نتایج جستجو برای: hsp27 mutation
تعداد نتایج: 292757 فیلتر نتایج به سال:
AIM Heat shock proteins (HSP) are an evolutionary conserved family of proteins that serve as molecular chaperones, preventing the formation of nonspecific protein aggregates and assisting proteins in the acquisition of their native structures. Furthermore, HSPs have anti-apoptotic properties and have been found to be elevated in many human cancers; their overexpression has been associated with ...
AIM After immediate teeth separation, expression of HSP27 in the mouse dental pulp was examined. Immunohistochemistry was performed to examine the incidence of HSP27 expression. MATERIALS AND METHODS A total of 36 8-week-old ddY mice were used as experimental subjects and a wedge was inserted in between maxillary right molars. The wedge was removed 30 min or 3 h after insertion. Animals were ...
Objectives. Elevated plasma homocysteine (Hcy) could lead to endothelial dysfunction and is viewed as an independent risk factor for atherosclerosis. Heat shock protein 27 (HSP27), a small heat shock protein, is reported to exert protective effect against atherosclerosis. This study aims to investigate the protective effect of HSP27 against Hcy-induced endothelial cell apoptosis in human umbili...
We previously reported that transforming growth factor-β (TGF-β) stimulates heat shock protein 27 (HSP27) induction through p44/p42 mitogen-activated protein (MAP) kinase, p38 MAP kinase and stress-activated protein kinase/ c-Jun N-terminal kinase (SAPK/JNK) in osteoblast-like MC3T3-E1 cells. In addition, we recently reported that the Rho-kinase inhibitors Y27632 and fasudil suppressed the TGF-...
BACKGROUND The recent discovery of the classical estrogen receptor alpha (ERalpha) in androgen-insensitive prostate cancer has shed new light on the role of estrogens in endocrine therapy failure. To get more information on downstream events of estrogen signaling in these tumors, we investigated the relation between ERalpha gene expression, and the estrogen-inducible heat shock protein HSP27 in...
The present study established a heat-stressed rat heart model, and used an H9c2 myocardial cell line to investigate the expression profiles of heat shock protein (Hsp)27 and αB-crystallin, both in vivo and in vitro. Rats and myocardial cells were subjected to 42 ˚C for 0, 20, 40, 60, 80 or 100 min, following which the mRNA and protein expression levels of Hsp27 and αB-crystallin were measured. ...
BACKGROUND αB-crystallin and HSP27 are mammalian intracellular small heat shock proteins. RESULTS These proteins exchange subunits in a rapid and temperature-dependent manner. CONCLUSION This facile subunit exchange suggests that differential expression could be used by the cell to regulate the response to stress. SIGNIFICANCE A robust technique defines parameters for the dynamic interact...
PURPOSE The role of heat shock proteins (Hsp) in injury response has been well established, but it is now becoming apparent that the phosphorylation state of Hsp27 may be a critical determinant of its ability to act in a protective capacity. In this study, the expression of Hsp27 and its phosphorylation were evaluated in an experimental glaucoma model in Brown Norway rats and in a spontaneous m...
Although nephrotic syndrome is a very common kidney disease, little is known about the molecular changes occurring within glomerular capillary loops during development of disease. The characteristic histologic change is retraction (effacement) of the distal “foot” processes of glomerular epithelial cells (GEC) which surround the capillary loops. The GEC foot processes are an essential part of t...
In SH-SY5Y human neuroblastoma cells, the cholinergic agonist, carbachol, stimulates phosphorylation of the small heat shock protein 27 (HSP27). Carbachol increases phosphorylation of both Ser-82 and Ser-78 while the phorbol ester, phorbol-12, 13-dibutyrate (PDB) affects only Ser-82. Muscarinic receptor activation by carbachol was confirmed by sensitivity of Ser-82 phosphorylation to hyoscyamin...
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