Induction of heat shock proteins (HSPs) by sodium arsenite in cultured astrocytes and reduction of hydrogen peroxide-induced cell death

Neurospora crassa cells, grown at 28 °C for 14 h and heat shocked at 48 °C for 45 min, showed the synthesis of 11 heat-shock proteins (nHSPs) in one-dimensional electrophoretic profiles. Treatment with sodium arsenite induced the synthesis of two heat-shock proteins, nHSP70 and nHSP80, and a third, arsenite-specific protein, not induced by hyperthermia. Exposure to 0.5 or 1.0 mM H2O2 led to the induction of two of the heat-inducible nHSP70 family polypeptides. Sodium selenite, used in concert with H2O2, and arsenite were observed to modulate that heat-shock response. In addition, H2O2, menadione, and the glutathione depleters diamide and diethyl maleate promoted the synthesis of another protein, designated oxidative stress-responsive protein (OSP). A DNA-binding protein, specific for Neurospora DNA, was also demonstrated in extracts of heat-shocked cells.

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201; HEAT SHOCK PROTEINS (HSPs) PROTECTED CARDIAC MYOCYTES AGAINST INJURY INDUCED BY HYDROGEN PEROXIDE(H2O2)

Shock ◽

10.1097/00024382-199401001-00202 ◽

1994 ◽

Vol 1 (Supplement) ◽

pp. 56

Author(s):

Meidong Liu ◽

Xianzhong Xiao ◽

Zhengyao Luo

Keyword(s):

Hydrogen Peroxide ◽

Heat Shock ◽

Heat Shock Proteins ◽

Cardiac Myocytes ◽

Shock Proteins

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Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway

International Immunology ◽

10.1093/intimm/12.11.1539 ◽

2000 ◽

Vol 12 (11) ◽

pp. 1539-1546 ◽

Cited By ~ 869

Author(s):

Sreyashi Basu ◽

Robert J. Binder ◽

Ryuichiro Suto ◽

Kirstin M. Anderson ◽

Pramod K. Srivastava

Keyword(s):

Cell Death ◽

Dendritic Cells ◽

Heat Shock ◽

Heat Shock Proteins ◽

Apoptotic Cell ◽

Apoptotic Cell Death ◽

Shock Proteins

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Heat Shock Proteins: Endogenous Modulators of Apoptotic Cell Death

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.2001.5427 ◽

2001 ◽

Vol 286 (3) ◽

pp. 433-442 ◽

Cited By ~ 518

Author(s):

Carmen Garrido ◽

Sandeep Gurbuxani ◽

Luigi Ravagnan ◽

Guido Kroemer

Keyword(s):

Cell Death ◽

Heat Shock ◽

Heat Shock Proteins ◽

Apoptotic Cell ◽

Apoptotic Cell Death ◽

Shock Proteins ◽

Endogenous Modulators

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Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death

The International Journal of Biochemistry & Cell Biology ◽

10.1016/j.biocel.2012.04.002 ◽

2012 ◽

Vol 44 (10) ◽

pp. 1622-1631 ◽

Cited By ~ 177

Author(s):

Julie Acunzo ◽

Maria Katsogiannou ◽

Palma Rocchi

Keyword(s):

Cell Death ◽

Heat Shock ◽

Heat Shock Proteins ◽

Small Heat Shock Proteins ◽

Αb Crystallin ◽

Shock Proteins

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Heat shock protein synthesis over time in infective Trichinella spiralis larvae raised in suboptimal culture conditions

Journal of Helminthology ◽

10.1079/joh2003225 ◽

2004 ◽

Vol 78 (3) ◽

pp. 243-247 ◽

Cited By ~ 9

Author(s):

J. Martinez ◽

J. Perez-Serrano ◽

W.E. Bernadina ◽

I. Rincon ◽

F. Rodriguez-Caabeiro

Keyword(s):

Cell Death ◽

Protein Synthesis ◽

Heat Shock ◽

Heat Shock Proteins ◽

Heat Shock Protein ◽

Trichinella Spiralis ◽

Culture Conditions ◽

Induce Stress ◽

Shock Proteins ◽

Over Time

AbstractChanges in the viability, infectivity and heat shock protein (Hsp) levels are reported in Trichinella spiralis first stage larvae (L1) stored in 199 medium for up to seven days at 37°C. These conditions induce stress that the larvae, eventually, cannot overcome. After three days of storage, the infectivity and viability were unchanged, although higher Hsp70 levels were observed. After this time, larvae gradually lost viability and infectivity, coinciding with a decrease in Hsp70 and Hsp90 and an increase in actin (a housekeeping protein). In addition, a possibly inducible heat shock protein, Hsp90i, appeared as constitutive Hsp90 disappeared. No significant changes in Hsp60 levels were detected at any time. These results suggest that heat shock proteins initially try to maintain homeostasis, but on failing, may be involved in cell death.

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SECOND ANOXIA-REOXYGENATION DOES NOT CAUSE THE APOPTOTIC CELL DEATH OF NEONATAL CARDIOMYOCYTES: POSSIBLE ROLE OF CHANGES OF mRNA EXPRESSION OF CYTOPROTECTIVE GENES

Fiziolohichnyĭ zhurnal ◽

10.15407/fz55.01.019 ◽

2009 ◽

Vol 55 (1) ◽

pp. 19-26

Author(s):

O.V. Surova ◽

◽

V.E. Dosenko ◽

V.S. Nagibin ◽

L.V. Tumanovskaya ◽

...

Keyword(s):

Cell Death ◽

Heat Shock ◽

Heat Shock Proteins ◽

Apoptotic Cell ◽

First Episode ◽

Mrna Levels ◽

Neonatal Cardiomyocytes ◽

Genes Expression ◽

Shock Proteins

The cells death and genes expression in neonatal cardiomyocytes culture at two anoxia-reoxygenation modeling were investigated. The primary culture of neonatal cardiomyocytes was undergone 30 min of anoxia followed by 24 h (A-R1) and the second anoxia-reoxygenation – 30 min and 60 min respectively (A-R2). The percentages of living, necrotic, apoptotic and autophagic cells were determined by staining with bis-benzimide, propidium iodide and monodansylcadaverine. Anoxia-reoxygenation significantly influenced the ratio of living, necrotic, apoptotic and autophagic cells both at its first A-R1 and second A-R2 episodes. It was shown that the main mechanism of cell death after the both periods of anoxia-reoxygenation is necrosis. The changes of mRNA levels of genes of heat shock proteins HSP70 and HSP90, antiapoptotic protein Bcl2 and key regulator of au-tophagy FRAP in cardiomyocytes culture were established. The data obtained allow to make suggestion that in 24 h after the first episode of anoxia-reoxygenation A-R1 the overexpression of heat shock proteins starts the cascade of reactions that causes the necrotic cell death prevalent and the blocking of apoptotic program at second anoxia-reoxygenation A-R2.

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