Interactions of the Proteasomal System with Chaperones

Kästle, Marc; Grune, Tilman

doi:10.1016/b978-0-12-397863-9.00004-3

Cited by 55 publications

(49 citation statements)

References 187 publications

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“…Similarly, multiple mechanism(s) may underlie HSPmediated inhibition of cisplatin ototoxicity. In other systems, HSPs protect cells against damage-induced death by preventing the accumulation and aggregation of damaged proteins, as well as by promoting proper re-folding of denatured proteins (Jolly and Morimoto 2000;Yamamoto et al 2000;Martindale and Holbrook 2002;Mayer and Bukau 2005;Kastle and Grune 2012). The protection conferred by HSPs is not limited to these "chaperone" activities; HSPs also inhibit lipid peroxidation and oxidative damage to DNA (Park et al 1998;Su et al 1999;Martindale and Holbrook 2002).…”

Section: Discussionmentioning

confidence: 99%

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Baker

Roy

Brandon

et al. 2014

JARO

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Cisplatin is a highly successful and widely used chemotherapy for the treatment of various solid malignancies in both adult and pediatric patients. Side effects of cisplatin treatment include nephrotoxicity and ototoxicity. Cisplatin ototoxicity results from damage to and death of cells in the inner ear, including sensory hair cells. We showed previously that heat shock inhibits cisplatin-induced hair cell death in whole-organ cultures of utricles from adult mice. Since heat shock protein 70 (HSP70) is the most upregulated HSP in response to heat shock, we investigated the role of HSP70 as a potential protectant against cisplatin-induced hair cell death. Our data using utricles from HSP70 −/− mice indicate that HSP70 is necessary for the protective effect of heat shock against cisplatin-induced hair cell death. In addition, constitutive expression of inducible HSP70 offered modest protection against cisplatin-induced hair cell death. We also examined a second heat-inducible protein, heme oxygenase-1 (HO-1, also called HSP32). HO-1 is an enzyme responsible for the catabolism of free heme. We previously showed that induction of HO-1 using cobalt protoporphyrin IX (CoPPIX) inhibits aminoglycoside-induced hair cell death. Here, we show that HO-1 also offers significant protection against cisplatin-induced hair cell death. HO-1 induction occurred primarily in resident macrophages, with no detectable expression in hair cells or supporting cells. Depletion of macrophages from utricles abolished the protective effect of HO-1 induction. Together, our data indicate that HSP induction protects against cisplatin-induced hair cell death, and they suggest that resident macrophages mediate the protective effect of HO-1 induction.

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Section: Discussionmentioning

confidence: 99%

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Baker

Roy

Brandon

et al. 2014

JARO

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“…If the substrate is irreversible unfolded bcl-2-associated athanogene 1 (BAG-1) and the carboxyl terminus of HIP (CHIP) replace the HIP and Hsp40 proteins; CHIP is an E3 Ub ligase and ubiquitinates both the substrate and the binders (i.e., the BAG-1 and Hsp70 proteins) for degradation by the proteasome. The ubiquitination of BAG-1 and Hsp70 act as a signal for substrate degradation (K€ astle and Grune, 2012). In addition, it was proposed that as a response to oxidative stress Hsp70 interacts with the proteasome 19S RP promoting the 19S RP-20S CP disassembly; this process then enables the 20S CP-mediated degradation of oxidized proteins .…”

Section: Ups and The Network Of Molecular Chaperonesmentioning

confidence: 99%

“…Additional integrated modules of the PN can be considered the regulatory pathways of the cellular stress (e.g., heat or oxidative) responses which mobilize the proteome caretakers; mitotic cells can also dilute proteome damage by mitosis (Niforou et al, 2014;Trougakos et al, 2013). As it is now realized there is significant cross talk between the various PN constituent components; this cross talk appears to be critical for the maintenance of cellular proteostasis and proteome stability (Balantinou et al, 2009;Fusco et al, 2012;K€ astle and Grune, 2012;LTw et al, 2013;Sun et al, 2009;Trougakos et al, 2013;Tsakiri et al, 2013a,b,c).…”

Section: Introductionmentioning

confidence: 98%

The Amazing Ubiquitin-Proteasome System: Structural Components and Implication in Aging

Tsakiri

Trougakos

2015

International Review of Cell and Molecular Biology

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“…5C) (45,46). Accumulation of misfolded proteins can lead to proteotoxic stress and inflammation (47)(48)(49). Proteotoxicity in the cytosol can initiate the unfolded protein response, resulting in ER stress.…”

Section: The Ubiquitin-proteasome System Is Enriched In Msx1/ Msx2 D/mentioning

confidence: 99%

Muscle Segment Homeobox Genes Direct Embryonic Diapause by Limiting Inflammation in the Uterus

Cha¹,

Bartos²,

Li³

et al. 2015

Journal of Biological Chemistry

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Background: Embryonic diapause is a reproductive strategy that confers blastocyst dormancy and uterine quiescence without implantation until conditions become favorable. Results: Mice devoid of uterine muscle segment homeobox genes (Msx) show heightened inflammatory signature with failure of diapause. Conclusion: Msx coordinates various pathways limiting inflammation in the uterus for diapause. Significance: This study identifies a previously unrecognized role of Msx in this unique phenomenon.

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Interactions of the Proteasomal System with Chaperones

Cited by 55 publications

References 187 publications

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

The Amazing Ubiquitin-Proteasome System: Structural Components and Implication in Aging

Muscle Segment Homeobox Genes Direct Embryonic Diapause by Limiting Inflammation in the Uterus

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