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

Richter‐Landsberg, Christiane; Goldbaum, Olaf

doi:10.1007/s000180300028

Cited by 81 publications

(65 citation statements)

References 137 publications

(132 reference statements)

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“…Tau under normal conditions is a highly soluble protein, and the molecular mechanisms leading to the formation of insoluble aggregates are not yet resolved. The accumulation of abnormally folded proteins, as a result of a variety of stress situations, triggers stress responses that lead to the induction of heat shock proteins (HSPs) (for review, see Richter-Landsberg and Goldbaum, 2003). HSPs act as molecular chaperones that facilitate protein repair and renaturation (Sherman and Goldberg, 2001).…”

Section: Introductionmentioning

confidence: 99%

Proteolytic Stress Causes Heat Shock Protein Induction, Tau Ubiquitination, and the Recruitment of Ubiquitin to Tau-Positive Aggregates in Oligodendrocytes in Culture

Goldbaum¹,

Richter‐Landsberg²

2004

J. Neurosci.

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Molecular chaperones and the ubiquitin-proteasome system are participants in the defense against unfolded proteins and provide an effective protein quality control system that is essential for cellular functions and survival. Ubiquitinated tau-positive inclusion bodies containing the small heat shock protein ␣B-crystallin in oligodendrocytes are consistent features of a variety of neurodegenerative diseases, and defects in the proteasome system might contribute to the aggregation process. Oligodendrocytes, the myelin-forming cells of the CNS, are specifically sensitive to stress situations. Here we can show that in cultured rat brain oligodendrocytes proteasomal inhibition by MG-132 or lactacystin caused apoptotic cell death and the induction of heat shock proteins in a time-and concentrationdependent manner. Specifically, ␣B-crystallin was upregulated, and ubiquitinated proteins accumulated. After incubation with MG-132 the tau was dephosphorylated, which enhanced its microtubule-binding capacity. Proteasomal inhibition led to ubiquitination of tau and its association with ␣B-crystallin and to the occurrence of thioflavine S-positive aggregates in the oligodendroglial cytoplasm. These aggregates were positive for tau and also contained ubiquitin and ␣B-crystallin; hence they resembled the glial cytoplasmic inclusions observed in white matter disease and frontotemporal dementias with parkinsonism linked to chromosome 17 (FTDP-17). In summary, the data underscore the specific sensitivity of oligodendrocytes to stress situations and point to a causal relationship of proteasomal impairment and inclusion body formation.

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Section: Introductionmentioning

confidence: 99%

Proteolytic Stress Causes Heat Shock Protein Induction, Tau Ubiquitination, and the Recruitment of Ubiquitin to Tau-Positive Aggregates in Oligodendrocytes in Culture

Goldbaum¹,

Richter‐Landsberg²

2004

J. Neurosci.

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“…The upregulation of stress proteins is an important step for inhibiting protein aggregation and misfolding following stress (Richter-Landberg and Goldbaum, 2003). To investigate GRP78 mRNA expression in tissues that were exposed to heat stress, fluorescent quantification using the RT-PCR assay was used to quantify GRP78 mRNA expression, and the housekeeping gene GAPDH was used as a reference to normalize GRP78 mRNA levels in order to reduce systematic errors.…”

Section: Discussionmentioning

confidence: 99%

Association analysis between SNPs in the 5'-flanking region of the chicken GRP78 gene, thermotolerance parameters, and tissue mRNA expression

Kong¹,

Zhang²,

Ji³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. Glucose-regulated protein 78 (GRP78) is a molecular chaperone in the endoplasmic reticulum and can be induced by different kinds of environmental and physiological stress. Thus far, the role of the GRP78 gene in thermotolerance in chickens has not been investigated. In the present study, we detected sequence variations in the 5ꞌ-flanking region of the GRP78 gene and evaluated several thermotolerance parameters, such as T3, corticosterone, H/L ratio, and levels of CD3 + , CD4 + , and CD8 + T cells, to further determine its associations at 35° and 15°C. The sequencing results revealed 10 SNPs in the 5'-flanking region of the GRP78 gene, and seven mutations were chosen for further genotyping in a White Recessive Rock (WRR) chicken population. The SNP C.-744C>G in WRR chickens was significantly correlated with heat tolerance parameters under both conditions; it may therefore exert 6111 Chicken GRP78 gene expression and thermotolerance ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (2): 6110-6123 (2015) a potential hereditary effect on heat tolerance, and the genotype GG may be advantageous for thermotolerance. The heart, liver, brain, and leg muscle tissues of 8-day-old WRR chickens were sampled from heat stress groups, which were defined by exposure to 1, 2, 3, and 6 h of persistent thermal stress, and a control group, which was not exposed to thermal stress. Quantitative real-time polymerase chain reaction assay indicated that the mRNA expression level of the GRP78 gene increased gradually under heat stress, peaked at 3 h, and then decreased. We conclude that the mRNA expression of the GRP78 gene is time-and tissue-dependent.

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“…Conversely, it has been reported that HSP expression plays a protective role and provides tolerance against cellular stress. It is involved in the modulation of proteolytic machinery, preventing protein misfolding and aggregation, thereby accelerating cellular repair processes 32 . In this experiment, voluntary exercise did not alter the level of HSP90 expression when compared to the restraint stress-induced group.…”

Section: Discussionmentioning

confidence: 99%

The neuroprotective effects of voluntary exercise in a restraint stress model

Jongkamonwiwat¹,

Krityakiarana²

2012

ScienceAsia

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Cell damage and cell generation can be altered in a stressed and exercised brain. However, it is not known whether voluntary exercise can prevent cell damage or cell death in stress situations, especially in the striatal region. To address this question, male Sprague-Dawley rats (3 months old) were separated into three groups (sedentary, restraint stress, and voluntary exercise + restraint stress groups). The stress circumstances were restraint stress, light stress, and tilt cage. To assess cell damage, staining for the heat shock protein (HSP90) was undertaken and the numbers of cells showing positive HSP90 expression were counted. Neurogenesis was investigated by staining for nestin markers. The restraint stress effects were assessed by determining the number of HSP90 expressed cells produced in the dorsal striatum. A significant difference was found when the number of HSP90 positive cells in the restraint stress and the voluntary exercise + restraint stress groups were compared to those in the sedentary control group. In both experimental conditions there was neurogenesis in the striatal area. However, the group that received voluntary exercise presented a significantly higher number of nestin-expressing cells over the restraint stress group. Voluntary exercise might have an adaptive effect on neurogenesis in terms of replenishing the cellular stressed neurons but it has no effect on ameliorating the level of stress marker. The evaluation of the effects of voluntary exercise on neurogenesis in the striatal region in the stressed model might contribute to a better understanding of beneficial interventions in movement disorders related to patients with depression.

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

Cited by 81 publications

References 137 publications

Proteolytic Stress Causes Heat Shock Protein Induction, Tau Ubiquitination, and the Recruitment of Ubiquitin to Tau-Positive Aggregates in Oligodendrocytes in Culture

Proteolytic Stress Causes Heat Shock Protein Induction, Tau Ubiquitination, and the Recruitment of Ubiquitin to Tau-Positive Aggregates in Oligodendrocytes in Culture

Association analysis between SNPs in the 5'-flanking region of the chicken GRP78 gene, thermotolerance parameters, and tissue mRNA expression

The neuroprotective effects of voluntary exercise in a restraint stress model

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