ER stress, but blocked caspase-3 activation after ER stress. In contrast, caspase-3 activation by genotoxic stress was unaffected by knockdown of HSP105, suggesting ER stress-specificity in the apoptotic action of HSP105. However, knockdown of HSP105 did not alter cell survival after ER stress, but instead diverted signaling to a caspase-3-independent cell death pathway, indicating that HSP105 is necessary for apoptotic signaling after UPR activation by ER stress. Thus, HSP105 appears to chaperone the responses to ER stress through its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a noncaspase-3-dependent process.

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“…Sections were incubated at 4 ° C overnight with the following primary antibodies: anti-mouse PD-1 (clone 29F.1A12, rat IgG2a) for which specificity has previously been described 14 ; RGC markers anti-Brn3a (clone 5A3.2, mouse IgG1, Millipore/Chemicon) 15 and anti-NeuN (mouse IgG1, clone A60, Millipore/Chemicon) 16 ; amacrine cell marker anti-mouse AP2α (3B5, mouse IgG2b, Developmental Studies Hybridoma Bank) 17 ; or apoptotic cell marker rabbit anti-mouse activated caspase-3 (R&D Systems) 18 . For immunohistochemistry, the Rat IgG Vectastain ABC Kit, AEC substrate kit, and hematoxylin QS counterstain (Vector) were used according to product instructions.…”

Section: Methodsmentioning

confidence: 99%

Role of the Immune Modulator Programmed Cell Death-1 during Development and Apoptosis of Mouse Retinal Ganglion Cells

Chen

Sham

Chan³

et al. 2009

Invest. Ophthalmol. Vis. Sci.

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PURPOSE Mammalian programmed cell death-1 (PD-1) is a membrane-associated receptor regulating the balance between T cell activation, tolerance and immunopathology, however its role in neurons has not yet been defined. We investigate the hypothesis that PD-1 signaling actively promotes retinal ganglion cell (RGC) death within the developing mouse retina. METHODS Mature retinal cell types expressing PD-1 were identified by immunofluorescence staining of vertical retina sections; developmental expression was localized by immunostaining and quantified by Western analysis. PD-1 involvement in developmental RGC survival was assessed in vitro using retina explants and in vivo using PD-1 knockout mice. PD-1 ligand gene expression was detected by RT-PCR. RESULTS PD-1 is expressed in most adult RGCs, and undergoes dynamic upregulation during the early postnatal window of retinal cell maturation and physiological programmed cell death (PCD). In vitro blockade of PD-1 signaling during this time selectively increases survival of RGCs. Furthermore, PD-1 deficient mice show a selective increase in RGC number in the neonatal retina at the peak of developmental RGC death. Lastly, throughout postnatal retina maturation, we find gene expression of both immune PD-1 ligand genes, PD-L1 and PD-L2. CONCLUSIONS These findings collectively support a novel role for a PD-1-mediated signaling pathway in developmental PCD during postnatal RGC maturation.

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HSP110, caspase‐3 and ‐9 expression in physiological apoptosis and apoptosis induced by in vivo embryonic exposition to all‐trans retinoic acid or irradiation during early mouse eye development

Cited by 9 publications

References 52 publications

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

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

HSP105 interacts with GRP78 and GSK3 and promotes ER stress-induced caspase-3 activation

Role of the Immune Modulator Programmed Cell Death-1 during Development and Apoptosis of Mouse Retinal Ganglion Cells

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