The distribution of heat shock proteins in the nervous system of the unstressed mouse embryo suggests a role in neuronal and non-neuronal differentiation

Loones, M. T.; Chang, Yunhua; Morange, Michel

doi:10.1379/1466-1268(2000)005<0291:tdohsp>2.0.co;2

Cited by 79 publications

(65 citation statements)

References 73 publications

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“…Tissue extracts (TE) and whole-cell extracts (WCE) from K562 cells were prepared as described by Mosser et al (1988) or Loones et al (2000). Approximately 20-36 µg of TE or WCE per sample was used for SDS-PAGE.…”

Section: Ip and Western Blot Analysismentioning

confidence: 99%

Role of heat-shock factor 2 in cerebral cortex formation and as a regulatorof p35 expression

Chang¹,

Östling²,

Åkerfelt³

et al. 2006

Genes Dev.

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109

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Heat-shock factors (HSFs) are associated with multiple developmental processes, but their mechanisms of action in these processes remain largely enigmatic. Hsf2-null mice display gametogenesis defects and brain abnormalities characterized by enlarged ventricles. Here, we show that Hsf2 −/− cerebral cortex displays mispositioning of neurons of superficial layers. HSF2 deficiency resulted in a reduced number of radial glia fibers, the architectural guides for migrating neurons, and of Cajal-Retzius cells, which secrete the positioning signal Reelin. Therefore, we focused on the radial migration signaling pathways. The levels of Reelin and Dab1 tyrosine phosphorylation were reduced, suggesting that the Reelin cascade is affected in Hsf2 −/− cortices. The expression of p35, an activator of cyclin-dependent kinase 5 (Cdk5), essential for radial migration, was dependent on the amount of HSF2 in gain-and loss-of-function systems. p39, another Cdk5 activator, displayed reduced mRNA levels in Hsf2 −/− cortices, which, together with the lowered p35 levels, decreased Cdk5 activity. We demonstrate in vivo binding of HSF2 to the p35 promoter and thereby identify p35 as the first target gene for HSF2 in cortical development. In conclusion, HSF2 affects cellular populations that assist in radial migration and directly regulates the expression of p35, a crucial actor of radial neuronal migration.[Keywords: Corticogenesis; heat-shock factor; p35-Cdk5; radial cortical migration] Supplemental material is available at http://www.genesdev.org. Heat-shock factors (HSFs) were initially discovered to regulate heat-shock genes and the heat-shock response. The heat-shock response, conserved from yeast to man, is characterized by the induction of heat-shock genes encoding molecular chaperones (for review, see Pirkkala et al. 2001). A unique gene constitutes HSF in yeast, nematode, and fruit fly, whereas a family of four members is present in vertebrates. HSF1 and HSF2 are found in all vertebrate species, while HSF3 is specific for avian species and HSF4 is specific for mammals (Rabindran et al. 1991;Sarge et al. 1991;Schuetz et al. 1991;Nakai and Morimoto 1993;Nakai et al. 1997;Råbergh et al. 2000;Hilgarth et al. 2004;Le Goff et al. 2004). In vertebrates, HSF1 is the stress-responsive prototype, which cannot be substituted by any other HSF in stress-inducible hsp gene expression or in acquired thermotolerance (McMillan et al. 1998;Xiao et al. 1999;Zhang et al. 2002).A developmental role for the HSFs began to emerge when the Drosophila HSF was found to be required for oogenesis and early larval development (Jedlicka et al. 1997). Strikingly, these developmental effects of Drosophila HSF are not mediated by hsp gene induction. The basal expression levels of hsps during embryonic development in mouse are not affected by the lack of HSF1 (Xiao et al. 1999). Therefore, other target genes are likely to be controlled by HSF1 in development. Recently, binding of HSF1 and HSF4 to the FGF-7 promoter with opposing effects on FGF-7 gene expression su...

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Section: Ip and Western Blot Analysismentioning

confidence: 99%

Role of heat-shock factor 2 in cerebral cortex formation and as a regulatorof p35 expression

Chang¹,

Östling²,

Åkerfelt³

et al. 2006

Genes Dev.

