title: Mitogen-activated protein kinase signalling in oligodendrocytes: a comparison of primary cultures and CG-4.
abstract: 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.
authors.affiliation: Department of Medicine, Division of Neurology, UBC Hospital, University of British Columbia, 2211 Wesbrook Mall, BC, V6T 2B5, Vancouver, Canada.
authors.forename: R L
authors.initials: RL
authors.lastname: Stariha
authors.forename: S U
authors.initials: SU
authors.lastname: Kim
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D015415:Biomarkers; D016923:Cell Death; D002454:Cell Differentiation; D002455:Cell Division; D002460:Cell Line / Q000201:enzymology*; D002478:Cells, Cultured; D004790:Enzyme Induction; D005679:G(M3) Ganglioside / Q000096:biosynthesis; D005732:Gangliosides / Q000096:biosynthesis; D048031:JNK Mitogen-Activated Protein Kinases; D020935:MAP Kinase Signaling System; D019950:Mitogen-Activated Protein Kinase 1 / Q000502:physiology; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases / Q000502:physiology; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000502:physiology*; D009836:Oligodendroglia / Q000201:enzymology*; D011493:Protein Kinase C / Q000502:physiology; D051381:Rats; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D048051:p38 Mitogen-Activated Protein Kinases
chemical_list: D015415:Biomarkers; D005679:G(M3) Ganglioside; D005732:Gangliosides; D009419:Nerve Tissue Proteins; C033851:ganglioside, GD1b; D011493:Protein Kinase C; D048031:JNK Mitogen-Activated Protein Kinases; D019950:Mitogen-Activated Protein Kinase 1; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases; D048051:p38 Mitogen-Activated Protein Kinases; D013755:Tetradecanoylphorbol Acetate