Small Heat Shock Proteins in Physiological and Stress-Related Processes

Orejuela, Diana; Bergeron, Anne; Morrow, Geneviève; Tanguay, Robert M.

doi:10.1007/978-0-387-39717-7_7

Cited by 7 publications

(12 citation statements)

References 224 publications

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“…Bitar and Patil reported that gastrointestinal smooth muscles of rats undergo reductions in contractility with age 51 . In a recent review, Orejuela and colleagues noted that HSPB1 levels decrease in cultured human dermal fibroblasts as a function of aging and that the phosphorylated form of this protein decreases in gastrointestinal smooth muscle of older rats 7 . They proposed that the attenuated contractile response in these rats may be due to the lower association of unphosphorylated HSPB1 in complexes containing tropomyosin and actin.…”

Section: Changes In Hspb1 Regulation Of Actin Filament Dynamics In Agmentioning

confidence: 99%

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HSPB1, actin filament dynamics, and aging cells

Doshi

Hightower

Lee

2010

Annals of the New York Academy of Sciences

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Investigations into the possible roles of human HSPB1 in aging have focused on its role as a molecular chaperone protecting partially folded or unfolded proteins, particularly during oxidative stress. A thorough analysis of potential roles of HSPB1 in aging cells has been hampered by a limited knowledge of its functions in living cells. Most studies have employed cell-free extracts and purified proteins. For example, HSPB1 is known to bind actin in vitro, and this observation led to the hypothesis that HSPB1 regulates actin filament dynamics. In the study summarized herein, the role of HSPB1 in regulating actin filament dynamics was further investigated by using cultured human cells. These results show that HSPB1 and actin form a complex in vivo and that HSPB1 is important for cell motility. A model for HSPB1 as a regulator of actin filament dynamics is presented, and evidence from the literature on cytoskeletal alterations in aging cells is discussed.

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Section: Changes In Hspb1 Regulation Of Actin Filament Dynamics In Agmentioning

confidence: 99%

“…It has been proposed that small HSPs acting as molecular chaperones may affect the aging process beneficially by preventing protein aggregation and stabilizing partially unfolded proteins or folding intermediates (see the review by Orejuela et al . for additional background and references) 7 …”

Section: Introductionmentioning

confidence: 99%

HSPB1, actin filament dynamics, and aging cells

Doshi

Hightower

Lee

2010

Annals of the New York Academy of Sciences

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“…In Drosophila melanogaster , the 4 main sHsps show such chaperone‐like properties both in theses assays 48 as well as in a semi‐ in vivo test for luciferase reactivation in Xenopus eggs 49 . In vivo the function(s) of sHps seem quite variable and have been associated with numerous cellular and developmental processes 50–53 . In humans, mutations in sHsps have also been associated with a number of degenerative neuropathies like Charcot‐Marie and some desmin‐related myopathies 52,54 …”

Section: Small Hsps and Aging In Drosophilamentioning

confidence: 99%

“…In vivo the function(s) of sHps seem quite variable and have been associated with numerous cellular and developmental processes 50–53 . In humans, mutations in sHsps have also been associated with a number of degenerative neuropathies like Charcot‐Marie and some desmin‐related myopathies 52,54 …”

Section: Small Hsps and Aging In Drosophilamentioning

confidence: 99%

“…49 In vivo the function(s) of sHps seem quite variable and have been associated with numerous cellular and developmental processes. [50][51][52][53] In humans, mutations in sHsps have also been associated with a number of degenerative neuropathies like Charcot-Marie and some desmin-related myopathies. 52,54 In Drosophila, it is possible to target the overexpression of a protein both spatially and temporally using the Gal4/UAS system.…”

Section: Small Hsps and Aging In Drosophilamentioning

confidence: 99%

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Protection from aging by small chaperones

Morrow

Kim

Pêcheur

et al. 2010

Annals of the New York Academy of Sciences

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Aging is a complex process accompanied by a decreased capacity of cells to cope with random molecular damages. Damaged proteins can form aggregates and have cytotoxic properties, a feature of many age-associated diseases. Small Hsps are chaperones involved in the refolding and/or disposal of protein aggregates. In Drosophila melanogaster, the mitochondrial DmHsp22 is preferentially upregulated during aging. Its over-expression results in an extension of lifespan (>30%) and an increased resistance to stress. Although DmHsp22 has a chaperone-like activity in vitro, additional mechanisms by which it may extend lifespan in vivo are unknown. Genome-wide transcriptional analysis and comparative mitochondrial proteomic analysis by MALDI-TOF were performed to unveil differences in long-lived DmHsp22 over-expressing flies. Flies over-expressing DmHsp22 display an upregulation of genes normally downregulated with age and involved in energy production and protein biosynthesis. Interestingly, DmHsp22 over-expression extended lifespan of normal fibroblasts by slowing the aging process. However, its expression also increased the malignant properties of human transformed cells. The delicate balance between beneficial and noxious effects of this small chaperone are discussed.

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