Expression of stress proteins alpha B-crystallin, ubiquitin, and hsp27 in pallido-nigral spheroids of aged rhesus monkeys

Schultz, Christian; Dick, Edward J.; Cox, A.B.; Hubbard, Gene B.; Braak, Heiko

doi:10.1016/s0197-4580(01)00229-9

Cited by 33 publications

(22 citation statements)

References 21 publications

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“…A marked induction of both proteins in astrocytes was seen after heat shock [94]. Accumulation of HSP27, aB-crystallin and ubiquitin was demonstrated to be localized to spheroid bodies in astroglial processes in old rhesus monkeys and baboons [95,96]. An increase in aBcrystallin in astrocytes is characteristic for a wide variety of neurodegenerative disorders, including Alzheimer's disease (AD), Parkinson's disease (PD) and Alexander's disease [43], and is also a consistent component of glial cell inclusions (see below).…”

Section: Hsps and A Ab-crystallinmentioning

confidence: 92%

Stress proteins in neural cells: functional roles in health and disease

Richter‐Landsberg¹,

Goldbaum²

2003

Cellular and Molecular Life Sciences (CMLS)

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Heat shock proteins (HSPs) or stress proteins participate in protein synthesis, protein folding, transport and translocalization processes. Stress situations trigger a heat shock response leading to their induction. Similarly, they can be upregulated by impairment of the proteasomal degradation pathway. The upregulation of stress proteins is an important step in prevention of protein aggregation and misfolding after stress, and also is essential during development and differentiation. A number of HSPs are constitutively or inducibly expressed in the nervous system and connected to protection of nerve cells and glia. The cytoskeleton is affected by stress, and HSPs have been shown to interact with the cytoskeleton in normal cells and to assist proper assembly, spatial organization and cross-linking properties. The integrity of the cytoskeleton is disturbed in many neurodegenerative disorders, and filamentous cytoplasmic inclusion bodies, containing a variety of HSPs, are observed. This review summarizes the recent literature on the presence and induction of HSPs in neural cells, and their possible functional roles in health and disease are discussed.

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Section: Hsps and A Ab-crystallinmentioning

confidence: 92%

Stress proteins in neural cells: functional roles in health and disease

Richter‐Landsberg¹,

Goldbaum²

2003

Cellular and Molecular Life Sciences (CMLS)

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“…The major risk factor for neurodegenerative diseases is aging. Although the induction of heat shock proteins is impaired with aging, chaperones in general are increased with aging (Fargnoli et al 1990;Maiello et al 1998;Soti and Csermely 2000;Schultz et al 2001;Walters et al 2001;Gupte et al 2010). For example, heat shock proteins 40, 27, 60, 70, and constitutive heat shock protein 70 are known to increase in the aged central nervous system (Lee et al 2000;Lu et al 2004).…”

Section: Adaptation and Sensitization To Proteotoxic Stressmentioning

confidence: 99%

Adaptation and Sensitization to Proteotoxic Stress

Leak

2013

Dose-Response

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ᮀ Although severe stress can elicit toxicity, mild stress often elicits adaptations. Here we review the literature on stress-induced adaptations versus stress sensitization in models of neurodegenerative diseases. We also describe our recent findings that chronic proteotoxic stress can elicit adaptations if the dose is low but that high-dose proteotoxic stress sensitizes cells to subsequent challenges. In these experiments, long-term, low-dose proteasome inhibition elicited protection in a superoxide dismutase-dependent manner. In contrast, acute, high-dose proteotoxic stress sensitized cells to subsequent proteotoxic challenges by eliciting catastrophic loss of glutathione. However, even in the latter model of synergistic toxicity, several defensive proteins were upregulated by severe proteotoxicity. This led us to wonder whether high-dose proteotoxic stress can elicit protection against subsequent challenges in astrocytes, a cell type well known for their resilience. In support of this new hypothesis, we found that the astrocytes that survived severe proteotoxicity became harder to kill. The adaptive mechanism was glutathione dependent. If these findings can be generalized to the human brain, similar endogenous adaptations may help explain why neurodegenerative diseases are so delayed in appearance and so slow to progress. In contrast, sensitization to severe stress may explain why defenses eventually collapse in vulnerable neurons.

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“…The basal expression level of Hsp70 in the absence of any proteotoxic signal such as heat shock is known to increase as the organisms age in D. melanogaster (Wheeler et al 1995). Tissue-specific induction of stress proteins in mammals is also observed during normal ageing (Schultz et al 2001) indicating that induction of Hsp expression during ageing is evolutionarily conserved across a broad range of taxa. Ageing-associated up-regulation of Hsps has also been documented including some recent genome-wide studies of gene expression changes (Wheeler et al 1995; King and Tower 1999; Wheeler et al 1999; Landis et al 2004).…”

Section: Discussionmentioning

confidence: 99%

Relationship between heat shock protein 70 expression and life span in Daphnia

Schumpert

Handy

Dudycha

et al. 2014

Mechanisms of Ageing and Development

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The longevity of an organism is directly related to its ability to effectively cope with cellular stress. Heat shock response (HSR) protects the cells against accumulation of damaged proteins after exposure to elevated temperatures and also in ageing cells. To understand the role of Hsp70 in regulating life span of Daphnia, we examined the expression of Hsp70 in two ecotypes that exhibit strikingly different life spans. D. pulicaria, the long lived ecotype, showed a robust Hsp70 induction as compared to the shorter lived D. pulex. Interestingly, the short-lived D. pulex isolates showed no induction of Hsp70 at the mid point in their life span. In contrast to this, the long-lived D. pulicaria continued to induce Hsp70 expression at an equivalent age. We further show that the Hsp70 expression was induced at transcriptional level in response to heat shock. The transcription factor responsible for Hsp70 induction, heat shock factor-1 (HSF-1), although present in aged organisms did not exhibit DNA-binding capability. Thus, the decline of Hsp70 induction in old organisms could be attributed to a decline in HSF-1’s DNA-binding activity. These results for the first time, present a molecular analysis of the relationship between HSR and life span in Daphnia.

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Expression of stress proteins alpha B-crystallin, ubiquitin, and hsp27 in pallido-nigral spheroids of aged rhesus monkeys

Cited by 33 publications

References 21 publications

Stress proteins in neural cells: functional roles in health and disease

Stress proteins in neural cells: functional roles in health and disease

Adaptation and Sensitization to Proteotoxic Stress

Relationship between heat shock protein 70 expression and life span in Daphnia

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