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Article ; Online: Diversity in the Oligodendrocyte Lineage: Current Evidence.

Trotter, Jacqueline / Mittmann, Thomas

2019 Volume 101, Issue 3, Page(s) 356–357

Abstract: In this issue of Neuron, Spitzer et al. (2019) demonstrate age- and region-dependent diversity in the expression of voltage-gated ion channels and neurotransmitter receptors in oligodendrocyte progenitors. These define their interactions with neurons and ...

Abstract	In this issue of Neuron, Spitzer et al. (2019) demonstrate age- and region-dependent diversity in the expression of voltage-gated ion channels and neurotransmitter receptors in oligodendrocyte progenitors. These define their interactions with neurons and thus suggest an increasing functional heterogeneity with age and between brain regions.
MeSH term(s)	Cell Lineage ; Neurons ; Oligodendrocyte Precursor Cells ; Oligodendroglia
Language	English
Publishing date	2019-02-07
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2019.01.032
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Zs.A 2496: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 92: Show issues

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Article ; Online: Missing in Action: Dysfunctional RNA Metabolism in Oligodendroglial Cells as a Contributor to Neurodegenerative Diseases?

Hoch-Kraft, Peter / Trotter, Jacqueline / Gonsior, Constantin

Neurochemical research

2019 Volume 45, Issue 3, Page(s) 566–579

Abstract: The formation of myelin around axons by oligodendrocytes (OL) poses an enormous synthetic and energy challenge for the glial cell. Local translation of transcripts, including the mRNA for the essential myelin protein Myelin Basic Protein (MBP) at the ... ...

Abstract	The formation of myelin around axons by oligodendrocytes (OL) poses an enormous synthetic and energy challenge for the glial cell. Local translation of transcripts, including the mRNA for the essential myelin protein Myelin Basic Protein (MBP) at the site of myelin deposition has been recognised as an efficient mechanism to assure proper myelin sheath assembly. Oligodendroglial precursor cells (OPCs) form synapses with neurons and may localise many additional mRNAs in a similar fashion to synapses between neurons. In some diseases in which demyelination occurs, an abundance of OPCs is present but there is a failure to efficiently remyelinate and to synthesise MBP. This compromises axonal survival and function. OPCs are especially sensitive to cellular stress as occurring in neurodegenerative diseases, which can impinge on their ability to translate mRNAs into protein. Stress causes the build up of cytoplasmic stress granules (SG) in which many RNAs are sequestered and translationally stalled until the stress ceases. Chronic stress in particular could convert this initially protective reaction of the cell into damage, as persistence of SG may lead to pathological aggregate formation or long-term translation block of SG-associated RNAs. The recent recognition that many neurodegenerative diseases often exhibit an early white matter pathology with a proliferation of surviving OPCs, renders a study of the stress-associated processes in oligodendrocytes and OPCs especially relevant. Here, we discuss a potential dysfunction of RNA regulation in myelin diseases such as Multiple Sclerosis (MS) and Vanishing white matter disease (VWM) and potential contributions of OL dysfunction to neurodegenerative diseases such as Amyotrophic lateral sclerosis (ALS), Alzheimer's disease (AD) and Fragile X syndrome (FXS).
MeSH term(s)	Animals ; Cell Differentiation ; Humans ; Neurodegenerative Diseases/etiology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neuroglia/metabolism ; Neuroglia/pathology ; Oligodendroglia/metabolism ; Oligodendroglia/pathology ; RNA/genetics
Chemical Substances	RNA (63231-63-0)
Language	English
Publishing date	2019-03-06
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	199335-5
ISSN	1573-6903 ; 0364-3190
ISSN (online)	1573-6903
ISSN	0364-3190
DOI	10.1007/s11064-019-02763-y
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Zs.A 1368: Show issues

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Article ; Online: The role of the NG2 proteoglycan in OPC and CNS network function.

Sakry, Dominik / Trotter, Jacqueline

Brain research

2016 Volume 1638, Issue Pt B, Page(s) 161–166

Abstract: In the normal mammalian CNS, the NG2 proteoglycan is expressed by oligodendrocyte precursor cells (OPC) but not by any other neural cell-type. NG2 is a type-1 membrane protein, exerting multiple roles in the CNS including intracellular signaling within ... ...

