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Implication de deux protéines de choc thermique
humaines HSP70 et HSP22 dans les voies de la
réparation de l'ADN : approche structurale et

Abstract : HSP22 and HSP70 are human proteins belonging to Heat Shock Proteins family. The
involvement of HSP70 and HSP22 in DNA repair pathways after stress is described in this thesis. These
proteins have the ability, as suggested by their name, to be over expressed in cells after heat shock but also
following a huge variety of stresses and in several diseases and cellular disorders (Tavaria M et al, 1996). In
order to increase the knowledge on these proteins, a structural study has been initiated. The three-dimensional
structures of these proteins are not or only partially known (Osipiuk J et al, 1999). Protein structural assays
have lead to the creation of clones oh HSP70-1 and HSP22 and structural predictions have been performed for
C-terminal part of HSP70-1 and HSP22, suggesting a β-fold organization for the HSP70-1 substrate binding
domain and for the HSP22 α-crystallin domain. Results obtained in a DNA repair pathways study have shown
that the HSP70s induced by stress (HSP72 and HSP70-1) take part in these pathways after several stresses (Xray
and UV, magnetic field, hydrogen peroxide, cis-platin). HSP72 and HSP70-1 are phosphorylated by
PI3kinases related family members ATM, ATR and DNA-PK (Sarkaria JN et al, 1998) after ionizing
radiation and perform a two phases displacement between the cytoplasm and the nucleus; HSP72 and HSP70-
1 are involved in the early stages of DNA repair processes. HSP22 seems to be involved in DNA double
strand break (DSB) repair pathways after X-ray irradiation (Paull TT and Gellert M, 1998; Lobrich M and
Jeggo PA, 2005). Moreover, HSP22 appears to be involved in cellular aging processes as has been observed
for its homolog in the fly drosophila (Morrow G et al 2004). The method Diffraction Enhanced Imaging
(DEI; Chapman D et al, 1997), developed at the ESRF biomedical beam line ID17, in order to achieve
histological information, has been tested in a radiobiological context on primary chondrocytes and fibroblasts.
Irradiation using this method has not caused more damage than irradiation of primary cultured human cells
with a conventional source delivering the same dose (Rothkamm K and Lobrich M, 2003). In rat glioblastoma
cells, HSP70 response is increased under “synchrotron PAT-Plat” therapy conditions (platinum
photoactivation via synchrotron light (Corde S et al, 2003; Biston MC et al, 2004)).
Document type :
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Contributor : Wendy Rénier <>
Submitted on : Tuesday, October 24, 2006 - 4:47:45 PM
Last modification on : Monday, October 19, 2020 - 11:09:41 AM
Long-term archiving on: : Friday, November 25, 2016 - 1:50:06 PM


  • HAL Id : tel-00109542, version 1




Wendy Rénier. Implication de deux protéines de choc thermique
humaines HSP70 et HSP22 dans les voies de la
réparation de l'ADN : approche structurale et
fonctionnelle. Ingénierie biomédicale. Université Joseph-Fourier - Grenoble I, 2006. Français. ⟨tel-00109542⟩



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