Assignment of the human protein tyrosine phosphatase epsilon (PTPRE) gene to chromosome 10q26 by fluorescence in situ hybridization
- Univ. of Nijmegen (Netherlands); and others
Phosphorylation of cellular protein tyrosine residues is an important mechanism for the transduction of external signals to the intracellular compartment. Protein tyrosine phosphatases (PTPases) act in concert with protein tyrosine kinases (PTKs) to regulate the level of tyrosine phosphorylation in these proteins. PTKs have been studied in detail, and many have been shown to be proto-oncogenes. Because PTPases can be considered functional antagonists of PTKs it has been postulated that these PTPases might act as tumor suppressors. Over 30 different PTPase genes have been isolated so far, and the chromosomal localization has been determined for many of them. Comparison of such mapping data with temporal and spatial expression patterns of individual PTPase genes and losses of heterozygosity (LOH) in relevant tumor types could be indicative of their proposed tumor suppressive activity. Until now, chromosomal deletions have been reported only for the PTPRG gene in primary renal and lung carcinomas and cancer-derived cell lines, but a causal role for a loss of PTPase activity in tumor formation remains to be determined. 15 refs., 1 fig.
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 273473
- Journal Information:
- Genomics, Journal Name: Genomics Journal Issue: 1 Vol. 30; ISSN 0888-7543; ISSN GNMCEP
- Country of Publication:
- United States
- Language:
- English
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