Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Differentiation*
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Cell Line
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Cloning, Molecular
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Gene Expression Regulation, Enzymologic*
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Gene Expression Regulation, Neoplastic*
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Gene Library
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Mice
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Molecular Sequence Data
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Oligodeoxyribonucleotides
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Polymerase Chain Reaction / methods
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Protein Tyrosine Phosphatases / genetics*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Regulatory Sequences, Nucleic Acid
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Restriction Mapping
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Sequence Homology, Nucleic Acid
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Signal Transduction
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Teratoma
Substances
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Oligodeoxyribonucleotides
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RNA, Messenger
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Protein Tyrosine Phosphatases
Associated data
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GENBANK/D10272
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GENBANK/D10273
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GENBANK/D10274
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GENBANK/D10275
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GENBANK/D10276
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GENBANK/M90099
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GENBANK/S36169
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GENBANK/S88464
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GENBANK/S88466
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GENBANK/S88468