Calcium signaling mechanisms disrupt the cytoskeleton of primary astrocytes and neurons exposed to diphenylditelluride

Heimfarth, Luana; Ferreira, Fernanda da Silva; Pierozan, Paula; Loureiro, Samanta Oliveira; Mingori, Moara Rodrigues; Moreira, José Cláudio Fonseca; Rocha, João Batista Teixeira da; Pessoa-Pureur, Regina

doi:10.1016/j.bbagen.2016.07.023

Cited by 12 publications

(12 citation statements)

References 53 publications

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“…K + -evoked increase in GFAP fiber formation has been identified in the supraoptic nucleus by simulating the increase in extracellular K + levels that occurs following synchronized burst-like discharges of oxytocin neurons during lactation (Wang & Hatton, 2009). By contrast, increased cytosolic Ca 2+ level following glutamate activation of NMDARs elicits GFAP fiber depolymerization (Heimfarth et al, 2016).…”

Section: Neuronal Activitymentioning

confidence: 99%

“…At cellular level, activation of N ‐methyl‐ d ‐aspartic acid receptor (NMDA) receptors (NMDARs), L‐type voltage‐dependent Ca 2+ channels or metabotropic glutamate receptors upregulates Ca 2+ influx and increases cytosolic Ca 2+ level, which further activates PKA and PKC that cause hyperphosphorylation of GFAP in astrocytes. The hyperphosphorylation disrupts GFAP cytoskeleton along with RhoA‐activated stress fiber formation, leading to altered cell morphology (Heimfarth et al, ).…”

Section: Expression Of Gfap and Its Regulationmentioning

confidence: 99%

“…K + ‐evoked increase in GFAP fiber formation has been identified in the supraoptic nucleus by simulating the increase in extracellular K + levels that occurs following synchronized burst‐like discharges of oxytocin neurons during lactation (Wang & Hatton, ). By contrast, increased cytosolic Ca 2+ level following glutamate activation of NMDARs elicits GFAP fiber depolymerization (Heimfarth et al, ). Moreover, changes in extracellular ion levels can change intracellular osmolality, ion concentration, volume, and transporter activity (Jiao, Cui, Wang, Li, & Wang, ), which also influence the polymerization status of GFAP as previously reviewed (Wang & Parpura, ).…”

Section: Expression Of Gfap and Its Regulationmentioning

confidence: 99%

“…Moreover, compartment‐specific activations of protein kinase play key roles in the quick plastic change in GFAP fibers. That is, changes in Ca 2+ influx (Heimfarth et al, ), the activity of pERK1/2 (Wang & Hatton, ), and PKA (Wang et al, ) at different cellular compartments can determine membrane protein recycling via altering GFAP plasticity. This regulatory process of GFAP plasticity coupling with cytosolic transport machinery and membrane recycling processes forms the basis of a reassembling‐transport coupling model (Figure A).…”

Section: Mechanisms Underlying Gfap Guiding Rolementioning

confidence: 99%

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Neurochemical regulation of the expression and function of glial fibrillary acidic protein in astrocytes

Liu

et al. 2019

Glia

116

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Glial fibrillary acidic protein (GFAP), a type III intermediate filament, is a marker of mature astrocytes. The expression of GFAP gene is regulated by many transcription factors (TFs), mainly Janus kinase‐2/signal transducer and activator of transcription 3 cascade and nuclear factor κ‐light‐chain‐enhancer of activated B cell signaling. GFAP expression is also modulated by protein kinase and other signaling molecules that are elicited by neuronal activity and hormones. Abnormal expression of GFAP proteins occurs in neuroinflammation, neurodegeneration, brain edema‐eliciting diseases, traumatic brain injury, psychiatric disorders and others. GFAP, mainly in α‐isoform, is the major component of cytoskeleton and the scaffold of astrocytes, which is essential for the maintenance of astrocytic structure and shape. GFAP also has highly morphological plasticity because of its quick changes in assembling and polymerizing states in response to environmental challenges. This plasticity and its corresponding cellular morphological changes endow astrocytes the functions of physical barrier between adjacent neurons and stabilizer of extracellular environment. Moreover, GFAP colocalizes and even molecularly associates with many functional molecules. This feature allows GFAP to function as a platform for direct interactions between different molecules. Last, GFAP involves transportation and localization of other functional proteins and thus serves as a protein transport guide in astrocytes. This guiding role of GFAP involves an elastic retraction and extension cytoskeletal network that couples with GFAP reassembling, transporting, and membrane protein recycling machinery. This paper reviews our current understanding of the expression and functions of GFAP as well as their regulation.

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Section: Neuronal Activitymentioning

confidence: 99%

Section: Expression Of Gfap and Its Regulationmentioning

confidence: 99%

Section: Expression Of Gfap and Its Regulationmentioning

confidence: 99%

Section: Mechanisms Underlying Gfap Guiding Rolementioning

confidence: 99%

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Neurochemical regulation of the expression and function of glial fibrillary acidic protein in astrocytes

Liu

et al. 2019

Glia

116

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“…In cells, the role of divalent cations on vimentin structure and function can be highly complex. Besides a direct interaction with the protein, divalent cations could act on vimentin dynamics through multiple mechanisms, including regulation of proteases or kinases in the case of calcium [27][28][29], binding to ATP for kinase reactions or facilitating GTP binding to GTPases in the case of magnesium.…”

Section: Introductionmentioning

confidence: 99%

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Mónico

Zorrilla

Rivas

2020

IJMS

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The intermediate filament protein vimentin constitutes a critical sensor for electrophilic and oxidative stress. We previously showed that vimentin interacts with zinc, which affects its assembly and redox sensing. Here, we used vimentin wt and C328S, an oxidation-resistant mutant showing improved NaCl-induced polymerization, to assess the impact of zinc on soluble and polymerized vimentin by light scattering and electron microscopy. Zinc acts as a switch, reversibly inducing the formation of vimentin oligomeric species. High zinc concentrations elicit optically-detectable vimentin structures with a characteristic morphology depending on the support. These effects also occur in vimentin C328S, but are not mimicked by magnesium. Treatment of vimentin with micromolar ZnCl2 induces fibril-like particles that do not assemble into filaments, but form aggregates upon subsequent addition of NaCl. In contrast, when added to NaCl-polymerized vimentin, zinc increases the diameter or induces lateral association of vimentin wt filaments. Remarkably, these effects are absent or attenuated in vimentin C328S filaments. Therefore, the zinc-vimentin interaction depends on the chemical environment and on the assembly state of the protein, leading to atypical polymerization of soluble vimentin, likely through electrostatic interactions, or to broadening and lateral association of preformed filaments through mechanisms requiring the cysteine residue. Thus, the impact of zinc on vimentin assembly and redox regulation is envisaged.

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Astroglial Regulation of Magnocellular Neuroendocrine Cell Activities in the Supraoptic Nucleus

2020

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Calcium signaling mechanisms disrupt the cytoskeleton of primary astrocytes and neurons exposed to diphenylditelluride

Cited by 12 publications

References 53 publications

Neurochemical regulation of the expression and function of glial fibrillary acidic protein in astrocytes

Neurochemical regulation of the expression and function of glial fibrillary acidic protein in astrocytes

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Astroglial Regulation of Magnocellular Neuroendocrine Cell Activities in the Supraoptic Nucleus

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