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Allocortex

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Allocortex – Free Register to Access Experts & Abstracts

Rehana K. Leak – One of the best experts on this subject based on the ideXlab platform.

  • Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    , 2016
    Co-Authors: Jessica M. Posimo, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    In Parkinson’s and Alzheimer’s diseases, the Allocortex accumulates aggregated proteins such as synuclein and tau well before neocortex. We present a new high-throughput model of this topographic difference by microdissecting neocortex and Allocortex from the postnatal rat and treating them in parallel fashion with toxins. Allocortical cultures were more vulnerable to low concentrations of the proteasome inhiinhibitors MG132 and PSI but not the oxidative poison H2O2. The proteasome appeared to be more impaired in Allocortex because MG132 raised ubiquitin-conjugated proteins and lowered proteasome activity in Allocortex more than neocortex. Allocortex cultures were more vulnerable to MG132 despite greater MG132-induced rises in heat shock protein 70, heme oxygenase 1, and catalase. Proteasome subunits PA700 and PA28 were also higher in Allocortex cultures, suggesting compensatory adaptations to greater proteasome impairment. Glutathione and ceruloplasmin were not robustly MG132-responsive and were basally higher in neocortical cultures. Notably, neocortex cultures became as vulnerable to MG132 as Allocortex when glutathione synthesis or autophagic defenses were inhibited. Conversely, the glutathione precursor N-acetyl cysteine rendered Allocortex resilient to MG132. Glutathione and ceruloplasmin levels were then examined in vivo as a function of age because aging is a natural model of proteasome inhibition and oxidative stress. Allocortical glutathione levels rose linearly with age but were similar to neocortex in whole tissue lysates. In contrast, ceruloplasmin levels were strikingly higher in neocortex at all ages and rose linearly until middl

  • Heat shock protein defenses in the neocortex and Allocortex of the telencephalon
    Neurobiology of aging, 2015
    Co-Authors: Jessica M. Posimo, Justin N. Weilnau, Amanda M. Gleixner, Matthew T. Broeren, Nicole L. Weiland, Jeffrey L. Brodsky, Peter Wipf, Rehana K. Leak
    Abstract:

    The telencephalic Allocortex develops protein inclusions before the neocortex in many age-related proteinopathies. One major defense mechanism against proteinopathic stress is the heat shock protein (Hsp) network. We therefore contrasted Hsp defenses in stressed primary neocortical and allocortical cells. Neocortical neurons were more resistant to the proteasome inhibitor MG132 than neurons from 3 allocortical subregions: entorhinal cortex, piriform cortex, and hippocampus. However, allocortical neurons exhibited higher MG132-induced increases in Hsp70 and heat shock cognate 70 (Hsc70). MG132-treated allocortical neurons also exhibited greater levels of protein ubiquitination. Inhibition of Hsp70/Hsc70 activity synergistically exacerbated MG132 toxicity in allocortical neurons more than neocortical neurons, suggesting that the Allocortex is more reliant on these Hsp defenses. In contrast, astrocytes harvested from the neocortex or Allocortex did not differ in their response to Hsp70/Hsc70 inhibition. Consistent with the idea that chaperones are maximally engaged in allocortical neurons, an increase in Hsp70/Hsc70 activity was protective only in neocortical neurons. Finally, the levels of select Hsps were altered in the neocortex and Allocortex in vivo with aging.

  • Correction: Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    PLoS ONE, 2013
    Co-Authors: Jessica M. Posimo, Amanda M. Titler, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    There were multiple errors in the Author Contributions statement. The Author Contributions statement should read: “Conceived and designed the experiments: RKL. Performed the experiments: JMP AMT. Analyzed the data: JMP AMT HJHC ASU. Wrote the paper: RKL.”

Jessica M. Posimo – One of the best experts on this subject based on the ideXlab platform.

  • Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    , 2016
    Co-Authors: Jessica M. Posimo, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    In Parkinson’s and Alzheimer’s diseases, the Allocortex accumulates aggregated proteins such as synuclein and tau well before neocortex. We present a new high-throughput model of this topographic difference by microdissecting neocortex and Allocortex from the postnatal rat and treating them in parallel fashion with toxins. Allocortical cultures were more vulnerable to low concentrations of the proteasome inhibitors MG132 and PSI but not the oxidative poison H2O2. The proteasome appeared to be more impaired in Allocortex because MG132 raised ubiquitin-conjugated proteins and lowered proteasome activity in Allocortex more than neocortex. Allocortex cultures were more vulnerable to MG132 despite greater MG132-induced rises in heat shock protein 70, heme oxygenase 1, and catalase. Proteasome subunits PA700 and PA28 were also higher in Allocortex cultures, suggesting compensatory adaptations to greater proteasome impairment. Glutathione and ceruloplasmin were not robustly MG132-responsive and were basally higher in neocortical cultures. Notably, neocortex cultures became as vulnerable to MG132 as Allocortex when glutathione synthesis or autophagic defenses were inhibited. Conversely, the glutathione precursor N-acetyl cysteine rendered Allocortex resilient to MG132. Glutathione and ceruloplasmin levels were then examined in vivo as a function of age because aging is a natural model of proteasome inhibition and oxidative stress. Allocortical glutathione levels rose linearly with age but were similar to neocortex in whole tissue lysates. In contrast, ceruloplasmin levels were strikingly higher in neocortex at all ages and rose linearly until middl

  • Heat shock protein defenses in the neocortex and Allocortex of the telencephalon
    Neurobiology of aging, 2015
    Co-Authors: Jessica M. Posimo, Justin N. Weilnau, Amanda M. Gleixner, Matthew T. Broeren, Nicole L. Weiland, Jeffrey L. Brodsky, Peter Wipf, Rehana K. Leak
    Abstract:

    The telencephalic Allocortex develops protein inclusions before the neocortex in many age-related proteinopathies. One major defense mechanism against proteinopathic stress is the heat shock protein (Hsp) network. We therefore contrasted Hsp defenses in stressed primary neocortical and allocortical cells. Neocortical neurons were more resistant to the proteasome inhibitor MG132 than neurons from 3 allocortical subregions: entorhinal cortex, piriform cortex, and hippocampus. However, allocortical neurons exhibited higher MG132-induced increases in Hsp70 and heat shock cognate 70 (Hsc70). MG132-treated allocortical neurons also exhibited greater levels of protein ubiquitination. Inhibition of Hsp70/Hsc70 activity synergistically exacerbated MG132 toxicity in allocortical neurons more than neocortical neurons, suggesting that the Allocortex is more reliant on these Hsp defenses. In contrast, astrocytes harvested from the neocortex or Allocortex did not differ in their response to Hsp70/Hsc70 inhibition. Consistent with the idea that chaperones are maximally engaged in allocortical neurons, an increase in Hsp70/Hsc70 activity was protective only in neocortical neurons. Finally, the levels of select Hsps were altered in the neocortex and Allocortex in vivo with aging.

  • Correction: Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    PLoS ONE, 2013
    Co-Authors: Jessica M. Posimo, Amanda M. Titler, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    There were multiple errors in the Author Contributions statement. The Author Contributions statement should read: “Conceived and designed the experiments: RKL. Performed the experiments: JMP AMT. Analyzed the data: JMP AMT HJHC ASU. Wrote the paper: RKL.”

Roger L. Reep – One of the best experts on this subject based on the ideXlab platform.

  • Manatee cerebral cortex: cytoarchitecture of the caudal region in Trichechus manatus latirostris.
    Brain behavior and evolution, 1995
    Co-Authors: C D Marshall, Roger L. Reep
    Abstract:

    In several brains of the Florida manatee, Trichechus manatus latirostris, the architecture of caudal regions of cerebral cortex was examined in order to complete a map of cortical areas in the brain of this unique herbivore. Through observation of sections stained for Nissl substance, myelinated axons, acetylcholinesterase and cytochrome oxidase, we have identified 11 new cortical areas based on qualitative cytoarchitectural appearance and measurements of laminar thicknesses, for a total of 24 such cortical areas in manatee cerebral cortex. Some areas exhibit poorly differentiated laminae while in others there are 6 clearly demarcated layers, often with sublaminar organization. Some previously identified areas were found to extend into the region caudal to the vertically oriented lateral fissure. As in other mammalian brains, cortical areas in manatees are organized in concentric rings of Allocortex, mesocortex, and isocortex. Putative functional roles have been assigned to most of the identified areas based on location, architecture, behavioral and anatomical considerations, and extrapolation from other taxa in which functional mapping has been done.

