Expression of 300-kilodalton intermediate filament-associated protein distinguishes human glioma cells from normal astrocytes.

Yang, Hsiang-Yu; Lieska, N.; Glick, Roberta P.; Shao, Dongguo; Pappas, George D.

doi:10.1073/pnas.90.18.8534

Cited by 12 publications

(16 citation statements)

References 43 publications

(48 reference statements)

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“…16 Among brain tumors, glioblastoma is the most diffuse and the one with the poorest prognosis. 1 Up until now, only a few molecular markers, such as intermediatefilament-associated proteins, laminin-8, nestin, epidermal growth factor receptor, and tenascin, [30][31][32][33][34] have been used to differentiate glioma cells from adjacent parenchyma, but none of them is unique to glioma cells, making both therapeutic molecular targeting and immunohistochemical diagnosis problematic. Prompted by these considerations, we screened mouse and rat glioma cell lines for the presence and intracellular localization of the four PKA regulatory subunits, an issue apparently never addressed before.…”

Section: Discussionmentioning

confidence: 99%

Selective distribution of protein kinase A regulatory subunit RIIα in rodent gliomas

Mucignat‐Caretta

Cavaggioni²,

Redaelli³

et al. 2008

Neuro-Oncology

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Differential diagnosis of brain tumor types is mainly based on cell morphology and could benefit from additional markers. The cAMP second-messenger system is involved in regulating cell proliferation and differentiation and is conceivably modulated during cancer transformation. The cAMP second-messenger system mainly activates protein kinases, which are in part docked to cytoskeleton, membranes, or organelles by anchoring proteins, forming protein aggregates that are detergent insoluble and not freely diffusible and that are characteristic for each cell type. The intracellular distribution of the detergent-insoluble regulatory subunits (R) of the cAMP-dependent protein kinase has been examined in mouse and rat glioma cells both in vitro and in vivo by immunohistochemistry. In normal rodent brains, the RIIalpha regulatory subunit is detergent insoluble only in ependymal cells, while in the rest of the brain it is present in soluble form. Immunohistochemistry shows that in both mouse and rat glioma cell lines, RIIalpha is mainly detergent insoluble. RIIalpha is localized close to the nucleus, associated with smooth vesicles in the trans-Golgi network area. Both paclitaxel and vinblastine cause a redistribution of RIIalpha within the cell. Under conditions that increased intracellular cAMP, apoptosis of glioma cells was observed, and it was accompanied by RIIalpha redistribution. Also in vivo, detergent-insoluble RIIalpha can be observed in mouse and rat gliomas, where it delineates the border between normal brain tissue and glioma. Therefore, intracellular distribution of detergent-insoluble RIIalpha can assist in detecting tumor cells within the brain, thus making the histologic diagnosis of brain tumors more accurate, and may represent an additional target for therapy.

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Section: Discussionmentioning

confidence: 99%

Selective distribution of protein kinase A regulatory subunit RIIα in rodent gliomas

Mucignat‐Caretta

Cavaggioni²,

Redaelli³

et al. 2008

Neuro-Oncology

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“…During this time, they maintain their contact with the pial surface, but retract their basal attachment to the ventricular zone. As they translocate to their destination in the gray or white matter, they upregulate expression of GFAP as they lose their bipolar morphology and form additional processes (Malatesta et al, 2000; Voigt, 1989; Yang et al, 1993a, 1993b). In the spinal cord, after the initial wave of neurogenesis is complete (~E9–11), progenitors in the ventricular zone begin to differentiate into astrocytes (E12.5).…”

Section: Astrocyte Developmentmentioning

confidence: 99%

“Targeting astrocytes in CNS injury and disease: A translational research approach”

Filous

Silver

2016

Progress in Neurobiology

136

104

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Astrocytes are a major constituent of the central nervous system. These glia play a major role in regulating blood-brain barrier function, the formation and maintenance of synapses, glutamate uptake, and trophic support for surrounding neurons and glia. Therefore, maintaining the proper functioning of these cells is crucial to survival. Astrocyte defects are associated with a wide variety of neuropathological insults, ranging from neurodegenerative diseases to gliomas. Additionally, injury to the CNS causes drastic changes to astrocytes, often leading to a phenomenon known as reactive astrogliosis. This process is important for protecting the surrounding healthy tissue from the spread of injury, while it also inhibits axonal regeneration and plasticity. Here, we discuss the important roles of astrocytes after injury and in disease, as well as potential therapeutic approaches to restore proper astrocyte functioning.

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“…Interestingly, trapping CFTR in the ER with Brefeldin A results in accumulation of a stable, “mature” Band B form that is able to exit the ER upon Brefeldin A washout, indicating that the key folding step is distinct from Golgi processing. This folding transition also involves reorganization and/or release of cytosolic chaperones (Yang et al, 1993; Meacham et al, 1999) and results in a substantial change in CFTR structure as demonstrated by limited proteolysis (Zhang et al, 1998). Importantly, the ΔF508 mutation prevents this latter step.…”

Section: Cftr Foldingmentioning

confidence: 99%

Mechanisms of CFTR Folding at the Endoplasmic Reticulum

Kim

Skach

2012

Front. Pharmacol.

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In the past decade much has been learned about how Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) folds and misfolds as the etiologic cause of cystic fibrosis (CF). CFTR folding is complex and hierarchical, takes place in multiple cellular compartments and physical environments, and involves several large networks of folding machineries. Insertion of transmembrane (TM) segments into the endoplasmic reticulum (ER) membrane and tertiary folding of cytosolic domains begin cotranslationally as the nascent polypeptide emerges from the ribosome, whereas posttranslational folding establishes critical domain–domain contacts needed to form a physiologically stable structure. Within the membrane, N- and C-terminal TM helices are sorted into bundles that project from the cytosol to form docking sites for nucleotide binding domains, NBD1 and NBD2, which in turn form a sandwich dimer for ATP binding. While tertiary folding is required for domain assembly, proper domain assembly also reciprocally affects folding of individual domains analogous to a jig-saw puzzle wherein the structure of each interlocking piece influences its neighbors. Superimposed on this process is an elaborate proteostatic network of cellular chaperones and folding machineries that facilitate the timing and coordination of specific folding steps in and across the ER membrane. While the details of this process require further refinement, we finally have a useful framework to understand key folding defect(s) caused by ΔF508 that provides a molecular target(s) for the next generation of CFTR small molecule correctors aimed at the specific defect present in the majority of CF patients.

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Expression of 300-kilodalton intermediate filament-associated protein distinguishes human glioma cells from normal astrocytes.

Abstract: The

Cited by 12 publications

References 43 publications

Selective distribution of protein kinase A regulatory subunit RIIα in rodent gliomas

Selective distribution of protein kinase A regulatory subunit RIIα in rodent gliomas

“Targeting astrocytes in CNS injury and disease: A translational research approach”

Mechanisms of CFTR Folding at the Endoplasmic Reticulum

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