Hsp104, Hsp70, and Hsp40

Glover, John R.; Lindquist, Susan

doi:10.1016/s0092-8674(00)81223-4

Cited by 1,282 publications

(638 citation statements)

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“…The phenomenon of disaggregation was first reported in S. cerevisiae where heat denatured proteins can be efficiently reactivated by the cooperative action of Hsp70-Hsp40 and the oligomeric, ring forming AAA+ ATPase chaperone Hsp104 (Glover and Lindquist, 1998;Parsell et al, 1994). Soon after the discovery of Hsp104 disaggregase in yeast, an orthologous protein called ClpB was shown to possess disaggregation activity in E. coli and in chloroplasts and mitochondria of higher eukaryotes .…”

Section: Ii441 Chaperone Mediated Refolding and Disaggregationmentioning

confidence: 99%

“…Soon after the discovery of Hsp104 disaggregase in yeast, an orthologous protein called ClpB was shown to possess disaggregation activity in E. coli and in chloroplasts and mitochondria of higher eukaryotes . Several in vitro studies have shown that the Hsp104 or ClpB system alone has little or no disaggregation activity and requires collaboration with the Hsp70 system for effective disaggregation (Glover and Lindquist, 1998;Goloubinoff et al, 1999).…”

Section: Ii441 Chaperone Mediated Refolding and Disaggregationmentioning

confidence: 99%

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Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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Section: Ii441 Chaperone Mediated Refolding and Disaggregationmentioning

confidence: 99%

Section: Ii441 Chaperone Mediated Refolding and Disaggregationmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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“…Hsp16.9, Hsp17.1, Hsp17.3 and Hsp18.1 are shown to prevent the aggregation or denaturation of proteins during HS (Lee et al, 1995;Yeh et al, 1997;Young et al, 1999;Low et al, 2000). Hsp100 is shown to rescue the heat-induced protein aggregates by their re-solubilization during the recovery phase (Glover and Lindquist, 1998). Certain other Hsps such as Hsp40, Hsp60, Hsp70 and Hsp90 (alone or in co-operation) stabilize the heat-denatured proteins (Hartl et al, 1994;Glover and Lindquist, 1998;Buchner, 1999).…”

Section: Synthesis To Propose a Modelmentioning

confidence: 99%

“…Hsp100 is shown to rescue the heat-induced protein aggregates by their re-solubilization during the recovery phase (Glover and Lindquist, 1998). Certain other Hsps such as Hsp40, Hsp60, Hsp70 and Hsp90 (alone or in co-operation) stabilize the heat-denatured proteins (Hartl et al, 1994;Glover and Lindquist, 1998;Buchner, 1999). Detailed studies in model systems like Arabidopsis, yeast and human cell lines show that several different Hsps act in synchronous manner to prevent aggregation or re-fold the aggregated proteins.…”

Section: Synthesis To Propose a Modelmentioning

confidence: 99%

Genetic engineering for heat tolerance in plants

Singh

Grover

2008

Physiol Mol Biol Plants

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High temperature tolerance has been genetically engineered in plants mainly by over-expressing the heat shock protein genes or indirectly by altering levels of heat shock transcription factor proteins. Apart from heat shock proteins, thermotolerance has also been altered by elevating levels of osmolytes, increasing levels of cell detoxification enzymes and through altering membrane fluidity. It is suggested that Hsps may be directly implicated in thermotolerance as agents that minimize damage to cell proteins. The other three above approaches leading to thermotolerance in transgenic experiments though operate in their own specific ways but indirectly might be aiding in creation of more reductive and energy-rich cellular environment, thereby minimizing the accumulation of damaged proteins. Intervention in protein metabolism such that accumulation of damaged proteins is minimized thus appears to be the main target for genetically-engineering crops against high temperature stress. High temperature-induced gene expression system is one of the best-studied model systems for analyzing induced gene expression. The molecular basis of heat shock (HS) response was revealed for the first time when Ritossa (1962) reported that temperature elevation brings about altered puffing pattern of polytene chromosomes in Drosophila. Tissieres et al. (1974) for the first time showed that the HS condition results in altered protein profile in the Drosophila cells. Further studies established that nearly all organisms, ranging from bacteria to man, respond to HS by synthesizing a new set of proteins called heat shock proteins (Hsp). The HS system has been investigated in great depth using diverse biological systems including microbes (e.g. Escherichia coli, Saccharomyces cerevisiae), animals (e.g. Drosophila melanogaster, Homo sapiens) and plants (e.g. Arabidopsis thaliana, Oryza sativa, Solanum lycopersicon) species. In recent years, detailed understanding has been gained on various components of the heat shock response (HSR) in living organisms including features like heat shock genes/proteins, heat shock promoters and heat shock elements (HSEs), heat shock factors (HSFs), possible receptors of the heat shock response, signaling components and chromatin remodeling aspects (Grover, 2002, Wahid et al., 2007.Plant scientists have a concern in altering the HS response as high ambient temperature is one of the major constraints in obtaining maximum output from the crop plants. Most crops are affected by daily fluctuations in high day and/or night temperatures. While some stages of plant growth may be more sensitive to high temperature than others, there is an overall reduction in plant performance when temperature is higher than the optimal temperature at specific growth stages. Conventional breeding for high temperature stress tolerance has not been much successful due to several reasons like lack of suitable source of genes in sexuallycompatible gene pools, complex nature of the HS trait, lack of understanding on the genetic mech...

