Characterization of Hypothermia-induced Cellular Stress Response in Mouse Tissues

Cullen, Katherine; Sarge, Kevin D.

doi:10.1074/jbc.272.3.1742

Cited by 74 publications

(47 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The combined treatment of GA and MPTP further increased Hsp70-HSE binding in the striatum when compared with groups pretreated with GA alone or treated with MPTP alone. The HSE binding, using the self-complementary HSE consensus oligonucleotide (5Ј-CTAGAAGCTTCTA-GAAGCTTCTAG-3Ј) (48), also showed a similar pattern of enhancement of HSE binding in the striatum of GA pretreated, MPTP-treated, or combined treated mice (data not shown). .…”

Section: Ga Pretreatment and Mptp Treatment Enhanced Hse Binding To Tmentioning

confidence: 69%

Geldanamycin Induces Heat Shock Protein 70 and Protects against MPTP-induced Dopaminergic Neurotoxicity in Mice

Shen

Wang

et al. 2005

Journal of Biological Chemistry

163

113

View full text Add to dashboard Cite

As key molecular chaperone proteins, heat shock proteins (HSPs) represent an important cellular protective mechanism against neuronal cell death in various models of neurological disorders. In this study, we investigated the effect as well as the molecular mechanism of geldanamycin (GA), an inhibitor of Hsp90, on 1-methyl-4-pheny-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity, a mouse model of Parkinson disease. Neurochemical analysis showed that pretreatment with GA (via intracerebral ventricular injection 24 h prior to MPTP treatment) increased residual dopamine content and tyrosine hydroxylase immunoreactivity in the striatum 24 h after MPTP treatment. To dissect out the molecular mechanism underlying this neuroprotection, we showed that the GA-mediated protection against MPTP was associated with a reduction of cytosolic Hsp90 and an increase in Hsp70, with no significant changes in Hsp40 and Hsp25 levels. Furthermore, in parallel with the induction of Hsp70, striatal nuclear HSF1 levels and HSF1 binding to heat shock element sites in the Hsp70 promoter were significantly enhanced by the GA pretreatment. Together these results suggested that the molecular cascade leading to the induction of Hsp70 is critical to the neuroprotection afforded by GA against MPTP-induced neurotoxicity in the brain and that pharmacological inhibition of Hsp90 may represent a potential therapeutic strategy for Parkinson disease. PD4 is the second most common human neurodegenerative disorder, affecting 1-3% of people over 65 years old and ϳ10% of those over 80 years old (1-4). The hallmark of PD pathology is the progressive loss of dopaminergic neurons in substantia nigra, leading to profound depletion of dopamine in the striatum, and consequently severe movement abnormalities (1, 3, 4). These pathological changes of PD are associated with formation of Lewy bodies (enriched for ␣-synuclein) in neuritis of dopaminergic and non-dopaminergic neurons (1, 5). For the last three decades, despite the symptomatic relief offered by L-3,4-dihydroxyphenylalanine, no effective neuroprotective strategy for PD has emerged to halt or slow down dopaminergic neurodegeneration (1, 3-6).Heat shock proteins (HSPs) represent an important cellular protective mechanism against a variety of stresses and insults (7-9). HSPs are a large family of evolutionary conserved proteins consisting of subfamilies with molecular masses of ϳ110, 90, 70, 60,40,[15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30]10,11). Some HSPs (such as Hsp40 and Hsp90) are constitutively expressed, whereas others (such as Hsp70 and Hsp27) are mainly induced after exposure of cells to environmental and physiological stressors (12)(13)(14)(15). A large body of evidence supports a critical role for HSPs in cellular protection against a variety of stressors and insults, including heat, hypoxia, ischemia, excitotoxicity, glucose deprivation, cancer, and aging (13, 16 -24 (32,33). Similarly, overexpression of Hsp70 in dopaminergic neurons using adeno-associa...

show abstract

Section: Ga Pretreatment and Mptp Treatment Enhanced Hse Binding To Tmentioning

confidence: 69%

Geldanamycin Induces Heat Shock Protein 70 and Protects against MPTP-induced Dopaminergic Neurotoxicity in Mice

Shen

Wang

et al. 2005

Journal of Biological Chemistry

163

113

View full text Add to dashboard Cite

show abstract

“…Cullen and Sarge (1997) reported that hypothermia elevated hsp 72 mRNA expression in the brain, heart, kidney, liver and lungs of mice. On the contrary, Matz et al (1995) noted hsp induction in the brown adipose tissue of cold-stressed mice but not in the brain, heart and lungs.…”

Section: Discussionmentioning

confidence: 99%

A note on heat shock protein 70 expression in goats subjected to road transportation under hot, humid tropical conditions

Zulkifli

Norbaiyah

Yoke-Kqueen

et al. 2010

Animal

View full text Add to dashboard Cite

The influence of two different stocking densities (0.20 m 2 /animal and 0.40 m 2 /animal) in transit under the hot, humid tropical conditions on heat shock protein (hsp) 70 induction was investigated in 60 Boer does. The animals were road transported for 3 h and the control group was kept under normal conditions in the farm. Irrespective of stocking density, transportation significantly increased hsp 70 densities ( P , 0.05) in the kidneys. The hsp 70 response in the kidneys was more profound compared with those of heart tissues. Higher stocking density was more stressful to the goats based on hsp 70 expression. These results suggest that, irrespective of stocking density, transportation under hot, humid tropical conditions evoked hsp 70 reactions.

show abstract

“…Cells subjected to a nonlethal heat shock increase cellular HSP70 levels, and those levels correlate with a transient resistance to higher, normally lethal temperatures (29). A review of results suggests that inactivation of either of the two genes (Hsp70.1 and Hsp70.3) results in deficient maintenance of acquired thermotolerance and increased sensitivity to heat stress-induced apoptosis (8,19,27). The synthetic or protein rescue functions of HSP70 are counterbalanced by participation in the ubiquitin pathway that clears the cell of unstable or damaged proteins by proteosome degradation (2).…”

Section: Discussionmentioning

confidence: 99%

Genomic Instability and Enhanced Radiosensitivity in Hsp70.1- and Hsp70.3-Deficient Mice

Hunt

Dix

Sharma

et al. 2004

Molecular and Cellular Biology

222

233

View full text Add to dashboard Cite

show abstract

Characterization of Hypothermia-induced Cellular Stress Response in Mouse Tissues

Cited by 74 publications

References 30 publications

Geldanamycin Induces Heat Shock Protein 70 and Protects against MPTP-induced Dopaminergic Neurotoxicity in Mice

Geldanamycin Induces Heat Shock Protein 70 and Protects against MPTP-induced Dopaminergic Neurotoxicity in Mice

A note on heat shock protein 70 expression in goats subjected to road transportation under hot, humid tropical conditions

Genomic Instability and Enhanced Radiosensitivity in Hsp70.1- and Hsp70.3-Deficient Mice

Contact Info

Product

Resources

About