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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Arrest of proteolipid transport through the Golgi apparatus in Jimpy brain.

Immunocytochemical investigations were performed on Jimpy and control mouse brains using three specific anti-myelin proteolipids antisera: immunoaffinity purified multivalent anti-(PLP + DM-20) proteolipid antibodies, anti-C-terminal hexapeptide 271-276 and anti-tridecapeptide 117-129 antisera. The results show that oligodendrocytes and myelin sheaths in normal mouse brain are labelled to the same extent by the three specific antisera; in contrast, in Jimpy brain these cellular structures are only stained by the multivalent antibodies and the site-specific, anti-tridecapeptide antiserum. The absence of labelling with C-terminal hexapeptide antiserum in mutant brain is interpreted as the result of either a large deletion or a point mutation producing a frameshift in the C-terminal part of the sequences of the proteolipids PLP and DM-20. Furthermore, we show that this mutation prevents the normal transport of proteolipid molecules through the Golgi apparatus. The existence of a minor, extra-Golgi apparatus metabolic route for proteolipids to myelin structures is also discussed.[1]


  1. Arrest of proteolipid transport through the Golgi apparatus in Jimpy brain. Roussel, G., Neskovic, N.M., Trifilieff, E., Artault, J.C., Nussbaum, J.L. J. Neurocytol. (1987) [Pubmed]
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