Results 1 to 10 of about 7,287 (179)
The Role of Hsp27 in Chemotherapy Resistance
Biomedicines, 2022 Heat shock protein (Hsp)-27 is a small-sized, ATP-independent, chaperone molecule that is overexpressed under conditions of cellular stress such as oxidative stress and heat shock, and protects proteins from unfolding, thus facilitating proteostasis and ...
Spyridon Voulgaris +2 more
exaly +5 more sources
Cells, 2022 Heat shock protein 27 (HSP27) is a protein that works as a chaperone and an antioxidant and is activated by heat shock, environmental stress, and pathophysiological stress. However, HSP27 dysregulation is a characteristic of many human cancers.
Haruna Isiyaku Umar +17 more
doaj +2 more sources
Biochemistry Research International, 2011 Hsp27 oligomer is reported to interact with F-actin as a barbed-end-capping protein. The present study determined the binding strength and stoichiometry of the interaction using fluorescence of probes attached to Hsp27 cysteine-137.
Philip Graceffa
doaj +3 more sources
Translocation of HSP27 and MKBP in Ischemic Heart.
Cell Structure and Function, 1999 HSP27 and MKBP translocate from the cytosolic to myofibril fraction in ischemic rat heart as demonstrated by immunoblotting. Immunohistochemistry analysis showed that ischemia enhances the Z line labeling of HSP27 and MKBP. Two dimensional gel electrophoresis showed that ischemia increases the hyperphosphorylated form of HSP27.
Shigeo Ohno, , Toshihiko Aki
exaly +4 more sources
Biological Significance of Decreased HSP27 in Human Atherosclerosis [PDF]
Arteriosclerosis, Thrombosis, and Vascular Biology, 2006 Objective— Because culprit atherosclerotic plaques contain proteases, we hypothesized that the diminished heat shock protein 27 (HSP27) released by atherosclerotic plaques could be due to proteolysis. We assessed the role of HSP27 in human vascular smooth muscle cells (VSMCs) under proteolytic injury.
Jean-Baptiste Michel +2 more
exaly +3 more sources
Cell Reports, 2023 SUMMARY In response to lysosomal damage, cells engage several quality-control mechanisms, including the selective isolation and degradation of damaged lysosomes by lysophagy. Here, we report that the selective autophagy adaptor SQSTM1/p62 is recruited to
Elizabeth R. Gallagher, E. Holzbaur
semanticscholar +1 more source
Journal of Controlled Release, 2023 Ischemic stroke causes brain endothelial cell (BEC) death and damages tight junction integrity of the blood-brain barrier (BBB). We harnessed the innate mitochondrial load of endothelial cell-derived extracellular vesicles (EVs) and utilized mixtures of ...
Kandarp M Dave +17 more
semanticscholar +1 more source
Sensitized heat shock protein 27 induces retinal ganglion cells apoptosis in rat glaucoma model [PDF]
International Journal of Ophthalmology, 2020 AIM: To investigate the relationships between the changes of heat shock protein 27 antibody (anti-HSP27) in serum/cerebrospinal fluid (CSF), intraocular pressure (IOP), retinal ganglion cell (RGC) apoptosis in a rat glaucoma model and disclose the ...
Wei Zhao +5 more
doaj +1 more source
The heat shock protein Hsp27 controls mitochondrial function by modulating ceramide generation
Cell Reports, 2023 SUMMARY Sphingolipids have key functions in membrane structure and cellular signaling. Ceramide is the central molecule of the sphingolipid metabolism and is generated by ceramide synthases (CerS) in the de novo pathway.
Rowan Boyd +9 more
semanticscholar +1 more source
Di-san junyi daxue xuebao, 2021 Objective To explore the role and underlying mechanism of heat shock protein 27 (HSP27) in bladder smooth muscle remodeling after bladder outlet obstruction (BOO).
LIAO Deyang +5 more
doaj +1 more source