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TPO1, a Member of a Novel Protein Family, Is Developmentally Regulated in Cultured Oligodendrocytes
Author(s) -
Krueger W. H. H.,
Gonye G. E.,
Madison D. L.,
Murray K. E.,
Kumar M.,
Spoerel N.,
Pfeiffer S. E.
Publication year - 1997
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1997.69041343.x
Subject(s) - myelin , biology , complementary dna , microbiology and biotechnology , oligodendrocyte , membrane protein , cytoplasm , open reading frame , biogenesis , proteolipid protein 1 , zinc finger , protein subcellular localization prediction , subcellular localization , peptide sequence , myelin basic protein , gene , biochemistry , transcription factor , membrane , central nervous system , neuroscience
Although the myelin membrane contains only a small set of major proteins, more sensitive assays indicate the presence of a plethora of uncharacterized proteins. We have used an antibody perturbation approach to reversibly block the differentiation of prooligodendroblasts into myelinating cells, and, in combination with a differential screening procedure, identified novel mRNAs that are activated during this period. One cDNA, TPO1, recognizes a 5.5‐kb mRNA that is strongly up‐regulated in oligodendrocytes after release of the differentiation block and that is expressed at high levels in brain tissue during active myelination. This cDNA represents at least two mRNAs differing from each other in their 5′‐termini. The TPO1 cDNA contains an open reading frame of 1,380 bp, encoding a protein of 51.8 kDa with a predicted pl of 9.1 that contains two regions homologous to nonclassic zinc finger motifs. Subcellular localization studies suggest the enriched presence of TPO1 in spherical structures along the major cytoplasmic processes of oligodendrocytes. TPO1, along with homologues expressed in testis, placenta, and PC12 cells, form a novel family of proteins with multiple hydrophobic domains possibly serving as membrane spanning regions. We postulate that in oligodendrocytes, TPO1 encodes a protein factor involved in myelin biogenesis.