Trehalose Accumulation during Cellular Stress Protects Cells and Cellular Proteins from Damage by Oxygen Radicals*
By N. Benaroudj, Do Hee Lee, A. Goldberg. Journal of Biological Chemistry, 2001
665 citations recorded by the source corpus.
The disaccharide trehalose, which accumulates dramatically during heat shock and stationary phase in many organisms, enhances thermotolerance and reduces aggregation of denatured proteins. Here we report a new role for trehalose in protecting cells against oxygen radicals. Exposure of Saccharomyces cerevisiae to a mild heat shock (38 °C) or to a proteasome inhibitor (MG132) induced trehalose accumulation and markedly increased the viability of the cells upon exposure to a free radical-generating system (H2O2/iron). When cells were returned to normal growth temperature (28 °C) or MG132 was removed from the medium, the trehalose content and resistance to oxygen radicals decreased rapidly. Furthermore, a mutant unable to synthesize trehalose was much more sensitive to killing by oxygen radicals than wild-type cells. Providing trehalose exogenously enhanced the resistance of mutant cells to H2O2. Exposure of cells to H2O2 caused oxidative damage to amino acids in cellular proteins, and trehalose accumulation was found to reduce such damage. After even brief exposure to H2O2, the trehalose-deficient mutant exhibited a much higher content of oxidatively damaged proteins than wild-type cells. Trehalose accumulation decreased the initial appearance of damaged proteins, presumably by acting as a free radical scavenger. Therefore, trehalose accumulation in stressed cells plays a major role in protecting cellular constituents from oxidative damage.
Subfields: Aging, Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/686705dc65d4bbc07dc128b69e2e8e5e7bdae62a
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Citations in the corpus
- “Sleeping Beauty”: Quiescence in Saccharomyces cerevisiae (2004, background): “The primary function of trehalose may be to protect proteins in quiescent cells from denaturation and damage by oxygen radicals (5).”
- Effect of trehalose on protein structure (2008, background): “This effect can be reversed if trehalose is made available to the mutants.(106) The reaction of oxygen radicals with pro-”
- New insights on trehalose: a multifunctional molecule. (2003, background): “This lack of protection by sucrose may have to do with its inability to quench oxygen radicals or be taken up by cells (Banaroudj et al., 2001).”
- The environmental stress response: a common yeast response to diverse environmental stresses (2003, background): “…treha- lose stabilizes protein structures and prevents aggregation of unfolded proteins (De Virgilio et al. 1994; Hottiger et al. 1994; Singer and Lindquist 1998a), while the sugar appears to protect cellular structures from oxidative damage in response to hydrogen peroxide (Benaroudj et al. 2001).”
- Exogenously-supplied trehalose protects thylakoid membranes of winter wheat from heat-induced damage (2010, background): “…accumulation and markedly increased the viability of the cells upon exposure to an H2O2-generating system, showing trehalose accumulation in stressed cells plays a major role in protecting cellular constituents from oxidative damage by acting as a free radical scavenger (Benaroudj et al. 2001).”
- A Putative LEA Protein, but no Trehalose, is Present in Anhydrobiotic Bdelloid Rotifers (2005, neutral): “Trehalose may well be a general stress molecule, being induced by osmotic stress, heat stress, oxidative stress, stationary phase and cold stress in micro-organisms (Larsen et al., 1987; Gadd et al., 1987; Hottiger et al., 1987; Eleutherio et al., 1997; Benaroudj et al., 2001; Kandror et al., 2002).”