Protein kinase C stimulation enhances the process formation of adult oligodendrocytes and induces proliferation

Althaus, Hans H.; Schröter, J.; Spoerri, P.E.; Schwartz, Peter J.; Klöppner, Sabine; Rohmann, A.; Neuhoff, Volker

doi:10.1002/jnr.490290408

Cited by 44 publications

(38 citation statements)

References 37 publications

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“…Previous studies have shown that phorbol esters induce striking changes in oligodendrocyte morphology and act as mitogens for oligodendrocyte progenitors, probably by way of activating PKC [24,[46][47][48]. Inter estingly, some of these effects of phorbol esters are strik ingly similar to those of PDGF and FGF, two of the factors that profoundly influence oligodendrocyte devel opment.…”

Section: Resultsmentioning

confidence: 78%

The Expression of Myristoylated Alanine-Rich C-Kinase Substrate in Oligodendrocytes Is Developmentally Regulated

Bhat

Zhang²,

Bhat³

1995

Dev Neurosci

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Myristoylated alanine-rich C-kinase substrate (MARCKS), a major substrate of activated protein kinase C (PKC), is thought to be involved in PKC-mediated signal transduction events. In the present study, we have examined the expression of MARCKS in primary cultures of rat glial cells. Western blot analysis of different glial cell types (i.e., astrocytes, oligodendrocytes and microglia) revealed a relatively high level of MARCKS protein in oligodendrocytes. MARCKS protein and MARCKS mRNA levels in oligodendrocytes increased with time in culture, indicating a developmental regulation in MARCKS gene expression in differentiating oligodendrocytes. Immunocytochemical examination of developing oligodendrocytes indicated a strong labeling of MARCKS distributed both in the cell body and in the lacy network of processes. These findings, in concert with our previous observations on the role of PKC in oligodendrogenesis, strongly implicate a PKC-signaling system in oligodendrocyte development.

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Section: Resultsmentioning

confidence: 78%

The Expression of Myristoylated Alanine-Rich C-Kinase Substrate in Oligodendrocytes Is Developmentally Regulated

Bhat

Zhang²,

Bhat³

1995

Dev Neurosci

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“…3) (Yong et al, 1988;Althaus et al, 1991;Yong et al, 1991Yong et al, , 1994. The importance of PKC in this phorbol esterinduced extension has been confirmed by showing that inhibitors of PKC can block this event (Yong et al, 1988;Althaus et al, 1991;Yong et al, 1994). Investigators have since attempted to determine the signalling events following PKC activation in OL, and have found various downstream regulators of this kinase.…”

Section: Mature Olmentioning

confidence: 98%

“…They can also be cultured in the mature GalC stage from adult mammalian tissue; for instance, purified or enriched populations of mature OL have been isolated from cow, pig, sheep and human tissue (Szuchet et al, 1980;Kim et al, 1983;Smyrnis et al, 1986;Kim, 1990;Althaus et al, 1991;Kim and Kim, 1991;Stariha et al, 1997). The obvious advantage of primary OL cultures is that the cultured cells have direct in vivo counterparts, unlike artificial cell lines.…”

Section: The Primary Oligodendrocyte Culture Modelmentioning

confidence: 99%

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Mitogen‐activated protein kinase signalling in oligodendrocytes: a comparison of primary cultures and CG‐4

Stariha¹,

Kim²

2001

Intl J of Devlp Neuroscience

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Oligodendrocytes play a significant role in the central nervous system, as these cells are responsible for myelinating axons and allowing for the efficient conduction of nerve impulses. Therefore, any understanding we can gain about the functional biology of oligodendrocytes will give us important insights into demyelinating diseases such as multiple sclerosis, where oligodendrocytes and myelin are damaged or destroyed. Currently, much attention has focussed on the role of a family of mitogen-activated protein kinases in OL. This kinase family includes the extracellular signal-regulated protein kinases (ERKs), the stress-activated c-Jun N-terminal kinase (JNK), and the 38 kDa high osmolarity glycerol response kinase (p38). The actions of mitogen-activated protein kinases in oligodendrocytes appear to range from proliferation and cell survival to differentiation and cell death. In the past, studies on oligodendrocytes have been hampered by the difficulties inherent in producing large enough quantities of these cells for experimentation. This problem arises in large part due to the post-mitotic nature of mature oligodendrocytes. Over the years, a cell line known as Central Glia-4 (CG-4) has become a popular oligodendrocyte model due to its potentially unlimited capacity for self-renewal. In this review, we will look at the suitability of the Central Glia-4 cell line as an oligodendrocyte model, specifically in respect to studies on mitogen-activated protein kinase signalling in oligodendrocytes.

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“…The only relevant contaminating cells at the time in vitro, where most of our experiments were performed, were positively labeled for glial fibrillary acidic protein; their number comes to approximately 10% of the cell population (Althaus et al, 1991). Hence, we investigated whether pig astrocytes respond to NGF.…”

Section: Which Glial Cell Type Expresses Trka?mentioning

confidence: 99%

Nerve growth factor signal transduction in mature pig oligodendrocytes

Hempel

Klöppner

et al. 1997

J. Neurosci. Res.

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It has previously been shown that nerve growth factor (NGF) is of functional significance for mature pig oligodendrocytes (OLs) in culture. The present data give evidence for the expression of TrkA, the so-called high-affinity NGF receptor, and of p75NTR, the so-called low-affinity NGF receptor. TrkA is upregulated during culturing, in contrast to the p75 receptor. Exposure of OLs to NGF induces an autophosphorylation of TrkA via its intrinsic tyrosine kinase. K-252a inhibits the TrkA autophosphorylation, which reduces the OL process formation to control levels. To the tyrosine-phosphorylated sites of TrkA several proteins, such as phospholipase C-gamma1, the adaptor protein SHC, the phosphotyrosine phosphatase SH-PTP2 (SYP) associate via their SH2 phosphotase SH-PTP2 domain. The association of SHC to TrkA is shown by co-immunoprecipitation. Indirect evidence for a possible activation of PLC-gamma1 is given by an NGF-induced increase of oligodendroglial [Ca2+]i. Downstream from TrkA, a mitogen-activated protein kinase cascade, which includes Erk1 and Erk2, is operating. An in-gel myelin basic protein kinase assay revealed that NGF activates predominantly Erk1. Finally, it is shown that NGF stimulates expression of c-fos.

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Protein kinase C stimulation enhances the process formation of adult oligodendrocytes and induces proliferation

Cited by 44 publications

References 37 publications

The Expression of Myristoylated Alanine-Rich C-Kinase Substrate in Oligodendrocytes Is Developmentally Regulated

The Expression of Myristoylated Alanine-Rich C-Kinase Substrate in Oligodendrocytes Is Developmentally Regulated

Mitogen‐activated protein kinase signalling in oligodendrocytes: a comparison of primary cultures and CG‐4

Nerve growth factor signal transduction in mature pig oligodendrocytes

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