Mutant p53 may selectively suppress glial specific proteins in pluripotential human neuroectodermal tumor cells.

Abstract

The p53 gene is mutated in pluripotential human neuroectodermal tumor DAOY cells which express both glial and neuronal markers. In most cells, nuclear m-p53 immunostaining was intense while cytoplasmic glial specific proteins (GSPs) were present at low levels. Conversely, glial fibrillary acidic protein (GFAP) and glutamine synthetase (GS) were expressed in the few cells devoid of nuclear m-p53 immunoreactivity. The level of neuron specific enolase (NSE) staining was low and not different between p53 positive and p53 negative cells. Therefore, a selective, mutually exclusive expression relationship exists between cytoplasmic GSPs and nuclear m-p53. Upon treatment with epidermal growth factor (EGF) and dibutyrylcyclic AMP, overall cytoplasmic GFAP and GS levels were increased while nuclear p53 was suppressed but a mutually exclusive expression pattern between these proteins was maintained. In cells which also express NSE, GFAP was selectively stimulated suggesting that nuclear expression of m-p53 and cytoplasmic expression of GSPs may be functionally related.

• Authors: H S U, A Banaie, L Rigby, J Chen
• Journal: Neuroscience letters (Neurosci Lett) Vol. 244 Issue 1 Pg. 41-6 (Mar 06 1998) ISSN: 0304-3940 [Print] Ireland
• PMID: 9578140 (Publication Type: Journal Article, Research Support, U.S. Gov't, Non-P.H.S.)

Chemical References

• Glial Fibrillary Acidic Protein
• Phosphopyruvate Hydratase
• Glutamate-Ammonia Ligase

Topics

• Cytoplasm (metabolism)
• Genes, p53
• Glial Fibrillary Acidic Protein (antagonists & inhibitors, biosynthesis)
• Glutamate-Ammonia Ligase (biosynthesis, genetics)
• Humans
• Immunohistochemistry
• Neuroectodermal Tumors (enzymology, genetics, metabolism)
• Phosphopyruvate Hydratase (biosynthesis, genetics)
• Point Mutation
• Polymerase Chain Reaction
• Tumor Cells, Cultured