Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes

摘要: The remarkable quantities of myelin membrane produced by oligodendrocytes has led us to examine the mechanisms involved in sorting and transport proteins lipids during myelinogenesis. Noting that it been proposed destined for apical surface polarized epithelial cells co-cluster with glycolipid-rich microdomains from trans-Golgi network (Simons van Meer: Biochemistry 27:6197-6202, 1988; Simons Wandinger-Ness: Cell 62:207-210, 1990), we hypothesized may adopt this mechanism Protein-lipid complexes were isolated utilizing detergent insolubility two-dimensional gel electrophoresis. A developmentally regulated protein, MVP17 (myelin vesicular protein 17 kDa), was identified. Microsequencing N-terminal peptide revealed a high homology human T-cell MAL (Alonso Weissman: Proc Nati Acad Sci USA 84:1997-2001, 1987). corresponding cDNA an oligodendrocyte library. predicted sequence showed 88.9% identity MAL, hydrophobicity profile suggested four transmembrane domains. In vitro translation demonstrated signal at deduced Mr kDa. Northern analyses indicated mRNA expression is restricted brain kidney up-regulated period active myelination. These data suggest biogenesis and/or function. © 1995 Wiley-Liss, Inc.