Self Cite

109

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“…Studies involving experimental exposure to electromagnetic fields have revealed numerous modifications in the expression of heat shock proteins in vivo [8] and in vitro, in cell lines [9]. HSP-90 is the most common type of heat shock protein [10] and occurs at higher levels in nerve tissues than in non nerve tissues [11] and is distributed in neurons in the limbic system, neocortex, striatus and thalamus [12,13]. This protein acts to regulate the activity of other proteins such as steroid hormone receptors [14] kinase [15], calmodulin [16], actin [17], and tubulin [18].…”

Section: Introductionmentioning

confidence: 99%

EXPOSURE TO 2.45 GHz MICROWAVE RADIATION PROVOKES CEREBRAL CHANGES IN INDUCTION OF HSP-90 Î±/Î² HEAT SHOCK PROTEIN IN RAT.

Jorge-Mora¹,

Álvarez-Folgueiras²,

Leiro³

et al. 2010

PIER

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Abstract-Physical agents such as non-ionizing continuous-wave 2.45 GHz radiation may cause damage that alters cellular homeostasis and may trigger activation of the genes that encode heat shock proteins (HSP). We used Enzyme-Linked ImmunoSorbent Assay (ELISA) and immunohistochemistry to analyze the changes in levels of HSP-90 and its distribution in the brain of Sprague-Dawley rats, ninety minutes and twenty-four hours after acute (30min) continuous exposure to 2.45 GHz radiation in a the Gigahertz Transverse Electromagnetic (GTEM cell). In addition, we studied further indicators of neuronal insult: dark neurons, chromatin condensation and nucleus fragmentation, which were observed under optical conventional or fluorescence microscopy after DAPI staining. The cellular distribution of protein HSP-90 in the brain increased with each corresponding SAR (0.034 ± 3.10 −3 , 0.069 ± 5.10 −3 , 0.27 ± 21.10 −3 W/kg), in hypothalamic nuclei, limbic cortex and somatosensorial cortex after exposure to the radiation. At twenty-four hours post-irradiation, levels of HSP-90 protein remained high in all hypothalamic nuclei for all SARs, and in the parietal cortex, except the limbic system, HSP-90 levels were lower than in non-irradiated rats, almost half the levels in rats exposed to the highest power radiation. Non-apoptotic cellular nuclei and a some dark neurons were found ninety minutes and twenty-four hours after maximal SAR exposure. The results suggest that acute exposure to electromagnetic fields triggered an imbalance in anatomical HSP-90 levels but the anti-apoptotic mechanism is probably sufficient to compensate the non-ionizing stimulus. Further studies are required to determine the regional effects of chronic electromagnetic pollution on heat shock proteins and their involvement in neurological processes and neuronal damage.

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“…3 ± 7 It appears to be highly expressed in specific organs or tissues such as the heart, 8 skeletal striated muscles, epidermis, cartilage, bone 9 and specific areas of the central nervous system. 10,11 But nothing is known about how the possible role of this protein may explain such a specific distribution.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion

Favet

Duverger

et al. 2001

Cell Death Differ

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Although multiple functions for the small heat shock protein HSP25 have been proposed, its specific role during developmental and differentiation processes is not known. Cartilage is one of the tissues in which HSP25 is specifically and highly expressed during development. C1 cells, able to form aggregates in vitro, can be induced to differentiate into chondrocytes. In this study, we generated two stable transfected clones overexpressing HSP25 at two different levels. Cell morphology and growth rate were modified in both clones, although the actin content and distribution did not seem to be altered. Overexpressing clones had more difficulties in coalescing, leading to smaller aggregates and they did not differentiate into chondrocytes. Subsequently, these aggregates tended to dissociate into loose masses of dying cells. The strength of all these effects was directly correlated to the level of HSP25 overexpression. These data suggest that overexpressing HSP25 decreases cellular adhesion and interferes with chondrocyte differentiation. Cell Death and Differentiation (2001) 8, 603 ± 613.

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The distribution of heat shock proteins in the nervous system of the unstressed mouse embryo suggests a role in neuronal and non-neuronal differentiation

Cited by 79 publications

References 73 publications

Role of heat-shock factor 2 in cerebral cortex formation and as a regulatorof p35 expression

Role of heat-shock factor 2 in cerebral cortex formation and as a regulatorof p35 expression

EXPOSURE TO 2.45 GHz MICROWAVE RADIATION PROVOKES CEREBRAL CHANGES IN INDUCTION OF HSP-90 Î±/Î² HEAT SHOCK PROTEIN IN RAT.

Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion

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