Over-expression of 70-kDa heat shock protein confers protection against monochloramine-induced gastric mucosal cell injury

Oyaké, Jinko; Otaka, Michiro; Matsuhashi, Tamotsu; Jin, Mario; Odashima, Masaru; Komatsu, Kyoji; Wada, Isao; Horikawa, Youhei; Ohba, Reina; Hatakeyama, Natsumi; Itoh, Hidenori; Watanabe, Sumio

doi:10.1016/j.lfs.2006.01.013

Cited by 52 publications

(53 citation statements)

References 35 publications

(37 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The apoptosis rate of intestinal epithelia inversely correlates with villus height and crypt depth and is accelerated by oxidative stress (Marshman et al 2001). Many studies have shown that the expression of Hsp70 was induced to prevent apoptosis and necrosis by gastrointestinal lesion of stress (Oyake et al 2006;Wada et al 2006). In addition, it has been reported that food restriction can affect Hsp70 expression in rats (Ahmad et al 1995).…”

Section: Discussionmentioning

confidence: 99%

“…Hsp70, one of the most abundant and best-characterized proteins in Hsps family, is a molecular chaperone involved in the folding of nascent and misfolded protein under nonstressful conditions. Hsp70 also protects the cells from various stresses (Oyake et al 2006). Since Hsp70 is a universal cytoprotection protein, it may enhance the tolerance to environmental changes or pathogenic conditions, increase the survival rate of stressed cells, and may also play critical role in cardiovascular diseases, organism decay, or cellular aging (Njemini et al 2007).…”

Section: Introductionmentioning

confidence: 99%

“…Since Hsp70 is a universal cytoprotection protein, it may enhance the tolerance to environmental changes or pathogenic conditions, increase the survival rate of stressed cells, and may also play critical role in cardiovascular diseases, organism decay, or cellular aging (Njemini et al 2007). Hsp70 has been known to protect intestinal epithelial cells from toxic agents and ulcerogenic conditions in gastrointestinal mucosa, where it is important location for digestion, absorption, and metabolism of nutrients and easily suffers injury from various stresses (Watanabe et al 2004;Oyake et al 2006). Overexpression of Hsp70 can accelerate ulcer healing by promoting cell proliferation, inhibiting cell apoptosis, and accelerating protein synthesis (Pierzchalski et al 2006).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Heat shock protein 70 is upregulated in the intestine of intrauterine growth retardation piglets

Zhong

Wang

Zhang

et al. 2010

Cell Stress and Chaperones

View full text Add to dashboard Cite

The objective of this study is to investigate the expression and distribution of heat shock protein 70 (Hsp70) in the intestine of intrauterine growth retardation (IUGR) piglets. Samples from the duodenum, prejejunum, distal jejunum, ileum, and colon of IUGR and normalbody-weight (NBW) piglets were collected at birth. The results indicated that the body and intestine weight of IUGR piglets were significantly lower than NBW piglets. The villus height and villus/crypt ratio in jejunum and ileum of IUGR piglets were significantly reduced compared to NBW piglets. These results indicated that IUGR causes abnormal gastrointestinal morphologies and gastrointestinal dysfunction. The mRNA of hsp70 was increased in prejejunum (P<0.05), distal jejunum (P<0.05), and colon in IUGR piglets. However, the hsp70 mRNA in ileum of piglets with IUGR was decreased. Similar to hsp70 mRNA, the protein levels of Hsp70 in prejejunum (P<0.05), distal jejunum, and colon (P<0.05) in IUGR piglets were higher than those in NBW piglets. These results indicated that the expression of Hsp70 in the intestinal piglets was upregulated by IUGR, and different intestinal sites had different responses to stress. Meanwhile, the localization of Hsp70 in the epithelial cells of the whole villi and intestinal gland rather than in the lamina propria and myenteron suggested that Hsp70 has a cytoprotective role in epithelial cell function and structure.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Heat shock protein 70 is upregulated in the intestine of intrauterine growth retardation piglets

