Evidence for Enhanced Cytoprotective Function of HSP90-Overexpressing Small Intestinal Epithelial Cells

Tamaki, Kumiko; Otaka, Michiro; Takada, Makiko; Yamamoto, Soh; Odashima, Masaru; Watanabe, Sumio

doi:10.1007/s10620-010-1558-x

Cited by 12 publications

(9 citation statements)

References 33 publications

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“…18 Some previous animal studies indicate that HSP90 may have a dual role and increase inflammation in some conditions, while being protective and down-regulating inflammation in other conditions. [19][20][21] Fatigue has previously been an overlooked and ignored phenomenon in IBD but is increasingly recognised as one of the major problems for many patients. Clinically significant fatigue affects roughly 50% of patients at the time of diagnosis.…”

Section: Discussionmentioning

confidence: 99%

Heat-shock protein 90α in plasma reflects severity of fatigue in patients with Crohn’s disease

et al. 2019

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Heat-shock proteins (HSPs) are evolutionarily conserved proteins with important cellular homeostasis functions during harmful conditions, including inflammation. Some HSPs are secreted extracellularly and act on distant cells by down-regulating inflammation and increasing cellular stress defence mechanisms. HSP90α has been postulated to signal fatigue in chronic inflammation. We investigated whether HSP90α is associated with fatigue in patients with Crohn’s disease. Fifty-three patients with newly diagnosed Crohn’s disease were included in a cross-sectional study. Data on demographics and disease distribution were obtained. Fatigue was measured by the fatigue visual analogue scale (fVAS). Disease activity was assessed by the Simple Endoscopic Score for Crohn’s disease and Harvey Bradshaw Index. C-reactive protein, faecal calprotectin and HSP90α were also measured. The median fVAS score was 52 mm, indicating significant fatigue. HSP90α scores correlated significantly with fVAS ( r = 0.31, P = 0.03). In a multivariate regression model, HSP90α was the only significant contributor to fVAS scores (β = 0.31, P = 0.03). When patients were dichotomised into groups with high and low HSP90α concentrations, significantly higher fVAS scores were demonstrated in the group with high HSP90α ( M = 62.4, confidence interval 53.0–71.8 vs. 43.3, 31.6–55.0; P = 0.01). Thus, HSP90α may contribute to fatigue generation and/or modulation in patients with Crohn’s disease.

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Section: Discussionmentioning

confidence: 99%

Heat-shock protein 90α in plasma reflects severity of fatigue in patients with Crohn’s disease

et al. 2019

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“…HSP90 is another general cytosolic chaperone orchestrating the folding of many proteins including structural proteins and inducible proteins. However, HSP90 alone is insufficient to assist the refolding of partially denatured proteins and requires other chaperones, such as HSP70, to complete this task [36,37]. A decrease in the expression of HSP70 was sometimes detected in the proximal and midbody wall muscle tissues of animals exposed to heavy metals [38].…”

Section: Discussionmentioning

confidence: 99%

The Co-induced Effects of Molybdenum and Cadmium on Antioxidants and Heat Shock Proteins in Duck Kidneys

Xia

Luo

Liu

et al. 2015

Biol Trace Elem Res

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Molybdenum (Mo) is an essential element for human beings and animals; however, high dietary intake of Mo can lead to adverse reactions. Cadmium (Cd) is harmful to health. To investigate the toxicity of Mo combined with Cd in duck kidneys, 240 ducks were randomly divided into six groups and treated with a commercial diet containing Mo, Cd or Mo combined with Cd. Kidneys were collected on days 30, 60, 90 and 120 for determining the expression of heat shock proteins (HSPs), including HSP60, HSP70 and HSP90 in the kidney through quantitative RT-PCR. We also determined the antioxidant activity indexes in the kidney mitochondria. Moreover, kidney tissues at 120 days were subjected to histopathological analysis with the optical microscope. The results indicated that the expression of HSPs was highly significantly (P <0.01) upregulated in the kidneys of the combination groups and the Cd group. Exposure to Cd and a high dose of Mo decreased the total antioxidative capacity and the activity of xanthine oxidase, while malondialdehyde levels and the activity of nitric oxide synthase increased compared with those of the control groups in the kidney mitochondria. This was particularly evident at 90 and 120 days. Histopathological lesions included congestion and bleeding in the renal interstitium, swelling of the distal convoluted tubule epithelial cells, granular degeneration and blister degeneration in the renal tubular epithelial cells. These results suggest that a combination of Mo and Cd leads to greater tissue damage and has a synergistic effect on kidney damage. Oxidative damage of kidney mitochondria may be a potential nephrotoxicity mechanism of molybdenum and cadmium, and the high expression of HSPs may play a role in the resistance of kidney toxicity induced by Mo and Cd.

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“…Several studies have shown that elevation of Hsp70 in heart provided protection against stress-induced myocardial injury. Additionally, Hsp90 and Hsp60 might play an important role in protecting small intestinal epithelial and mucosal cells from hydrogen peroxide-induced or indomethacin-induced cell injury (Takada et al 2010;Tamaki et al 2011). The variations of Hsp27 expression are associated with strengthening of the cytoskeleton and an increased tolerance of the cell to injury induced by stress (Guay et al 1997).…”

Section: Discussionmentioning

confidence: 99%

The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts

Zhao

Zhang

Wang

et al. 2013

Cell Stress and Chaperones

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The aim of this study was to investigate the effects of cold stress on the expression levels of heat shock proteins (Hsps90, 70, 60, 40, and 27) and inflammatory factors (iNOS, COX-2, NF-κB, TNF-α, and PTGEs) and oxidative indexes in hearts of chickens. Two hundred forty 15-day-old male chickens were randomly divided into 12 groups and kept at the temperature of 12±1°C for acute and chronic cold stress. There were one control group and five treatment groups for acute cold stress, three control groups, and three treatment groups for chronic cold stress. After cold stress, malondialdehyde level increased in chicken heart; the activity of superoxide dismutase and glutathione peroxidase in the heart first increased and then decreased. The inflammatory factors mRNA levels were increased in cold stress groups relative to control groups. The histopathological analysis showed that heart tissues were seriously injured in the cold stress group. Additionally, the mRNA levels of Hsps (70, 60, 40, and 27) increased significantly (P<0.05) in the cold stress groups relative to the corresponding control group. Meanwhile, the mRNA level and protein expression of Hsp90 decreased significantly (P<0.05) in the stress group, and showed a gradually decreasing tendency. These results suggested that the levels of inflammatory factors and Hsps expression levels in heart tissues can be influenced by cold stress. Hsps commonly played an important role in the protection of the heart after cold stress.

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Evidence for Enhanced Cytoprotective Function of HSP90-Overexpressing Small Intestinal Epithelial Cells

Cited by 12 publications

References 33 publications

Heat-shock protein 90α in plasma reflects severity of fatigue in patients with Crohn’s disease

Heat-shock protein 90α in plasma reflects severity of fatigue in patients with Crohn’s disease

The Co-induced Effects of Molybdenum and Cadmium on Antioxidants and Heat Shock Proteins in Duck Kidneys

The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts

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