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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
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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
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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
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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
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Biochemical and Biophysical Research Communications, 1999
The small heat-shock proteins (sHsp), including Hsp27 and alphaB-crystallin, usually form large oligomers in cells. It has been suggested that the sHsp form oligomers by binding either a conserved C-terminal amino acid sequence or the less conserved N-terminal region. However, the site of binding has not been precisely determined. We used the yeast two-
C, Liu, M J, Welsh
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The small heat-shock proteins (sHsp), including Hsp27 and alphaB-crystallin, usually form large oligomers in cells. It has been suggested that the sHsp form oligomers by binding either a conserved C-terminal amino acid sequence or the less conserved N-terminal region. However, the site of binding has not been precisely determined. We used the yeast two-
C, Liu, M J, Welsh
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1997
Abstract Hsp25, Hsp28, mammalian small or low-molecular-weight heat shock protein (Arrigo, Landry, 1994). The nucleotide sequences of mammalian hsp27 genes encode proteins with highly conserved sequences. Hsp27.
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Abstract Hsp25, Hsp28, mammalian small or low-molecular-weight heat shock protein (Arrigo, Landry, 1994). The nucleotide sequences of mammalian hsp27 genes encode proteins with highly conserved sequences. Hsp27.
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Hsp27 as a Prognostic and Predictive Factor in Cancer
2002Once the diagnosis of a particular type of cancer has been established, the physicians need to know the aggressiveness of the tumor in order to decide which treatments should be applied. The aggressiveness of the malignant tumor is evaluated by the clinic (e.g., growth rate or given symptoms), by laboratory/image data (e.g., presence of tumor markers ...
Daniel R, Ciocca, Laura M, Vargas-Roig
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Structure–Functions of HspB1 (Hsp27)
2011Human HspB1 (also denoted Hsp27) is a well-known member, together with alphaB-crystallin, of the small heat-shock (or stress) proteins (sHsps) (20-40 kDa). In this chapter, I describe procedures for testing the oligomeric and phosphorylation patterns of HspB1 as well as its interaction with specific partner/client polypeptides using tissue culture ...
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Hsp27 Expression in Neuroblastoma: Correlation With Disease Stage
JNCI Journal of the National Cancer Institute, 1994The 27-kd heat shock protein (Hsp27) is differentially expressed in some malignancies, including breast carcinoma, leukemia, and malignant fibrous histiocytoma. In breast carcinoma, a high-level expression of Hsp27 has been associated with shorter disease-free survival in patients with localized disease.We have observed variable levels of Hsp27 among ...
D R, Ungar +7 more
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Protection of Neuronal and Cardiac Cells by HSP27
2002One of the aspects of heat shock protein biology, which has attracted the most attention, is their protective effect when over-expressed (for reviews see Latchman 1991; Yellon and Latchman 1992; Parsell and Lindquist 1993; Benjamin and McMillan 1998; Gray, et al. 1999).
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