Abstract	In the normal mammalian CNS, the NG2 proteoglycan is expressed by oligodendrocyte precursor cells (OPC) but not by any other neural cell-type. NG2 is a type-1 membrane protein, exerting multiple roles in the CNS including intracellular signaling within the OPC, with effects on migration, cytoskeleton interaction and target gene regulation. It has been recently shown that the extracellular region of NG2, in addition to an adhesive function, acts as a soluble ECM component with the capacity to alter defined neuronal network properties. This region of NG2 is thus endowed with neuromodulatory properties. In order to generate biologically active fragments yielding these properties, the sequential cleavage of the NG2 protein by α- and γ-secretases occurs. The basal level of constitutive cleavage is stimulated by neuronal network activity. This processing leads to 4 major NG2 fragments which all have been associated with distinct biological functions. Here we summarize these functions, focusing on recent discoveries and their implications for the CNS. This article is part of a Special Issue entitled SI:NG2-glia(Invited only).
MeSH term(s)	Animals ; Antigens/metabolism ; Central Nervous System/metabolism ; Humans ; Oligodendroglia/metabolism ; Proteoglycans/metabolism ; Stem Cells/metabolism
Chemical Substances	Antigens ; Proteoglycans ; chondroitin sulfate proteoglycan 4
Language	English
Publishing date	2016-05-01
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	1200-2
ISSN	1872-6240 ; 0006-8993
ISSN (online)	1872-6240
ISSN	0006-8993
DOI	10.1016/j.brainres.2015.06.003
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Zs.A 161: Show issues

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Article: The Intracellular Cleavage Product of the NG2 Proteoglycan Modulates Translation and Cell-Cycle Kinetics via Effects on mTORC1/FMRP Signaling.

Nayak, Tanmoyita / Trotter, Jacqueline / Sakry, Dominik

Frontiers in cellular neuroscience

2018 Volume 12, Page(s) 231

Abstract: The NG2 proteoglycan is expressed by oligodendrocyte precursor cells (OPCs) and is abundantly expressed by tumors such as melanoma and glioblastoma. Functions of NG2 include an influence on proliferation, migration and neuromodulation. Similar to other ... ...

Abstract	The NG2 proteoglycan is expressed by oligodendrocyte precursor cells (OPCs) and is abundantly expressed by tumors such as melanoma and glioblastoma. Functions of NG2 include an influence on proliferation, migration and neuromodulation. Similar to other type-1 membrane proteins, NG2 undergoes proteolysis, generating a large ectodomain, a C-terminal fragment (CTF) and an intracellular domain (ICD) via sequential action of α- and γ-secretases which is enhanced by neuronal activity. Functional roles of NG2 have so far been shown for the full-length protein, the released ectodomain and CTF, but not for the ICD. In this study, we characterized the role of the NG2 ICD in OPC and Human Embryonic Kidney (HEK) cells. Overexpressed ICD is predominantly localized in the cell cytosol, including the distal processes of OPCs. Nuclear localisation of a fraction of the ICD is dependent on Nuclear Localisation Signals. Immunoprecipitation and Mass Spectrometry followed by functional analysis indicated that the NG2 ICD modulates mRNA translation and cell-cycle kinetics. In OPCs and HEK cells, ICD overexpression results in an mTORC1-dependent upregulation of translation, as well as a shift of the cell population toward S-phase. NG2 ICD increases the active (phosphorylated) form of mTOR and modulates downstream signaling cascades, including increased phosphorylation of p70S6K1 and increased expression of eEF2. Strikingly, levels of FMRP, an RNA-binding protein that is regulated by mTOR/p70S6K1/eEF2 were decreased. In neurons, FMRP acts as a translational repressor under activity-dependent control and is mutated in Fragile X Syndrome (FXS). Knock-down of endogenous NG2 in primary OPC reduced translation and mTOR/p70S6K1 phosphorylation in Oli-
Language	English
Publishing date	2018-08-07
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2018.00231
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Article ; Online: Health-Related Quality of Life and Depression Symptoms in a Cross Section of Patients with Advanced Lung Cancer before and during the COVID-19 Pandemic.

Petrillo, Laura A / El-Jawahri, Areej / Heuer, Lauren B / Post, Kathryn / Gallagher, Emily R / Trotter, Chardria / Elyze, Madeleine / Vyas, Charu / Plotke, Rachel / Turk, Yael R / Han, Jacqueline / Temel, Jennifer S / Greer, Joseph A

Journal of palliative medicine

2022 Volume 25, Issue 11, Page(s) 1639–1645

Abstract: Background: ...

Abstract	Background:
MeSH term(s)	Adult ; Humans ; Quality of Life ; COVID-19 ; Pandemics ; Depression ; Lung Neoplasms
Language	English
Publishing date	2022-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1427361-5
ISSN	1557-7740 ; 1096-6218
ISSN (online)	1557-7740
ISSN	1096-6218
DOI	10.1089/jpm.2022.0049
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Zs.A 5440: Show issues

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Article: NG2-positive cells in CNS function and the pathological role of antibodies against NG2 in demyelinating diseases.

