Flavonoids inhibit the expression of heat shock proteins.

Hosokawa, Nobuko; Hirayoshi, Kazunori; Nakai, Asami; Hosokawa, Yu; Marui, Nobuyuki; Yoshida, Masaro; Sakai, Toshiyuki; Nishino, Hoyoku; Aoike, Akira; Kawai, Keiichi; Nagata, Kazuhiro

doi:10.1247/csf.15.393

Cited by 170 publications

(119 citation statements)

References 30 publications

Supporting

Mentioning

110

Contrasting

Unclassified

Order By: Relevance

“…Another kind of effect, an inhibition of hsp70 synthesis, may be responsible for this result. An inhibition of the hsp70 synthesis by substances like glycerol, copper and some flavonoids was described by several research groups (Edington et al, 1989;Hosokawa et al, 1990;Sanders & Martin, 1994). Werner et al (1998) in the course of a bioassay-directed fractionation (data not shown).…”

Section: Accepted Manuscriptmentioning

confidence: 90%

Expression of heat shock protein 70 in a permanent cell line (EPC) exposed to sediment extracts from the North Sea and the Baltic Sea

Kinder

Sierts-Herrmann

Biselli

et al. 2007

Marine Environmental Research

View full text Add to dashboard Cite

Section: Accepted Manuscriptmentioning

confidence: 90%

Expression of heat shock protein 70 in a permanent cell line (EPC) exposed to sediment extracts from the North Sea and the Baltic Sea

Kinder

Sierts-Herrmann

Biselli

et al. 2007

Marine Environmental Research

View full text Add to dashboard Cite

“…15,16 The present study investigated the effects of quercetin on the acceleration of matrix Figure 4. The time course changes of HSP70 and the expression of extracellular matrix genes in articular cartilage after microwave (MW) irradiation.…”

Section: Effects Of Quercetin On Hsp70 Induction and Matrix Gene Exprmentioning

confidence: 99%

Effects of heat stimulation via microwave applicator on cartilage matrix gene and HSP70 expression in the rabbit knee joint

Tonomura

Takahashi

Mazda

et al. 2007

Journal Orthopaedic Research

View full text Add to dashboard Cite

The objective of this study was to investigate the effects of heat stimulation on the expression of extracellular matrix genes and heat-shock protein 70 (HSP70) in rabbit articular cartilage in vivo. Heat stimulation was applied to the knee joints of Japanese white rabbits for 20 min using a microwave (MW) applicator (2.45-GHz, 0-80 W). After 8-72 h, the articular cartilage was removed from the knee joints and proteins and total RNA were extracted. As controls, knee joints without heat stimulation were analyzed. The expression of HSP70 was confirmed by real-time PCR and Western blotting. The expression of proteoglycan core protein (PG) and type II collagen (Col II) was quantified using real-time PCR to assess cartilage matrix metabolism. Compared to controls, HSP70 expression was higher with more than 40 W of heat stimulation. The expression of PG and Col II mRNA was higher, with more than 20 W of heat stimulation and peaked with 40 W. When quercetin was used to inhibit the induction of HSP70 expression, PG mRNA expression did not increase. External MW application stimulated HSP70 expression in the articular cartilage in vivo. The expression of extracellular matrix genes was increased by appropriate heat stimulation. ß

show abstract

“…Heat shock transcription factor 1 is found to be a primary component of the heat shock element binding activity in cells exposed to heat shock and many other physiological stresses (27)(28)(29). Hosokawa et al (30) reported that specific flavonoids, including quercetin, inhibited the transcription of various HSPs after heat shock and that this effect was due to the inhibition of heat shock transcription factor activation.…”

mentioning

confidence: 99%

Differential Effects of Mitochondrial Heat Shock Protein 60 and Related Molecular Chaperones to Prevent Intracellular β-Amyloid-induced Inhibition of Complex IV and Limit Apoptosis

Veereshwarayya

Kumar

Rosen

et al. 2006

Journal of Biological Chemistry

118

View full text Add to dashboard Cite

Defects in mitochondrial oxidative metabolism, in particular decreased activity of cytochrome c oxidase, have been reported in Alzheimer disease tissue and in cultured cells that overexpress amyloid precursor protein. Mitochondrial dysfunction contributes to neurodegeneration in Alzheimer disease partly through formation of reactive oxygen species and the release of sequestered molecules that initiate programmed cell death pathways. The heat shock proteins (HSP) are cytoprotective against a number of stressors, including accumulations of misfolded proteins and reactive oxygen species. We reported on the property of Hsp70 to protect cultured neurons from cell death caused by intraneuronal ␤-amyloid. Here we demonstrate that Hsp60, Hsp70, and Hsp90 both alone and in combination provide differential protection against intracellular ␤-amyloid stress through the maintenance of mitochondrial oxidative phosphorylation and functionality of tricarboxylic acid cycle enzymes. Notably, ␤-amyloid was found to selectively inhibit complex IV activity, an effect selectively neutralized by Hsp60. The combined effect of HSPs was to reduce the free radical burden, preserve ATP generation, decrease cytochrome c release, and prevent caspase-9 activation, all important mediators of ␤-amyloid-induced neuronal dysfunction and death.Current evidence indicates that intracellular accumulation of ␤-amyloid in neurons leads to the formation of an insoluble pool in which the peptide is highly aggregated as well as a soluble pool in which toxic oligomers are found (1-3). A␤-(1-42) 2 is generated in both the endoplasmic reticulum and the intermediate compartment (4). Because neuronal mitochondria are frequently found in close association with the endoplasmic reticulum (5), it is possible that the local concentration of A␤ is relatively higher in their vicinity compared with other cellular locations. Conceivably, exposure of mitochondria to A␤ alters membrane stability and/or their normal oxidative phosphorylation functions. These considerations make it feasible that a direct impact of intracellular ␤-amyloid on mitochondrial function may contribute to neurodegeneration in AD through energy failure and activation of apoptosis.A recent study of mitochondrial function in a transgenic model and in AD patients has shown that oxidative phosphorylation is inhibited by the presence of intracellular ␤-amyloid (6), leading to a reduction in ATP production. ATP depletion leads to partial membrane depolarization, release of the voltagedependent Mg 2ϩ block of NMDA receptors, increase in calcium influx, and a decrease in calcium buffering capacity (7). The increase in intracellular calcium enhances free radical generation and triggers several pathways that lead to cellular dysfunction and death (8). Examination of brains from patients suffering from AD identifies a high fraction of cells undergoing apoptosis, which is suggested as an important mechanism for neuronal cell loss (9). One of the major events related to activation of the intrinsic programmed ce...

show abstract

Flavonoids inhibit the expression of heat shock proteins.

Cited by 170 publications

References 30 publications

Expression of heat shock protein 70 in a permanent cell line (EPC) exposed to sediment extracts from the North Sea and the Baltic Sea

Expression of heat shock protein 70 in a permanent cell line (EPC) exposed to sediment extracts from the North Sea and the Baltic Sea

Effects of heat stimulation via microwave applicator on cartilage matrix gene and HSP70 expression in the rabbit knee joint

Differential Effects of Mitochondrial Heat Shock Protein 60 and Related Molecular Chaperones to Prevent Intracellular β-Amyloid-induced Inhibition of Complex IV and Limit Apoptosis

Contact Info

Product

Resources

About