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Differential expression of a novel murine non-receptor protein tyrosine phosphatase during differentiation of P19 embryonal carcinoma cells
- Source :
- Biochemical and Biophysical Research Communications. 184:1241-1249
- Publication Year :
- 1992
- Publisher :
- Elsevier BV, 1992.
-
Abstract
- Summary Protein phosphorylation on tyrosine residues is one of the major mechanisms of cell signal transduction and is regulated by protein tyrosine kinases and protein tyrosine phosphatases. Here we report the molecular cloning of an additional member of the protein tyrosine phosphatase-family from differentiated murine P19 embryonal carcinoma cells. This non-receptor protein tyrosine phosphatase, P19-PTP, does not contain regulatory sequences, homologous to the ones found in other non-receptor PTPases. P19-PTP is differentially expressed during in vitro differentiation of P19 EC cells, in that P19-PTP mRNA could only be detected in embryoid bodies, derived from P19 cells.
- Subjects :
- Molecular Sequence Data
Restriction Mapping
Biophysics
Protein tyrosine phosphatase
Regulatory Sequences, Nucleic Acid
Biology
SH2 domain
Polymerase Chain Reaction
environment and public health
Biochemistry
Gene Expression Regulation, Enzymologic
Receptor tyrosine kinase
Cell Line
Mice
Sequence Homology, Nucleic Acid
Animals
Amino Acid Sequence
RNA, Messenger
Cloning, Molecular
Tyrosine
Molecular Biology
Gene Library
Base Sequence
GRB10
Teratoma
Cell Differentiation
Cell Biology
Molecular biology
Gene Expression Regulation, Neoplastic
enzymes and coenzymes (carbohydrates)
Oligodeoxyribonucleotides
embryonic structures
ROR1
biology.protein
Protein Tyrosine Phosphatases
Tyrosine kinase
Signal Transduction
Proto-oncogene tyrosine-protein kinase Src
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 184
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....37d182213985c520b5c8b162443e6878
- Full Text :
- https://doi.org/10.1016/s0006-291x(05)80015-4