Mutation of Amino Acids 246-251 Alters Nuclear Accumulation of Human Heat Shock Protein (HSP) 72 with Stress, But Does Not Reduce Viability

1999 ◽  
Vol 31 (3) ◽  
pp. 523-532 ◽  
Author(s):  
A.A. Knowlton
Keyword(s):  
Amino Acids ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Nuclear Accumulation ◽  
Human Heat Shock Protein

scholarly journals C-terminal amino acids are essential for human heat shock protein 70 dimerization

2014 ◽  
Vol 20 (1) ◽  
pp. 61-72 ◽  
Author(s):  
Guillaume Marcion ◽  
Renaud Seigneuric ◽  
Evelyne Chavanne ◽  
Yves Artur ◽  
Loïc Briand ◽  
...  
Keyword(s):  
Amino Acids ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Terminal Amino ◽  
Human Heat Shock Protein

scholarly journals Stimulation of the Human Heat Shock Protein 70 Promoter in Vitro by Simian Virus 40 Large T Antigen

1989 ◽  
Vol 264 (27) ◽  
pp. 16160-16164
Author(s):  
I C Taylor ◽  
W Solomon ◽  
B M Weiner ◽  
E Paucha ◽  
M Bradley ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Large T Antigen ◽  
Human Heat Shock Protein ◽  
Stimulation Of

scholarly journals Circulating Human Heat Shock Protein 60 in the Plasma of British Civil Servants

Circulation ◽  
2002 ◽  
Vol 106 (2) ◽  
pp. 196-201 ◽  
Author(s):  
Jo Lewthwaite ◽  
Natalie Owen ◽  
Anthony Coates ◽  
Brian Henderson ◽  
Andrew Steptoe
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Civil Servants ◽  
Heat Shock Protein 60 ◽  
Human Heat Shock Protein

High level soluble expression and ATPase characterization of human heat shock protein GRP78

2017 ◽  
Vol 82 (2) ◽  
pp. 186-191
Author(s):  
Shuang Wu ◽  
Hongpeng Zhang ◽  
Miao Luo ◽  
Ke Chen ◽  
Wei Yang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Soluble Expression ◽  
High Level ◽  
Human Heat Shock Protein

Genomic Cloning of a Human Heat Shock Protein 40 (Hsp40) Gene (HSPF1) and Its Chromosomal Localization to 19p13.2

Genomics ◽  
1996 ◽  
Vol 38 (3) ◽  
pp. 446-449 ◽  
Author(s):  
Mami Hata ◽  
Katsuzumi Okumura ◽  
Masao Seto ◽  
Kenzo Ohtsuka
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Chromosomal Localization ◽  
Genomic Cloning ◽  
Human Heat Shock Protein

scholarly journals Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70

2005 ◽  
Vol 289 (4) ◽  
pp. C1034-C1041 ◽  
Author(s):  
Mohamed Kodiha ◽  
Angel Chu ◽  
Omar Lazrak ◽  
Ursula Stochaj
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Level ◽  
Nuclear Accumulation ◽  
Stress Exposure ◽  
Nucleocytoplasmic Shuttling ◽  
Nuclear Compartment ◽  
Intracellular Targeting ◽  
Shock Proteins

Heat shock proteins of the hsp/hsc70 family are essential chaperones, implicated in the stress response, aging, and a growing number of human diseases. At the molecular level, hsc70s are required for the proper folding and intracellular targeting of polypeptides as well as the regulation of apoptosis. Cytoplasmic members of the hsp/hsc70 family are believed to shuttle between nuclei and cytoplasm; they are found in both compartments of unstressed cells. Our experiments demonstrate that actin filament-destabilizing drugs trigger the nuclear accumulation of hsc70s in unstressed and heat-shocked cells recovering from stress. Using human-mouse heterokaryons, we show that stress inhibits shuttling and sequesters the chaperone in nuclei. The inhibition of hsc70 shuttling upon heat shock is only transient, and transport is reestablished when cells recover from stress. Hsc70 shuttling is controlled by hsc70 retention in the nucleus, a process that is mediated by two distinct mechanisms, ATP-sensitive binding of hsc70s to chaperone substrates and, furthermore, the association with nucleoli. The nucleolar protein fibrillarin and ribosomal protein rpS6 were identified as components that show an increased association with hsc70s in the nucleus upon stress exposure. Together, our data suggest that stress abolishes the exit of hsc70s from the nucleus to the cytoplasm, thereby limiting their function to the nuclear compartment. We propose that during recovery from stress hsc70s are released from nuclear and nucleolar anchors, which is a prerequisite to restore shuttling.

ANALYSIS OF THE POLYMORPHIC HUMAN HEAT SHOCK PROTEIN 70 GENES IN SEVERE SEPSIS

Shock ◽  
1997 ◽  
Vol 7 (Supplement) ◽  
pp. 20
Author(s):  
S Schröder ◽  
M Reck ◽  
A Hoeft ◽  
F Stüber
Keyword(s):  
Severe Sepsis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Human Heat Shock Protein
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