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          Institute: MPI für Neurobiologie     Collection: Neuroimmunology     Display Documents



  history
ID: 10833.0, MPI für Neurobiologie / Neuroimmunology
Endoplasmic reticulum stress in PLP-overexpressing transgenic rats: Gray matter oligodendrocytes are more vulnerable than white matter oligodendrocytes
Authors:Bauer, Jan; Bradl, Monika; Klein, Matthias; Leisser, M.; Deckwerth, T. L.; Wekerle, Hartmut; Lassmann, Hans
Language:English
Date of Publication (YYYY-MM-DD):2002-01
Title of Journal:Journal of Neuropathology and Experimental Neurology
Journal Abbrev.:J. Neuropathol. Exp. Neurol.
Volume:61
Issue / Number:1
Start Page:12
End Page:22
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Studies dealing with transport of proteins from the oligodendrocyte cell body it) the myelin sheath reveal the presence of different transport pathways. Proteolipid protein (PLP) is synthesized at the rough endoplasmic reticulum (ER) and then processed through the Golgi apparatus and transported to the myelin membranes, Myelin basic protein (MBP) on the other hand is synthesized locally at the ends of cell processes where its messenger RNA is translated Oil free ribosomes, Here we show that in rats that overexpress PLP. impairment of PLP transport front the cell body to the processes interferes with the translocation of other membrane proteins such as myelin- associated glycoprotein (MAG) and myelin oligodendrocyte glycoprotein (MOG), but not with peripherally translated MBP. In addition, it also impedes the transport of non-myelin proteins, for example the amyloid precursor protein (APP). At the ultrastructural level, the ER of these metabolically disturbed oligodendrocytes revealed extreme swelling of the cisternae, and immunohistochemistry revealed intense expression of the ER chaperone molecule BiP/GRP78 and ER folding enzyme protein disulfide isomerase (PDI). These features Suggest that these oligodendrocytes, which were found exclusively in gray matter areas of the spinal cord, started in unfolded protein response while suffering from ER stress. Some of these disturbed oligodendrocytes were seen to undergo programmed cell death. These results indicate that gray matter oligodendrocyte differ from white matter Oligodendrocytes in their capacity to stabilize metabolic disturbances by an unfolded protein response.
Free Keywords:amyloid precursor protein (APP); endoplasmic reticulum; oligodendrocytes; proteolipid protein (PLP); rats; stress; transgenic
External Publication Status:published
Document Type:Article
Affiliations:MPI für Neurobiologie/Neuroimmunology (Wekerle)
External Affiliations:Univ Vienna, Brain Res Inst, Div Neuroimmunol, Spitalgasse 4,; A-1090 Vienna, Austria; Univ Vienna, Brain Res Inst, Div Neuroimmunol, A-1090 Vienna, Austria; Max Planck Inst Neurobiol, Dept Neuroimmunol, Martinsried, Germany; Idun Pharmaceut Inc, San Diego, CA USA
Identifiers:ISI:000173097300002
ISSN:0022-3069
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