Results 121 to 130 of about 7,287 (179)
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HSP27 protects against ferroptosis of glioblastoma cells
Human Cell, 2021Ferroptosis, as an new form of non-apoptotic regulated cell death, plays an important role in human cancers. Although it is reported that HSP27 is an novel regulator of ferroptosis in cancer, it remains unknown how HSP27 affects ferroptosis in glioma. In this study, we examined the effect of HSP27 on the ferroptosis of glioblasotma.
Baohui Liu, Qianxue Chen, Yang Xu
exaly +4 more sources
International Journal of Radiation Oncology Biology Physics, 2011
HSP27 or HSP25 negatively regulates apoptosis pathways after radiation or chemotherapeutic agents. Abrogation of HSP27 function may be a candidate target for overcoming radio- and chemoresistance.Zerumbone (ZER), a cytotoxic component isolated from Zingiber zerumbet smith.
Joo-Won Nam +2 more
exaly +3 more sources
HSP27 or HSP25 negatively regulates apoptosis pathways after radiation or chemotherapeutic agents. Abrogation of HSP27 function may be a candidate target for overcoming radio- and chemoresistance.Zerumbone (ZER), a cytotoxic component isolated from Zingiber zerumbet smith.
Joo-Won Nam +2 more
exaly +3 more sources
Molecular and Cellular Endocrinology, 2007
Recently, we identified heat shock protein 27 (HSP27) as an estrogen receptor-beta (ERbeta) associated protein that acts as a co-repressor of estrogen signaling and serves as a biomarker of atherosclerosis. In this study, we sought to further characterize the subcellular interaction of HSP27 and ERbeta, as well as explore the factors that may modulate ...
William Gerthoffer +2 more
exaly +3 more sources
Recently, we identified heat shock protein 27 (HSP27) as an estrogen receptor-beta (ERbeta) associated protein that acts as a co-repressor of estrogen signaling and serves as a biomarker of atherosclerosis. In this study, we sought to further characterize the subcellular interaction of HSP27 and ERbeta, as well as explore the factors that may modulate ...
William Gerthoffer +2 more
exaly +3 more sources
Phytotherapy Research, 2022
Hepatocytes has been confirmed to undergo EMT and can be converted into myofibroblasts during hepatic fibrogenesis. However, the mechanism of hepatocyte EMT regulation in hepatic fibrosis, particularly through HSP27 (human homologue of rodent HSP25 ...
Xiaoling Zhang +3 more
semanticscholar +1 more source
Hepatocytes has been confirmed to undergo EMT and can be converted into myofibroblasts during hepatic fibrogenesis. However, the mechanism of hepatocyte EMT regulation in hepatic fibrosis, particularly through HSP27 (human homologue of rodent HSP25 ...
Xiaoling Zhang +3 more
semanticscholar +1 more source
Apoptosis, autophagy and atherosclerosis: relationships and the role of Hsp27.
Pharmacological Research, 2020Atherosclerosis is a multifactorial chronic inflammatory disease of the arterial wall, and an important pathological basis of coronary heart disease. Endothelial cells, vascular smooth muscle cells, and macrophages play important roles in the development
Ruiting Shan +3 more
semanticscholar +1 more source
The protective role of HSP27 in ocular diseases
Molecular Biology Reports, 2022Heat shock proteins (HSPs) are stress-induced proteins that are important constituents of the cell's defense system. The activity of HSPs enhances when the cell undergoes undesirable environmental conditions like stress. The protective roles of HSPs are due to their molecular chaperone and anti-apoptotic functions.
K, Sooraj +4 more
openaire +2 more sources
On the role of Hsp27 in regulating apoptosis
Apoptosis, 2003Heat shock proteins (Hsps) comprise several different families of proteins that are induced in response to a wide variety of physiological and environmental insults. One such protein which is highly induced during the stress response is a 27-kDa protein, termed Hsp27 whose expression is seen to correlate with increased survival in response to cytotoxic
C G, Concannon, A M, Gorman, A, Samali
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Hsp27 as a Therapeutic Target in Cancers
Current Drug Targets, 2014Heat shock protein 27 (Hsp27), induced by heat shock, environmental and pathophysiological stressors, is a multidimensional protein that acts as a protein chaperone and an antioxidant. This protein plays a major role in the inhibition of apoptosis and actin cytoskeletal remodeling.
Julie, Acunzo +4 more
openaire +2 more sources
Annals of the New York Academy of Sciences, 2000
Abstract: The heat shock protein HSP27 protects cells against a wide variety of toxic treatments and blocks apoptosis induced by exposures to anticancer drugs and activation of the death receptor fas. The molecular mechanisms of protection are unknown but appear to be regulated by phosphorylation of HSP27.
S J, Charette, J, Landry
openaire +2 more sources
Abstract: The heat shock protein HSP27 protects cells against a wide variety of toxic treatments and blocks apoptosis induced by exposures to anticancer drugs and activation of the death receptor fas. The molecular mechanisms of protection are unknown but appear to be regulated by phosphorylation of HSP27.
S J, Charette, J, Landry
openaire +2 more sources
Constitutive expression of Hsp27 in the rat cochlea
Hearing Research, 2002Heat shock protein-27 (Hsp27) is known to function as both a stress-inducible molecular chaperone and regulator of actin polymerization. For many cells in the cochlea, actin is part of the cytoskeleton and plays an important role in the maintenance of cochlear function.
Elena V, Leonova +3 more
openaire +2 more sources