Expression of mRNA species encoding heat shock protein 90 (hsp90) in control and hyperthermic rabbit brain

Quraishi, Hania; Rush, Sheila J.; Brown, Ian R.

doi:10.1002/(sici)1097-4547(19960201)43:3<335::aid-jnr8>3.0.co;2-k

Cited by 18 publications

(5 citation statements)

References 66 publications

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“…This protein is a useful marker of cellular stress due to their high constitutive levels of hsc70 protein in many cell types; however, previous studies both in [18,20]. In addition to hsc70, neurons express high vivo and in vitro have indicated that induction of hsp70 constitutive levels of hsp90 mRNA and protein which is dampened in several neuronal cell populations folmay also contribute to this buffering [39,40]. Cells lowing heat shock compared to glial cells [21,23].…”

Section: Discussionmentioning

confidence: 99%

The Neuronal Stress Response: Nuclear Translocation of Heat Shock Proteins as an Indicator of Hyperthermic Stress

Manzerra

Brown

1996

Experimental Cell Research

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Two characteristic features of the heat shock response, (i) induction of hsp70 protein and (ii) nuclear translocation of constitutive hsc70 and stress-inducible hsp70 protein, were utilized as markers of cellular stress in the rabbit brain. Following a physiologically relevant increase in body temperature of 2.7 +/- .3 degrees C, nonneuronal cell types, such as ependymal cells and oligodendrocytes, undergo a stress response as assayed by the above criteria. In contrast, several neuronal cell populations required an increased degree of hyperthermic stress (3.4 +/- .2 degrees C) before exhibiting nuclear translocation of constitutive hsc70 protein. Induction of hsp70 protein was not observed in these neuronal cells at either temperature. The present results suggest that certain neurons in the rabbit brain are buffered against induction of the heat shock response, perhaps due to their high constitutive levels of hsc70 protein.

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Section: Discussionmentioning

confidence: 99%

The Neuronal Stress Response: Nuclear Translocation of Heat Shock Proteins as an Indicator of Hyperthermic Stress

Manzerra

Brown

1996

Experimental Cell Research

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“…In central nervous system, Hsp90 is widely expressed in all regions at the latest stages of gestation and postnatal development. In the adult mammalian nervous system and at all stages of postnatal development, the Hsp90 constitutively expressed is preferentially localized on neurons [12,13,[17][18][19]. Most studies regarding the role of Hsp90 in nervous system have focused on its involvement on neurodegenerative diseases [20], however its importance in neuron differentiation remains mostly unknown.…”

Section: Introductionmentioning

confidence: 99%

Hsp90 activity is necessary to acquire a proper neuronal polarization

Benítez

Sánchez-Ponce

Garrido

2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Chaperones are critical for the folding and regulation of a wide array of cellular proteins. Heat Shock Proteins (Hsps) are the most representative group of chaperones. Hsp90 represents up to 1-2% of soluble protein. Although the Hsp90 role is being studied in neurodegenerative diseases, its role in neuronal differentiation remains mostly unknown. Since neuronal polarity mechanisms depend on local stability and degradation, we asked whether Hsp90 could be a regulator of axonal polarity and growth. Thus, we studied the role of Hsp90 activity in a well established model of cultured hippocampal neurons using an Hsp90 specific inhibitor, 17-AAG. Our present data shows that Hsp90 inhibition at different developmental stages disturbs neuronal polarity formation or axonal elongation. Hsp90 inhibition during the first 3h in culture promotes multiple axon morphology, while this inhibition after 3h slows down axonal elongation. Hsp90 inhibition was accompanied by decreased Akt and GSK3 expression, as well as, a reduced Akt activity. In parallel, we detected an alteration of kinesin-1 subcellular distribution. Moreover, these effects were seconded by changes in Hsp70/Hsc70 subcellular localization that seem to compensate the lack of Hsp90 activity. In conclusion, our data strongly suggests that Hsp90 activity is necessary to control the expression, activity or location of specific kinases and motor proteins during the axon specification and axon elongation processes. Even more, our data demonstrate the existence of a "time-window" for axon specification in this model of cultured neurons after which the inhibition of Hsp90 only affects axonal elongation mechanisms.

