Heat-Shock Genes and Development

Morange, Michel; Favet, Noelle; Loones, M. T.; Manuel, Martine; Mezger, Valérie; Michel, Evelyne; Rallu, Murielle; Sage, Julien

doi:10.1111/j.1749-6632.1998.tb08984.x

Cited by 11 publications

(7 citation statements)

References 15 publications

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“…P1-1, P4-3, P6-8, P8-2 correspond to C1 cells transfected with both the hygromycin resistance plasmid and the empty expression vector pSVK3 with no HSP25 insert. No HSP25 protein can be detected in proliferating untransfected C1 cells (lane 2), or in cells transfected with the empty vector (P clones: lanes 3,4,5,6). This indicates that HSP25 is barely, if at all, expressed in proliferating C1 cells.…”

Section: Screening Of Hsp25 Overexpressing Clonesmentioning

confidence: 97%

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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Section: Screening Of Hsp25 Overexpressing Clonesmentioning

confidence: 97%

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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“…The distribution pattern of Hsp25 during mouse embryonic development (Gernold et al 1993;Loones et al 1997;Morange et al 1998;Morange 1999;Davidson et al 2002) suggests that this protein is involved in the differentiation of tissues. Further evidence supporting this hypothesis has been obtained using ex vivo approaches (Spector et al 1994;Mehlen et al 1997;Davidson and Morange 2000;Favet et al 2001;Duverger et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Heat shock protein 25 plays multiple roles during mouse skin development

Duverger¹,

Morange²

2005

Cell Stress Chaper

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Heat shock protein (Hsp) 25 is a member of the small Hsp family. High levels of Hsp25 can be detected in skin. During adult epidermis differentiation, the concentration of Hsp25 increases as the distance of keratinocytes from the basal layer increases, in parallel with the extent of keratinization. We previously showed that Hsp25, mouse keratin (MK) 5, and MK14 participated in the formation of characteristic ring-shaped aggregates during the differentiation of the PAM212 keratinocyte cell line. We suggested that Hsp25 was involved in the disorganization of the MK5-MK14 keratin network before the establishment of the MK1-MK10 keratin network at the beginning of epidermis stratification. In this study, we have investigated the distribution of Hsp25 and keratins throughout skin development. We demonstrate that the distribution of Hsp25 and MK5 in the epidermis at the beginning of stratification and before keratinization is similar to that observed in PAM212 keratinocytes. These results indicate that there is a strong correlation between the mechanism we described ex vivo and the events taking place in vivo. Moreover, we show that Hsp25 is produced in different cell types in the epidermis and in the hair follicle at different stages of their development. Thus, our results suggest that Hsp25 is involved in more than one process during skin development.

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“…To date, most experimental work has examined the protective function of molecular chaperones in vitro, in isolated cells, or at a particular developmental stage (eg, embryo, adult); how chaperones protect complex processes such as development itself against stress is less well known. Clearly, many chaperones are essential for proper development; indeed, numerous chaperone mutants fail to develop or develop abnormally (Heikkila 1993a(Heikkila , 1993bAngelier et al 1996;Krone et al 1997;Morange et al 1998;Rutherford and Lindquist 1998;Luft and Dix 1999;Vega-Nunez et al 1999). These studies, however, seldom determine the precise molecular lesion against which chaperones protect.…”

Section: Introductionmentioning

confidence: 99%

Hsp70 and thermal pretreatment mitigate developmental damage caused by mitotic poisons in Drosophila

2002

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To assess the ability of the heat-inducible molecular chaperone heat-shock protein 70 (Hsp70) to mitigate a specific developmental lesion, we administered the antimicrotubule drugs vinblastine (VB) and colchicine (COL) to larvae of Drosophila engineered to express differing levels of Hsp70 after heat pretreatment (HP). VB and COL decreased survival during metamorphosis, disrupted development of the adult eye and other structures as well as their precursor imaginal disks, and induced chromosome nondisjunction in the wing imaginal disk as indicated by the somatic mutation and recombination test (SMART) assay. Hsp70-inducing HP reduced many of these effects. For the traits viability, adult eye morphology, eye imaginal disk morphology, cell death in the eye imaginal disks, and single and total mutant clone formation in the SMART assay, HP reduced the impact of VB to a greater extent in Drosophila with 6 hsp70 transgenes than in a sister strain from which the transgenes had been excised. Because the extra-copy strain has higher levels of Hsp70 than does the excision strain but is otherwise almost identical in genetic background to the excision strain, these outcomes are attributable to Hsp70. The hsp70 copy number had a variable interaction with HP and COL administration.

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Heat-Shock Genes and Development

Cited by 11 publications

References 15 publications

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

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

Heat shock protein 25 plays multiple roles during mouse skin development

Hsp70 and thermal pretreatment mitigate developmental damage caused by mitotic poisons in Drosophila

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