Cell differentiation in vitro and the expression of Oct‐2 protein and <i>oct</i>‐2 RNA

Pankratova, E. V.; Sytina, E. V.; Степченко, А. Г.

doi:10.1016/0014-5793(94)80120-7

Cited by 5 publications

(5 citation statements)

References 18 publications

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“…The Neuro2A cell is an established cell model for the examination of molecular events that regulate neuronal differentiation (Pankratova et al 1994 ; Riboni et al 1995 ; Carter et al 2003 ; Kouchi et al 2011 ), and upon stimulation with retinoic acid, they change from a stem cell-like morphology to a neuronal one, including formation and extension of neurites. An essential role for PLCη2 in neurite growth was previously demonstrated in Neuro2A cells (Popovics et al 2014 ), which was further investigated in this study.…”

Section: Discussionmentioning

confidence: 99%

Phospholipase C-η2 interacts with nuclear and cytoplasmic LIMK-1 during retinoic acid-stimulated neurite growth

Arastoo

Hacker

Popovics

et al. 2015

Histochem Cell Biol

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Neurite growth is central to the formation and differentiation of functional neurons, and recently, an essential role for phospholipase C-η2 (PLCη2) in neuritogenesis was revealed. Here we investigate the function of PLCη2 in neuritogenesis using Neuro2A cells, which upon stimulation with retinoic acid differentiate and form neurites. We first investigated the role of the PLCη2 calcium-binding EF-hand domain, a domain that is known to be required for PLCη2 activation. To do this, we quantified neurite outgrowth in Neuro2A cells, stably overexpressing wild-type PLCη2 and D256A (EF-hand) and H460Q (active site) PLCη2 mutants. Retinoic acid-induced neuritogenesis was highly dependent on PLCη2 activity, with the H460Q mutant exhibiting a strong dominant-negative effect. Expression of the D256A mutant had little effect on neurite growth relative to the control, suggesting that calcium-directed activation of PLCη2 is not essential to this process. We next investigated which cellular compartments contain endogenous PLCη2 by comparing immunoelectron microscopy signals over control and knockdown cell lines. When signals were analyzed to reveal specific labeling for PLCη2, it was found to be localized predominantly over the nucleus and cytosol. Furthermore in these compartments (and also in growing neurites), a proximity ligand assay revealed that PLCη2 specifically interacts with LIMK-1 in Neuro2A cells. Taken together, these data emphasize the importance of the PLCη2 EF-hand domain and articulation of PLCη2 with LIMK-1 in regulating neuritogenesis.

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Section: Discussionmentioning

confidence: 99%

Phospholipase C-η2 interacts with nuclear and cytoplasmic LIMK-1 during retinoic acid-stimulated neurite growth

Arastoo

Hacker

Popovics

et al. 2015

Histochem Cell Biol

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“…In order to compare the sub-cellular localisations of human CaBP isoforms we determined the distributions of each of the proteins following transfection of colour tagged constructs into retinoic acid differentiated neuro2A (N2A) cells [22]. As the CaBPs exhibit greatest expression levels in neuronal tissues we reasoned that these cells would provide a more accurate reflection of correct sub-cellular localisation.…”

Section: Resultsmentioning

confidence: 99%

Membrane targeting of the EF-hand containing calcium-sensing proteins CaBP7 and CaBP8

McCue

Burgoyne

Haynes

2009

Biochemical and Biophysical Research Communications

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The CaBP family of EF-hand containing small Ca2+-binding proteins have recently emerged as important regulators of multiple targets essential to normal neuronal function in the mammalian central nervous system. Of particular interest are CaBP7 and CaBP8, abundantly expressed brain proteins that exhibit the greatest sequence divergence from other family members. In this study, we have analysed their sub-cellular localisations in a model neuronal (Neuro2A) cell line and show that both proteins exhibit a membrane distribution distinct from the other CaBPs and consistent with localisation to the trans-Golgi network (TGN). Furthermore, we show that their localisation to the TGN critically depends upon an unusual predicted C-terminal transmembrane domain that if deleted or disrupted has dramatic consequences for protein targeting. CaBP7 and 8, therefore, possess a targeting mechanism that is unique amongst the CaBPs that may contribute to differential functional Ca2+-sensing by these family members.

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“…Unlike to neural progenitor cells, Neuro2a cannot differentiate into glial cells. In addition, Native Neuro2a cells express Wnt‐1 or other neurogenic transcription factors but do not express Oct‐3 or functional Oct family proteins (Pankratova et al. 1994).…”

Section: Discussionmentioning

confidence: 99%

“…Unlike to neural progenitor cells, Neuro2a cannot differentiate into glial cells. In addition, Native Neuro2a cells express Wnt-1 or other neurogenic transcription factors but do not express Oct-3 or functional Oct family proteins (Pankratova et al 1994). In contrast, P19EC cells are pluripotent cells that can differentiate into neuronal or non-neuronal cells depending on the type of stimulation.…”

Section: Similarities and Differences Between C38 And Bm88mentioning

confidence: 99%

C38, equivalent to BM88, is developmentally expressed in maturing retinal neurons and enhances neuronal maturation

Wakabayashi

Kosaka

Mochii

et al. 2010

Journal of Neurochemistry

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C38 antigen is specifically expressed in neuronal cells of the retina. The purpose of this study was to isolate C38 cDNA and determine its molecular functions. Sequence analysis of C38 cDNA revealed that C38 is equivalent to rat BM88, which has been reported to induce cell-cycle arrest and neuronal differentiation in Neuro2a cells. C38 and Ki67, a marker of proliferating cells, were not colocalized during retinal development. C38 was first detected in the retinal ganglion cells at embryonic day 16, much later than the expression of doublecortin, a marker of immature neurons. Although all the horizontal cells were post-mitotic at this stage, C38 was not detected in horizontal cells until the postnatal period. In addition, C38 overexpression did not induce neuronal differentiation or cell-cycle arrest of pluripotent P19 embryonal carcinoma cells. Instead, C38 promoted maturation during neuronal differentiation of P19 embryonal carcinoma cells by down-regulating Oct-3, a pluripotent cell marker and enhancing the expressions of positive regulators of neurogenesis. In conclusion, during retinal development, C38 is first expressed in post-mitotic retinal neurons and is up-regulated during their maturation. C38 does not induce neuronal competence in pluripotent cells, but does promote maturation in already committed neuronal cells.

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Cell differentiation in vitro and the expression of Oct‐2 protein and oct‐2 RNA

Cited by 5 publications

References 18 publications

Phospholipase C-η2 interacts with nuclear and cytoplasmic LIMK-1 during retinoic acid-stimulated neurite growth

Phospholipase C-η2 interacts with nuclear and cytoplasmic LIMK-1 during retinoic acid-stimulated neurite growth

Membrane targeting of the EF-hand containing calcium-sensing proteins CaBP7 and CaBP8

C38, equivalent to BM88, is developmentally expressed in maturing retinal neurons and enhances neuronal maturation

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