Analysis of the intracellular localization of p73 N-terminal protein isoforms TAp73 and ∆Np73 in medulloblastoma cell lines
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Cell Nucleus metabolism MeSH
- Child MeSH
- DNA-Binding Proteins chemistry metabolism MeSH
- Intracellular Space metabolism MeSH
- Nuclear Proteins chemistry metabolism MeSH
- Humans MeSH
- Medulloblastoma metabolism pathology MeSH
- Cell Line, Tumor MeSH
- Tumor Suppressor Proteins chemistry metabolism MeSH
- Child, Preschool MeSH
- Protein Isoforms metabolism MeSH
- Tumor Protein p73 MeSH
- Protein Transport MeSH
- Check Tag
- Child MeSH
- Humans MeSH
- Male MeSH
- Child, Preschool MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- delta Np73 protein, human MeSH Browser
- DNA-Binding Proteins MeSH
- Nuclear Proteins MeSH
- Tumor Suppressor Proteins MeSH
- Protein Isoforms MeSH
- Tumor Protein p73 MeSH
- TP73 protein, human MeSH Browser
The protein homologous to the tumor suppressor p53, p73, has essential roles in development and tumorigenesis. This protein exists in a wide range of isoforms with different, even antagonistic, functions. However, there are virtually no detailed morphological studies analyzing the endogenous expression of p73 isoforms at the cellular level in cancer cells. In this study, we investigated the expression and subcellular distribution of two N-terminal isoforms, TAp73 and ΔNp73, in medulloblastoma cells using immunofluorescence microscopy. Both proteins were observed in all cell lines examined, but differences were noted in their intracellular localization between the reference Daoy cell line and four newly established medulloblastoma cell lines (MBL-03, MBL-06, MBL-07 and MBL-10). In the new cell lines, TAp73 and ΔNp73 were located predominantly in cell nuclei. However, there was heterogeneity in TAp73 distribution in the cells of all MBL cell lines, with the protein located in the nucleus and also in a limited non-random area in the cytoplasm. In a small percentage of cells, we detected cytoplasmic localization of TAp73 only, i.e., nuclear exclusion was observed. Our results provide a basis for future studies on the causes and function of distinct intracellular localization of p73 protein isoforms with respect to different protein-protein interactions in medulloblastoma cells.
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