Trotter, Jacqueline

Journal of the neurological sciences

2005 Volume 233, Issue 1-2, Page(s) 37–42

Abstract: NG2 is expressed by a variety of immature glia in the CNS including oligodendrocyte progenitor cells, paranodal astrocytes and perisynaptic glia. The protein has a large extracellular domain with two LNS/Lam G domains at the N-terminus and a short ... ...

Abstract	NG2 is expressed by a variety of immature glia in the CNS including oligodendrocyte progenitor cells, paranodal astrocytes and perisynaptic glia. The protein has a large extracellular domain with two LNS/Lam G domains at the N-terminus and a short intracellular tail with a PDZ-recognition domain at the C-terminus. Experiments suggest that the protein plays a role in migration. The PDZ protein GRIP was identified as an intracellular binding partner of NG2 in immature glial cells. A complex is formed between GRIP, NG2 and the AMPA class of glutamate receptors: this may position these glial receptors towards sites of neuronal glutamate release at synapses and during myelination. Identification of neuronal receptors and links to the cytoskeleton of NG2 is of critical importance. Some Multiple Sclerosis patients have autoantibodies to NG2 in the cerebral spinal fluid: such antibodies could interfere with remyelination by lysing oligodendrocyte progenitor cells or blocking their migration but may also cause pathology by disrupting glial-neuronal signalling at synapses and paranodes.
MeSH term(s)	Animals ; Antibodies/adverse effects ; Antigens/chemistry ; Antigens/immunology ; Antigens/physiology ; Central Nervous System/cytology ; Central Nervous System/metabolism ; Central Nervous System/physiology ; Demyelinating Diseases/etiology ; Demyelinating Diseases/immunology ; Humans ; Models, Biological ; Neuroglia/metabolism ; Proteoglycans/chemistry ; Proteoglycans/immunology ; Proteoglycans/physiology ; Synapses/metabolism
Chemical Substances	Antibodies ; Antigens ; Proteoglycans ; chondroitin sulfate proteoglycan 4
Language	English
Publishing date	2005-06-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80160-4
ISSN	1878-5883 ; 0022-510X ; 0374-8642
ISSN (online)	1878-5883
ISSN	0022-510X ; 0374-8642
DOI	10.1016/j.jns.2005.03.024
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Zs.A 308: Show issues

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Article ; Online: Recovery from Toxic-Induced Demyelination Does Not Require the NG2 Proteoglycan.

Albrecht, Stefanie / Hagemeier, Karin / Ehrlich, Marc / Kemming, Claudia / Trotter, Jacqueline / Kuhlmann, Tanja

PloS one

2016 Volume 11, Issue 10, Page(s) e0163841

Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0163841
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Article ; Online: Oligodendrocyte precursor cells synthesize neuromodulatory factors.

Sakry, Dominik / Yigit, Hatice / Dimou, Leda / Trotter, Jacqueline

PloS one

2015 Volume 10, Issue 5, Page(s) e0127222

Abstract: NG2 protein-expressing oligodendrocyte progenitor cells (OPC) are a persisting and major glial cell population in the adult mammalian brain. Direct synaptic innervation of OPC by neurons throughout the brain together with their ability to sense neuronal ... ...

Abstract	NG2 protein-expressing oligodendrocyte progenitor cells (OPC) are a persisting and major glial cell population in the adult mammalian brain. Direct synaptic innervation of OPC by neurons throughout the brain together with their ability to sense neuronal network activity raises the question of additional physiological roles of OPC, supplementary to generating myelinating oligodendrocytes. In this study we investigated whether OPC express neuromodulatory factors, typically synthesized by other CNS cell types. Our results show that OPC express two well-characterized neuromodulatory proteins: Prostaglandin D2 synthase (PTGDS) and neuronal Pentraxin 2 (Nptx2/Narp). Expression levels of the enzyme PTGDS are influenced in cultured OPC by the NG2 intracellular region which can be released by cleavage and localizes to glial nuclei upon transfection. Furthermore PTGDS mRNA levels are reduced in OPC from NG2-KO mouse brain compared to WT cells after isolation by cell sorting and direct analysis. These results show that OPC can contribute to the expression of these proteins within the CNS and suggest PTGDS expression as a downstream target of NG2 signaling.
MeSH term(s)	Adult Stem Cells/physiology ; Animals ; Antigens/genetics ; Antigens/metabolism ; C-Reactive Protein/metabolism ; Cell Differentiation ; Cell Line ; HEK293 Cells ; Humans ; Intramolecular Oxidoreductases/genetics ; Intramolecular Oxidoreductases/metabolism ; Lipocalins/genetics ; Lipocalins/metabolism ; Mice ; Mice, Knockout ; Nerve Tissue Proteins/metabolism ; Oligodendroglia/cytology ; Oligodendroglia/metabolism ; Proteoglycans/genetics ; Proteoglycans/metabolism
Chemical Substances	Antigens ; Lipocalins ; Nerve Tissue Proteins ; Proteoglycans ; chondroitin sulfate proteoglycan 4 ; neuronal pentraxin ; C-Reactive Protein (9007-41-4) ; Intramolecular Oxidoreductases (EC 5.3.-) ; prostaglandin R2 D-isomerase (EC 5.3.99.2)
Language	English
Publishing date	2015-05-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0127222
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Article ; Online: The NG2 Protein Is Not Required for Glutamatergic Neuron-NG2 Cell Synaptic Signaling.