Zhong

Wang

Zhang

et al. 2010

Cell Stress and Chaperones

View full text Add to dashboard Cite

show abstract

“…Certain Hsps, especially Hsp70, are thought to play particularly important roles in protection against stress-induced cardiac cell damage such as ischemia-reperfusion injury. Hsp70, one of the most abundant and best characterized Hsps, is a molecular chaperone involved in the folding of nascent and misfolded proteins under nonstressful conditions, and it plays a significant role in the protection of cells against various cellular stressors including heat (Čvoro et al, 1998;Evdonin et al, 2006), hypoxia (Dwyer et al, 1989), ultraviolet irradiation (Li et al, 2005), oxidative stress (Drummond and Steinhardt, 1987), and various others (Oyake et al, 2006). The overexpression of Hsp70 can accelerate ulcer healing by promoting cell proliferation, inhibiting cell apoptosis, and accelerating protein synthesis (Pierzchalski et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Association of heat shock protein 70 expression with rat myocardial cell damage during heat stress in vitro and in vivo

Chen¹,

Zhang²,

Cheng³

et al. 2015

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT.To investigate the mechanism of sudden death as a result of stress-induced damage to heart tissue and myocardial cells and to investigate the cardioprotective role of Hsp70 during heat stress, the distribution and expression of Hsp70 was evaluated in the heart cells of heat-stressed rats in vivo and heat-stressed H9c2 cells in vitro. After exposure to heat stress at 42°C for different durations, we observed a significant induction of CK, CK-MB, and LDH as well as pathologic lesions characterized by acute degeneration, suggesting that cell damage occurs from the onset of heat stress. Immunocytochemistry showed that Hsp70 was distributed mainly in the cytoplasm of myocardial cells in vivo and in vitro. Hsp70-positive signals in the cytoplasm were more prominent in intact areas than in degenerated areas after 60 min of heat stress. Hsp70 protein levels in myocardial cells in vitro decreased from the beginning to the end of heat stress. Hsp70 protein levels in rat heart 1995 Hsp70 in heat-stressed rat cardiac cells ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (1): 1994-2005 tissues in vivo decreased gradually with prolonged heat stress, with a slight increase at the beginning of heat stress. These results indicate that Hsp70 plays a role in the response of cardiac cells to heat stress and that decreased Hsp70 levels are associated with damage to rat myocardial cells in vitro and in vivo. Significant differences were found in hsp70 mRNA, which began to increase after 20 min of heat stress in vitro and after 40 min in vivo. This indicates that hysteresis is involved in mRNA expression after heat stress in vivo.

show abstract

“…Also, cathelicidin and ß defensins are cationic peptides that play roles in the innate defensive system at mucosal surfaces preventing bacterial colonization. These elements have been demonstrated in gastric epithelial cells, and they accelerate ulcer healing (Tarnawski et al, 1999;Oyaka et al, 2006;Tanaka et al, 2007;Tulassay & Herszényi, 2010). The trefoil factor family (TFFs) comprises a group of small peptides (6.5-12 kDa) secreted abundantly by surface epithelium, which has been demonstrated play an important role in mucosal integrity (Taupin & Podolsky, 2003).…”

Section: Epithelial "Barrier"mentioning

confidence: 99%

Gastric Ulcer Etiology

Silva¹,

Sousa²

2011

Peptic Ulcer Disease

View full text Add to dashboard Cite

Over-expression of 70-kDa heat shock protein confers protection against monochloramine-induced gastric mucosal cell injury

Cited by 52 publications

References 35 publications

Heat shock protein 70 is upregulated in the intestine of intrauterine growth retardation piglets

Heat shock protein 70 is upregulated in the intestine of intrauterine growth retardation piglets

Association of heat shock protein 70 expression with rat myocardial cell damage during heat stress in vitro and in vivo

Gastric Ulcer Etiology

Contact Info

Product

Resources

About