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Biochem Biophys Res Commun. 1997 Dec 8;241(1):187-92.

Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells.

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Centre de Génétique Moléculaire et Cellulaire, Université Claude Bernard LYON-I, Villeurbanne, F-69622, France.


The mammalian small stress protein hsp27 is an oligomeric phosphoprotein which interferes with the cell death induced by several stimuli. In that sense, we and others have recently shown that human hsp27 expression induced cellular protection against tumor necrosis factor (TNFalpha), a protection which depends on the ability of hsp27 to decrease the level of reactive oxygen species and increase that of glutathione. Here, we have analyzed unphosphorylatable mutants of human hsp27 in which serines 15, 78, and 82 were replaced by alanines, glycines, or aspartic acids. Depending on the amino acid which was used to substitute the serine sites, a different pattern of hsp27 structural organization was observed. Alanine substitution generated large hsp27 aggregates while glycine and aspartic acid did the reverse. Hence, these phosphorylatable serine residues can be considered as key elements affecting hsp27 structural organization. Only the large aggregates of hsp27 were able to modulate reactive oxygen species and glutathione and generated cellular protection against TNFalpha. Moreover, using drugs that modulate the intracellular level of glutathione, we show that an increase in glutathione by itself was sufficient to generate large hsp27 structures while the reverse was observed in the case of glutathione deprivation.

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