Over-expression of HSP-70 protects astrocytes from combined oxygen-glucose deprivation

Papadopoulos, Marios C.; Sun, Xiao; Cao, Jianhua; Mivechi, Nahid F.; Giffard, Rona G.

doi:10.1097/00001756-199601310-00013

Cited by 80 publications

(50 citation statements)

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“…Scale bar, 10·µm. 3218 combined oxygen-glucose deprivation, and H2O2 exposure (Papadopoulos et al, 1996;Xu and Giffard, 1997). Overexpression of Hsp70 in cultured neurons is also associated with protection (Amin et al, 1996;Beaucamp et al, 1998;Fink et al, 1997;Uney et al, 1993), and overexpression of Hsp70 in astrocytes was found to protect cocultured wild type neurons (Xu et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…Ψ-2 or Phoenix packaging cells (a gift from Garry Nolan, Stanford University) were transfected with a retroviral plasmid containing inducible Hsp70 (Papadopoulos et al, 1996), or FLAG-hdj-2 (a gift from Don DeFranco; Qiao et al, 2003). Cells were infected with viral supernatant from the packaging cells as previously described (Papadopoulos et al, 1996).…”

Section: Transfection To Express Chaperonesmentioning

confidence: 99%

“…Cells were infected with viral supernatant from the packaging cells as previously described (Papadopoulos et al, 1996). Uninfected astrocytes and astrocytes expressing the control gene β-galactosidase (lac-Z) were used as controls (Papadopoulos et al, 1996;Xu and Giffard, 1997).…”

Section: Transfection To Express Chaperonesmentioning

confidence: 99%

See 2 more Smart Citations

Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury

Giffard

Zhao

et al. 2004

Journal of Experimental Biology

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188

127

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SUMMARY Chaperones, especially the stress inducible Hsp70, have been studied for their potential to protect the brain from ischemic injury. While they protect from both global and focal ischemia in vivo and cell culture models of ischemia/reperfusion injury in vitro, the mechanism of protection is not well understood. Protein aggregation is part of the etiology of chronic neurodegenerative diseases such as Huntington's and Alzheimer's, and recent data demonstrate protein aggregates in animal models of stroke. We now demonstrate that overexpression of Hsp70 in hippocampal CA1 neurons reduces evidence of protein aggregation under conditions where neuronal survival is increased. We have also demonstrated protection by the cochaperone Hdj-2 in vitro and demonstrated that this is associated with reduced protein aggregation identified by ubiquitin immunostaining. Hdj-2 can prevent protein aggregate formation by itself, but can only facilitate protein folding in conjunction with Hsp70. Pharmacological induction of Hsp70 was found to reduce both apoptotic and necrotic astrocyte death induced by glucose deprivation or oxygen glucose deprivation. Protection from ischemia and ischemia-like injury by chaperones thus involves at least anti-apoptotic,anti-necrotic and anti-protein aggregation mechanisms.

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Section: Discussionmentioning

confidence: 99%

Section: Transfection To Express Chaperonesmentioning

confidence: 99%

See 1 more Smart Citation

Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury

Giffard

Zhao

et al. 2004

Journal of Experimental Biology

Self Cite

188

127

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show abstract

“…Initial studies demonstrated induction of Hsp72 in cultured astrocytes exposed to heat shock or OGD (Bergeron et al, 1996) and further work confirmed that Hsp72 overexpression in astrocytes exposed to glucose deprivation (Xu and Giffard, 1997) or oxygen-glucose deprivation (Papadopoulos et al, 1996) was cytoprotective. Interestingly, overexpression of Hsp72 in astrocytes was shown to protect co-cultured neurons from ischemic injury (Xu et al, 1999); highlighting the integral role of astrocytes in neuronal homeostasis and survival.…”

Section: A Role For Hsp72 In Ischemiamentioning

confidence: 94%

Glial Cells, Inflammation and Heat Shock Proteins in Cerebral Ischemia

Tawfik¹,

White²,

Giffard³

2012

Advances in the Preclinical Study of Ischemic Stroke

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“…As an in vitro experiment, overexpression of Hsp70 inhibits apoptosis induced by ischemic stress in cardiomyocytes (Suzuki et al, 2002), astrocytes (Papadopoulos et al, 1996) and kidney cells (Meldrum et al, 2001). The mitochondrial chaperones Hsp60 and Hsp10 also protected cells from ischemic stress-induced apoptosis in cardiomyocytes (Lau et al, 1997;Lin et al, 2001).…”

Section: Antiapoptotic Functionmentioning

confidence: 99%