Passlick, Stefan / Trotter, Jacqueline / Seifert, Gerald / Steinhäuser, Christian / Jabs, Ronald

Cerebral cortex (New York, N.Y. : 1991)

2016 Volume 26, Issue 1, Page(s) 51–57

Abstract: NG2 glial cells (as from now NG2 cells) are unique in receiving synaptic input from neurons. However, the components regulating formation and maintenance of these neuron-glia synapses remain elusive. The transmembrane protein NG2 has been considered a ... ...

Abstract	NG2 glial cells (as from now NG2 cells) are unique in receiving synaptic input from neurons. However, the components regulating formation and maintenance of these neuron-glia synapses remain elusive. The transmembrane protein NG2 has been considered a potential mediator of synapse formation and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) clustering, because it contains 2 extracellular Laminin G/Neurexin/Sex Hormone-Binding Globulin domains, which in neurons are crucial for formation of transsynaptic neuroligin-neurexin complexes. NG2 is connected via Glutamate Receptor-Interacting Protein with GluA2/3-containing AMPARs, thereby possibly mediating receptor clustering in glial postsynaptic density. To elucidate the role of NG2 in neuron-glia communication, we investigated glutamatergic synaptic transmission in juvenile and aged hippocampal NG2 cells of heterozygous and homozygous NG2 knockout mice. Neuron-NG2 cell synapses readily formed in the absence of NG2. Short-term plasticity, synaptic connectivity, postsynaptic AMPAR current kinetics, and density were not affected by NG2 deletion. During development, an NG2-independent acceleration of AMPAR current kinetics and decreased synaptic connectivity were observed. Our results indicate that the lack of NG2 does not interfere with genesis and basic properties of neuron-glia synapses. In addition, we demonstrate frequent expression of neuroligins 1-3 in juvenile and aged NG2 cells, suggesting a role of these molecules in synapse formation between NG2 glia and neurons.
MeSH term(s)	Animals ; Antigens/genetics ; Glutamic Acid/metabolism ; Hippocampus/cytology ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice, Transgenic ; Neuroglia/cytology ; Neurons/cytology ; Proteoglycans/genetics ; Receptors, AMPA/metabolism ; Synapses/metabolism ; Synaptic Transmission/genetics
Chemical Substances	Antigens ; Membrane Proteins ; Proteoglycans ; Receptors, AMPA ; chondroitin sulfate proteoglycan 4 ; Glutamic Acid (3KX376GY7L)
Language	English
Publishing date	2016-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1077450-6
ISSN	1460-2199 ; 1047-3211
ISSN (online)	1460-2199
ISSN	1047-3211
DOI	10.1093/cercor/bhu171
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Zs.A 3235: Show issues

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Article ; Online: Oligodendrocyte precursor cells synthesize neuromodulatory factors.

Dominik Sakry / Hatice Yigit / Leda Dimou / Jacqueline Trotter

PLoS ONE, Vol 10, Iss 5, p e

2015 Volume 0127222

Abstract	NG2 protein-expressing oligodendrocyte progenitor cells (OPC) are a persisting and major glial cell population in the adult mammalian brain. Direct synaptic innervation of OPC by neurons throughout the brain together with their ability to sense neuronal network activity raises the question of additional physiological roles of OPC, supplementary to generating myelinating oligodendrocytes. In this study we investigated whether OPC express neuromodulatory factors, typically synthesized by other CNS cell types. Our results show that OPC express two well-characterized neuromodulatory proteins: Prostaglandin D2 synthase (PTGDS) and neuronal Pentraxin 2 (Nptx2/Narp). Expression levels of the enzyme PTGDS are influenced in cultured OPC by the NG2 intracellular region which can be released by cleavage and localizes to glial nuclei upon transfection. Furthermore PTGDS mRNA levels are reduced in OPC from NG2-KO mouse brain compared to WT cells after isolation by cell sorting and direct analysis. These results show that OPC can contribute to the expression of these proteins within the CNS and suggest PTGDS expression as a downstream target of NG2 signaling.
Keywords	Medicine ; R ; Science ; Q
Subject code	612
Language	English
Publishing date	2015-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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