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“…Indeed, a number of the heat shock proteins (HSPs) are affected by both anaesthetics and, given that HSP70, HSP84b and HSP 90 are known to have neuroprotective roles (7,23,25,26,35,36), this could pose significant risks to neurons during and after anaesthesia. Modulation of proteins like syntaxin B2 and dihydropyrimidinaselike proteins, which are involved in synaptic structure and function (1,2,18,21,22,39), could also have long-term effects on brain circuitry, so it is vital that we understand the outcomes of using particular anaesthetic agents.…”

Section: Discussionmentioning

confidence: 86%

Propofol anaesthesia alters the cerebral proteome differently from sevoflurane anaesthesia

Tsuboko

Sakamoto

2011

Biomed. Res.

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Previous studies suggest that propofol and sevoflurane anaesthesia in rats may have variable effects on the proteome. Brains from untreated rats and rats anaesthetised with intravenous propofol infusion or inhaled sevoflurane were collected at various time points post-anaesthesia and subjected to global protein expression profiling using two-dimensional gel electrophoresis. Significant changes in protein spot intensity (i.e. expression) between the propofol and sevoflurane groups demonstrated clear similarities and differences in proteomic regulation by these anaesthetics. The proteins regulated were broadly classified into groups involved in cytoskeletal/neuronal growth, cellular metabolism, signalling, and cell stress/death responses. Proteins concerned with cell death and stress responses were down-regulated by both agents, but the anaesthetics had variable effects on proteins in the other groups. Importantly, proteins such as Ulip2 and dihydropyrimidinaselike-2 were regulated in opposite directions by propofol and sevoflurane. Moreover, the timecourse of regulation of proteins varied depending on the agent used. These data suggest different underlying mechanisms of proteomic regulation. We found that sevoflurane anaesthesia had more pronounced effects, on a wider range of proteins, and over an apparently longer duration than propofol. Thus, sevoflurane could be considered a more disruptive anaesthetic agent. Our findings show that protein expression is regulated differentially according to the anaesthetic agent and the method of delivery support and extend our previous observations of differential genomic regulation by anaesthetics in the brain. This study highlights the power of proteomic studies in assessing the effects of certain anaesthetics on the integrity of neuronal structure and function.The utility of general anaesthetics is unquestioned, and their harmlessness with regard to mortality and morbidity has been evaluated and endorsed by clinical outcomes (3,(10)(11)(12)24). Little is known, however, regarding their comprehensive influence at the genomic or proteomic level, which is not reflected in mortality and morbidity. A number of genomic studies have been published, and we have shown that general anaesthesia alters gene expression, especially expression of genes involved in circadian rhythms and drug metabolism. For instance, we found persistent suppression of the expression of several genes implicated in circadian rhythms (e.g., Per2, Dbp, Egr1, Krox20 and NGF1-B) following treatment of rats with sevoflurane (20) and propofol or dexmedetomidine (41). We have also reported changes in the expression of drug metabolising enzymes in rats (e.g., Cyp2b15, Por, Nr1i2, Ces2, Ugt1a7, Abcb1a and Abcc2) in response to sevoflurane, isoflurane, propofol, or dexmedetomidine anaesthesia (30, 37) The observed changes varied depending on the identity of the anaesthetic used, and also on the mode of administration (inhaled vs. intravenous). Therefore, it is clear that anaesthetics have significant effects...

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Expression of mRNA species encoding heat shock protein 90 (hsp90) in control and hyperthermic rabbit brain

Cited by 18 publications

References 66 publications

The Neuronal Stress Response: Nuclear Translocation of Heat Shock Proteins as an Indicator of Hyperthermic Stress

The Neuronal Stress Response: Nuclear Translocation of Heat Shock Proteins as an Indicator of Hyperthermic Stress

Hsp90 activity is necessary to acquire a proper neuronal polarization

Propofol anaesthesia alters the cerebral proteome differently from sevoflurane anaesthesia

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