Defective biosynthesis of proteolipid protein in Pelizaeus-Merzbacher disease.
The brain of an 18-year-old patient with Pelizaeus-Merzbacher disease was examined by standard neuropathological and biochemical methods and by immunocytochemical and immunochemical techniques. Analysis revealed a lack of myelin-specific lipids, but showed a residual immunoreactivity for myelin basic protein, myelin-associated glycoprotein, and 2',3'-cyclic nucleotide-3'-phosphodiesterase. Examination by immunocytochemistry and enzyme-linked immunosorbent assay showed an absence of proteolipid apoprotein (lipophilin). The peripheral nervous system was normal. Pelizaeus-Merzbacher disease in humans shares many neuropathological and biochemical features with X-linked mutations in animals, e.g., the jimpy mouse and myelin-deficient rat. The specificity of this protein deficiency in Pelizaeus-Merzbacher disease gains additional support from the recent mapping of the lipophilin gene to the human X chromosome.
D000293:Adolescent; D001921:Brain / Q000378:metabolism / Q000473:pathology; D002490:Central Nervous System / Q000378:metabolism; D002648:Child; D002549:Diffuse Cerebral Sclerosis of Schilder / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D006651:Histocytochemistry; D006801:Humans; D007120:Immunochemistry; D050356:Lipid Metabolism; D008297:Male; D009185:Myelin Proteins / Q000378:metabolism; D009186:Myelin Sheath / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000096:biosynthesis*; D009900:Optic Nerve / Q000378:metabolism; D010375:Pedigree; D011510:Proteolipids / Q000096:biosynthesis*
D009185:Myelin Proteins; D009419:Nerve Tissue Proteins; D011510:Proteolipids