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“…The result is unfolding and aggregation of various cellular proteins [ 7 ], activation of the stress genes [ 8 ] and heat shock proteins (Hsps) synthesis. The concentration of proteins, products of these genes, is increased in response to stressors, thus protecting the cells from the damaging effects of stress and accelerating recovery by helping renaturation of partially-denaturated proteins [ 9 ].…”

mentioning

confidence: 99%

Evaluation of the Expression of the Low Weight Heat Shock Protein αB-crystallin in Pulmonary Neuroendocrine Tumours

Marinova¹,

Slavova²,

Trifonova³

et al. 2013

Proceeding BAS

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αB-crystallin is a major heat-inducible small heat shock protein, which is supposed to be implicated in tumour cell proliferation, differentiation, invasion, metastasis and apoptosis. Still the expression pattern of the phosphorylated on serin 59 form of αB-crystallin in lung cancer is not yet investigated.The aim of the present work is to study this pattern in different histological subtypes of pulmonary neuroendocrine tumours (pNETs).Surgically resected specimens from 143 patients with pNETs were studied. The histological subtype, pathological Tumour-Node-Metastasis stage and the immunohistochemical expression of phosphorylated αB-crystallin were evaluated.We demonstrated that the nucleus was the major localization site of the protein although there were some rare cases showing also diffuse cytoplasmic expression. High grade pNETs (small cell lung carcinoma and large cell neuroendocrine carcinoma) showed nuclear expression in all cases but most frequently it was in less than 50% of the tumour cells; cytoplasmic expression was shown in single cases. Just the opposite was observed in low and intermediate grade pNETs (typical carcinoids and atypical carcinoids) -nuclear expression was not seen in all of the cases, but when it was present it was in almost all tumour cells; the cases expressing phosphorylated αB-crystallin also in the cytoplasm were mainly typical carcinoids. We demonstrated that cytoplasmic 281 expression was associated with earlier stage and absence of metastases, which may determine it as a potential marker for a favourable prognosis in patients.We conclude that phosphorylated αB-crystallin probably plays a major role in pNETs biology, it may be associated with tumour grade, it may have a prognostic value, and it may be used as future target for therapy.Key words: heat shock proteins, αB-crystallin, pulmonary neuroendocrine tumours 1. Introduction. The lung cancer clinical course is determined by its histological and biological features [ 1 ]. The prognosis in lung cancer patients is associated with certain clinicopathological features as histological type, tumour size and invasion of adjacent structures (T-status), lymph node metastases (N-status) and pTNM (pathological Tumour-Node-Metastasis) stage [ 2, 3 ]. These features are not always sufficient for complete and objective assessment of lung tumours, which requires in-depth studies of immunohistochemical and genetic indicators that could serve as better markers for determining the biological behaviour of these tumours [ 4 ].Adenocarcinoma and squamous cell carcinoma are the most common lung tumours (85% of all lung cancers) and thus they are the most actively studied group. A more special and rare group are the pulmonary neuroendocrine tumours (pNETs) comprising very different tumours regarding biological behaviour and prognosis -typical carcinoids (TCs), atypical carcinoids (AtCs), small cell lung carcinomas (SCLCs) and large-cell neuroendocrine carcinomas (LCNECs) Various factors (such as hyperthermia, hypoxia, heavy metals, ethan...

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Hsp104, Hsp70, and Hsp40

Cited by 1,282 publications

References 49 publications

Firefly luciferase mutants as sensors of proteome stress

Firefly luciferase mutants as sensors of proteome stress

Genetic engineering for heat tolerance in plants

Evaluation of the Expression of the Low Weight Heat Shock Protein αB-crystallin in Pulmonary Neuroendocrine Tumours

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