Ajay S. Unnithan – One of the best experts on this subject based on the ideXlab platform.

  • Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    , 2016
    Co-Authors: Jessica M. Posimo, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    In Parkinson’s and Alzheimer’s diseases, the Allocortex accumulates aggregated proteins such as synuclein and tau well before neocortex. We present a new high-throughput model of this topographic difference by microdissecting neocortex and Allocortex from the postnatal rat and treating them in parallel fashion with toxins. Allocortical cultures were more vulnerable to low concentrations of the proteasome inhibitors MG132 and PSI but not the oxidative poison H2O2. The proteasome appeared to be more impaired in Allocortex because MG132 raised ubiquitin-conjugated proteins and lowered proteasome activity in Allocortex more than neocortex. Allocortex cultures were more vulnerable to MG132 despite greater MG132-induced rises in heat shock protein 70, heme oxygenase 1, and catalase. Proteasome subunits PA700 and PA28 were also higher in Allocortex cultures, suggesting compensatory adaptations to greater proteasome impairment. Glutathione and ceruloplasmin were not robustly MG132-responsive and were basally higher in neocortical cultures. Notably, neocortex cultures became as vulnerable to MG132 as Allocortex when glutathione synthesis or autophagic defenses were inhibited. Conversely, the glutathione precursor N-acetyl cysteine rendered Allocortex resilient to MG132. Glutathione and ceruloplasmin levels were then examined in vivo as a function of age because aging is a natural model of proteasome inhibition and oxidative stress. Allocortical glutathione levels rose linearly with age but were similar to neocortex in whole tissue lysates. In contrast, ceruloplasmin levels were strikingly higher in neocortex at all ages and rose linearly until middl

  • Correction: Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    PLoS ONE, 2013
    Co-Authors: Jessica M. Posimo, Amanda M. Titler, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    There were multiple errors in the Author Contributions statement. The Author Contributions statement should read: “Conceived and designed the experiments: RKL. Performed the experiments: JMP AMT. Analyzed the data: JMP AMT HJHC ASU. Wrote the paper: RKL.”

  • Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    PloS one, 2013
    Co-Authors: Jessica M. Posimo, Amanda M. Titler, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    In Parkinson’s and Alzheimer’s diseases, the Allocortex accumulates aggregated proteins such as synuclein and tau well before neocortex. We present a new high-throughput model of this topographic difference by microdissecting neocortex and Allocortex from the postnatal rat and treating them in parallel fashion with toxins. Allocortical cultures were more vulnerable to low concentrations of the proteasome inhiinhibitors MG132 and PSI but not the oxidative poison H2O2. The proteasome appeared to be more impaired in Allocortex because MG132 raised ubiquitin-conjugated proteins and lowered proteasome activity in Allocortex more than neocortex. Allocortex cultures were more vulnerable to MG132 despite greater MG132-induced rises in heat shock protein 70, heme oxygenase 1, and catalase. Proteasome subunits PA700 and PA28 were also higher in Allocortex cultures, suggesting compensatory adaptations to greater proteasome impairment. Glutathione and ceruloplasmin were not robustly MG132-responsive and were basally higher in neocortical cultures. Notably, neocortex cultures became as vulnerable to MG132 as Allocortex when glutathione synthesis or autophagic defenses were inhibited. Conversely, the glutathione precursor N-acetyl cysteine rendered Allocortex resilient to MG132. Glutathione and ceruloplasmin levels were then examined in vivo as a function of age because aging is a natural model of proteasome inhibition and oxidative stress. Allocortical glutathione levels rose linearly with age but were similar to neocortex in whole tissue lysates. In contrast, ceruloplasmin levels were strikingly higher in neocortex at all ages and rose linearly until middle age. PA28 levels rose with age and were higher in Allocortex in vivo, also paralleling in vitro data. These neo- and allocortical differences have implications for the many studies that treat the telencephalic mantle as a single unit. Our observations suggest that the topographic progression of protein aggregations through the cerebrum may reflect differential responses to low level protein-misfolding stress but also reveal impressive compensatory adaptations in Allocortex.

