Expression of the anti-apoptotic protein Hsp27 during both the keratinocyte differentiation and dedifferentiation of HaCat cells: expression linked to changes in intracellular protein organization?
We show here that Hsp27 increases its level of expression during the late phase of the keratinocyte differentiation of human HaCat cells. A similar phenomenon was observed when differentiated HaCat cells underwent a dedifferentiation process. In both cases, Hsp27 accumulated in the form of large native structures, which represent the chaperone active form of the protein. Hence, the presence of Hsp27 large oligomers does not appear to be the consequence of a particular differentiation process but should be considered as a marker of endogenous stress conditions. Such conditions may arise when drastic changes in the intracellular protein organization occur, such as during differentiation, dedifferentiation and probably also during the development of the senescent phenotype.
Arrigo
André-Patrick
AP
Equipe Stress Oxydant, Chaperons et Apoptose, Centre de Génétique Moléculaire et Cellulaire, CNRS UMR-5534, Université Claude Bernard Lyon-I, Bd. du 11 Novembre 1918, 69622 Villeurbanne Cedex, France. arrigo@univ-lyon1.fr
Ducasse
Cécile
C
D002454:Cell Differentiation; D002460:Cell Line; D016922:Cellular Senescence / Q000502:physiology*; D002850:Chromatography, Gel; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D006801:Humans; D015151:Immunoblotting; D015603:Keratinocytes / Q000166:cytology* / Q000378:metabolism; D018832:Molecular Chaperones; D009363:Neoplasm Proteins / Q000378:metabolism*
D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins