TPO1, a member of a novel protein family, is developmentally regulated in cultured oligodendrocytes

W. H.H. Krueger, G. E. Gonye, D. L. Madison, K. E. Murray, M. Kumar, N. Spoerel, S. E. Pfeiffer

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

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 n 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.

Original languageEnglish (US)
Pages (from-to)1343-1355
Number of pages13
JournalJournal of neurochemistry
Volume69
Issue number4
DOIs
StatePublished - Oct 1997

Keywords

  • Membrane protein
  • Myelin
  • OB- fold
  • Oligodendrocyte development
  • TPO1
  • Zinc finger

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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