Hailey J. H. Choi – One of the best experts on this subject based on the ideXlab platform.

  • Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    , 2016
    Co-Authors: Jessica M. Posimo, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    In Parkinson’s and Alzheimer’s diseases, the Allocortex accumulates aggregated proteins such as synuclein and tau well before neocortex. We present a new high-throughput model of this topographic difference by microdissecting neocortex and Allocortex from the postnatal rat and treating them in parallel fashion with toxins. Allocortical cultures were more vulnerable to low concentrations of the proteasome inhibitors MG132 and PSI but not the oxidative poison H2O2. The proteasome appeared to be more impaired in Allocortex because MG132 raised ubiquitin-conjugated proteins and lowered proteasome activity in Allocortex more than neocortex. Allocortex cultures were more vulnerable to MG132 despite greater MG132-induced rises in heat shock protein 70, heme oxygenase 1, and catalase. Proteasome subunits PA700 and PA28 were also higher in Allocortex cultures, suggesting compensatory adaptations to greater proteasome impairment. Glutathione and ceruloplasmin were not robustly MG132-responsive and were basally higher in neocortical cultures. Notably, neocortex cultures became as vulnerable to MG132 as Allocortex when glutathione synthesis or autophagic defenses were inhibited. Conversely, the glutathione precursor N-acetyl cysteine rendered Allocortex resilient to MG132. Glutathione and ceruloplasmin levels were then examined in vivo as a function of age because aging is a natural model of proteasome inhibition and oxidative stress. Allocortical glutathione levels rose linearly with age but were similar to neocortex in whole tissue lysates. In contrast, ceruloplasmin levels were strikingly higher in neocortex at all ages and rose linearly until middl

  • Correction: Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    PLoS ONE, 2013
    Co-Authors: Jessica M. Posimo, Amanda M. Titler, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    There were multiple errors in the Author Contributions statement. The Author Contributions statement should read: “Conceived and designed the experiments: RKL. Performed the experiments: JMP AMT. Analyzed the data: JMP AMT HJHC ASU. Wrote the paper: RKL.”

  • Neocortex and Allocortex Respond Differentially to Cellular Stress In Vitro and Aging In Vivo
    PloS one, 2013
    Co-Authors: Jessica M. Posimo, Amanda M. Titler, Hailey J. H. Choi, Ajay S. Unnithan, Rehana K. Leak
    Abstract:

    In Parkinson’s and Alzheimer’s diseases, the Allocortex accumulates aggregated proteins such as synuclein and tau well before neocortex. We present a new high-throughput model of this topographic difference by microdissecting neocortex and Allocortex from the postnatal rat and treating them in parallel fashion with toxins. Allocortical cultures were more vulnerable to low concentrations of the proteasome inhibitors MG132 and PSI but not the oxidative poison H2O2. The proteasome appeared to be more impaired in Allocortex because MG132 raised ubiquitin-conjugated proteins and lowered proteasome activity in Allocortex more than neocortex. Allocortex cultures were more vulnerable to MG132 despite greater MG132-induced rises in heat shock protein 70, heme oxygenase 1, and catalase. Proteasome subunits PA700 and PA28 were also higher in Allocortex cultures, suggesting compensatory adaptations to greater proteasome impairment. Glutathione and ceruloplasmin were not robustly MG132-responsive and were basally higher in neocortical cultures. Notably, neocortex cultures became as vulnerable to MG132 as Allocortex when glutathione synthesis or autophagic defenses were inhibited. Conversely, the glutathione precursor N-acetyl cysteine rendered Allocortex resilient to MG132. Glutathione and ceruloplasmin levels were then examined in vivo as a function of age because aging is a natural model of proteasome inhibition and oxidative stress. Allocortical glutathione levels rose linearly with age but were similar to neocortex in whole tissue lysates. In contrast, ceruloplasmin levels were strikingly higher in neocortex at all ages and rose linearly until middle age. PA28 levels rose with age and were higher in Allocortex in vivo, also paralleling in vitro data. These neo- and allocortical differences have implications for the many studies that treat the telencephalic mantle as a single unit. Our observations suggest that the topographic progression of protein aggregations through the cerebrum may reflect differential responses to low level protein-misfolding stress but also reveal impressive compensatory adaptations in Allocortex.