Moderate Hypoxia Increases Heat Shock Protein 90 Expression in Excised Rat Aorta

Almgren, C.M.; Olson, L. Karl

doi:10.1159/000025675

Cited by 24 publications

(19 citation statements)

References 18 publications

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“…Indeed, it has been reported that hypoxia induces HSP70 and HSP90 family proteins in various systems. [9][10][11][12] However, it is not known whether small HSPs are also induced by hypoxia.…”

Section: Introductionmentioning

confidence: 99%

Differential Hypoxia Response of hsp-16 Genes in the Nematode

Hong

Kwon

Shim

et al. 2004

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 99%

Differential Hypoxia Response of hsp-16 Genes in the Nematode

Hong

Kwon

Shim

et al. 2004

Journal of Molecular Biology

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“…This increase was attributed to eNOS phosphorylation as well as increases in eNOS activity and NO production. [13][14][15][16] While it is known that hypoxia induces multiple vascular growth factors including VEGF and upregulates Hsp90 expression in various cell types including endothelial cells, 17,18 the role of hypoxia on Hsp90 binding to eNOS and eNOS phosphorylation in coronary artery endothelium has not been examined.…”

mentioning

confidence: 99%

Hypoxia increases Hsp90 binding to eNOS via PI3K-Akt in porcine coronary artery endothelium

Chen

Meyrick

2004

Laboratory Investigation

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This study examines the molecular mechanisms by which hypoxia regulates phosphorylated endothelial nitric oxide synthase (eNOS) activity and NO production in porcine coronary artery endothelial cells (PCAEC). Exposure to hypoxia (pO 2 ¼ 10 mmHg) for periods up to 3 h resulted in a time-dependent increase in eNOS protein expression and an early (15 min) and sustained increase in eNOS phosphorylation at Ser-1177. Exposure to hypoxia for 30 min led to a doubling in eNOS activity (control ¼ 6.274.4 vs hypoxia ¼ 14.175.0 fmol cGMP/lg protein, Po0.05) and NO release (control ¼ 5.970.8 vs hypoxia ¼ 11.871.2 nM/lg protein, Po0.05). Hypoxia also led to a significant increase in Akt phosphorylation and upregulation of Hsp90 binding to eNOS. Pretreatment of cells with either 1 lg/ml geldanamycin (a specific inhibitor of Hsp90) or 500 nM wortmannin (a specific PI3 kinase inhibitor) suppressed hypoxia-stimulated Akt and eNOS phosphorylation and significantly attenuated hypoxia-stimulated Hsp90 binding to eNOS. Both eNOS activity and NO production were inhibited by geldanamycin and wortmannin. Although hypoxia led to early activation of p42/44 mitogen-activated protein kinases (MAPK), inhibition of their pathway by PD98059 did not suppress hypoxia-stimulated eNOS phosphorylation and eNOS activity. These data demonstrate that hypoxia leads to increased eNOS phosphorylation via stimulated Hsp90 binding to eNOS and activation of the PI3-Akt pathway. We conclude that a coordinated interaction between Hsp90 and PI3-Akt may be an important mechanism by which eNOS activity and NO production is upregulated in hypoxic heart.

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“…Besides the fact that very few studies deal with the relationship between hypoxia and HSP-90 [54] or HSP expressions in general, the piglet model for the study of hypothermia on the protection against brain damage is of particular interest [55]. Moreover, HSP expression can serve for the onset of therapeutic trials at the early stages of perinatal life.…”

Section: Discussionmentioning

confidence: 99%

Perinatal Expression of Heat-Shock Protein 90 in Different Regions of the Brain and in Non-Neural Tissues of the Piglet

David¹,

Grongnet²

2001

Neonatology

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Important stressful events occur at birth or within the few hours that follow. To establish a possible involvement of stress proteins, expression of heat-shock protein 90 was determined by Western blotting in several regions of the brain and in non-neural tissues of the developing piglet (fetal to 10 days and adult). Expression was found in all the tissues studied. While comparable values were found in the whole brain during development, decreased expressions were observed from 4 to 8 h to 2 days after birth in cerebellum, cortex, hypothalamus and striatum. In hippocampus, low expression was observed from 4 h postnatally onward. In non-neural tissues, low expression was observed after birth and in the adult for heart, liver and lungs. In kidney, low values were found from birth to 1 day of age. Changes in environmental parameters like temperature and/or hypoxia can be related to differential expressions of heat-shock proteins and they possibly result in severe developmental outcomes. The results are discussed in terms of using the newborn piglet as a model for the study of different forms of stress on the heat-shock protein expression during postnatal development.

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Moderate Hypoxia Increases Heat Shock Protein 90 Expression in Excised Rat Aorta

Cited by 24 publications

References 18 publications

Differential Hypoxia Response of hsp-16 Genes in the Nematode

Differential Hypoxia Response of hsp-16 Genes in the Nematode

Hypoxia increases Hsp90 binding to eNOS via PI3K-Akt in porcine coronary artery endothelium

Perinatal Expression of Heat-Shock Protein 90 in Different Regions of the Brain and in Non-Neural Tissues of the Piglet

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