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

David, Jean‐Claude; Grongnet, Jean‐François

doi:10.1159/000047079

Cited by 9 publications

(9 citation statements)

References 45 publications

(50 reference statements)

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“…The major stress inducible Hsp (Hsp70) confers myocardial protection from ischemia (McGuinness et al 2006). The Hsp kDa family of HSPs displays important functions like stabilizing target proteins in unassembled state (David and Grongnet 2001). However, it cannot be excluded that the abundant Hsp70 reaction can be influenced by cross reactivity with other Hsp members.…”

Section: Discussionmentioning

confidence: 99%

Expression and distribution of heat shock proteins in the heart of transported pigs

Bao

Sultan

Nowak

et al. 2008

Cell Stress and Chaperones

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Section: Discussionmentioning

confidence: 99%

Expression and distribution of heat shock proteins in the heart of transported pigs

Bao

Sultan

Nowak

et al. 2008

Cell Stress and Chaperones

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“…Specificity of anti-HSP27 (15), anti-HSP70 (16), and anti-HSP90 (17) has been previously established.…”

Section: Experimental Methodsmentioning

confidence: 99%

“…HSPs are classified in three large families according to their molecular weights (11)(12)(13). However, very few studies have described the developmental changes of HSPs at the time of birth (15)(16)(17). The protective role of HSPs against hypoxia at birth has not been investigated, although in the brain, these proteins are known to be cytoprotective after hypoxia-ischemia (18,19).…”

mentioning

confidence: 99%

Effects of Hypoxia on Stress Proteins in the Piglet Brain at Birth

et al. 2004

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Newborn piglets were submitted to normobaric hypoxia (5% O 2 , 95% N 2 ) for either 1 or 4 h. The effects of hypoxia on the neonatal brain were characterized through a time-course analysis of levels of various proteins such as heat shock proteins (HSP27, 70, and 90), hypoxia inducible factor-1␣ (HIF-1␣), neuronal nitric oxide synthase (nNOS), hemeoxygenase-2 (HO-2), and caspase-3. The expression of these proteins was determined at different stages of recovery up to 72 h in cerebellum, cortex, and hippocampus by Western blot analysis in hypoxic maintained animals that were made hypoxic at either 20 or 37°C. In all regions of the brain, HIF-1␣ and HSP27 expression were strongly increased until 22 h of recovery. No significant changes were observed for HSP70, HSP90, and HO-2. A small elevation of expression of nNOS was observed at early stages in the cerebellum and the cortex with no change in the hippocampus.Expression of caspase 3 was strongly increased in the cortex 24 and 48 h after hypoxia but unchanged in the hippocampus. These results are presented in terms of the porcine model of nonischemic hypoxia and its delayed neuronal effects on the cerebral outcome. Because of their recently established biochemical and functional interactions, the expression of the main HSPs, HIF-1␣, nNOS, and caspase-3 after hypoxia are delineated. Perinatal asphyxia and hypoxia are common causes of neonatal morbidity. Among survivors, several disabilities are observed, including pulmonary, renal, cardiac, and encephalopathic dysfunction (1,2). Asphyxia at birth can result in severe auditory problems for the infant (3,4) as well as increased risks of amnesia (5) and schizophrenia presenting at different stages (6). Outcomes of asphyxia and/or hypoxia-ischemia can also result in cognitive impairment and developmental delay for the infants (7). Such severe sequelae of birth hypoxia are apparent early at the molecular level in the brain. Impairment as a result of hypoxia includes the transient reduction of GABA receptor numbers (8), altered expression of glutamate transporters (9), and/or a disruption of myelin gene expression (10). Because of the severe consequences of hypoxia at birth time on cerebral functions, a better characterization of molecular changes within the hypoxic neonatal brain is of crucial importance.The study of the expression and induction of stress proteins in the hypoxic brain is of particular interest because heat shock proteins (HSPs) have cytoprotective properties and are induced after a variety of stressors, such as elevated temperature (11-13) or hypoxia (14). HSPs are classified in three large families according to their molecular weights (11-13). However, very few studies have described the developmental changes of HSPs at the time of birth (15-17). The protective role of HSPs against hypoxia at birth has not been investigated, although in the brain, these proteins are known to be cytoprotective after hypoxia-ischemia (18,19). Other proteins induced by neonatal hypoxic stress are also of interest. Hypoxia i...

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“…The sources and dilutions of antibodies are indicated in Table 1. Specificity of anti-Hsp27 (David et al 2001a), Hsp70 (David et al 2001b), and ␣B-crystallin (Tallot et al 2003), as well as anti-HspB8, B20 (Verschuure et al 2003) have been previously established. After overnight incubation at room temperature, the blots were washed 5 ϫ 5 minutes in the TBST buffer and 5% skim milk powder containing the second antibody (1:1000 anti-rabbit immunoglobulin G peroxidase coupled from Sigma).…”

Section: Western Blot Analysismentioning

confidence: 99%

“…This model presents several important molecular features for the study of stressassociated cerebral outcomes (David et al 2001a(David et al , 2001b. It displays several common similarities with the human infant after a hypoxic episode.…”

Section: Introductionmentioning

confidence: 99%

Effects of hypoxia on stress proteins in the piglet heart at birth

Louapre

Grongnet²,

Tanguay

et al. 2005

Cell Stress Chaper

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Hypoxia at birth represents a very stressful event that can result in severe lifelong consequences in different tissues, including those of the heart. Heat shock and other associated stress proteins are involved in cellular protection, but their roles are not clearly defined at the time of birth. Newborn piglets were subjected to 5% oxygen and 95% nitrogen for either 1 or 4 hours. They were allowed to recover over periods of 1 to 68 hours. The relative levels of ␣B-crystallin, HspB8, Hsp20, Hsp27, Hsp60, and Hsp70 as well as nitric oxide synthases (NOS) (endothelial NOS, inducible NOS, neuronal NOS) were examined by Western blot analysis. Surprisingly, ␣B-crystallin expression was drastically increased in animals submitted to hypoxia. The hypoxia-associated factor HIFI␣ was also strongly and rapidly overexpressed. Heme oxygenase 1 was also increased. To a lesser extent, neuronal NOS was also increased in the left ventricle of animals submitted to hypoxia. This work clearly shows that the Hsp chaperone ␣B-crystallin is strongly overexpressed in the left ventricle of animals submitted to hypoxia. This observation dissociates the response to low oxygenation of ␣B-crystallin and other stress-associated proteins including Hsp27, and it indicates that heme oxygenase is not alone among HSPs in its oxygen-related gene expression.

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

Cited by 9 publications

References 45 publications

Expression and distribution of heat shock proteins in the heart of transported pigs

Expression and distribution of heat shock proteins in the heart of transported pigs

Effects of Hypoxia on Stress Proteins in the Piglet Brain at Birth

Effects of hypoxia on stress proteins in the piglet heart at birth

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