Negative growth control by a novel lowMrphosphotyrosine protein phosphatase in normal and transformed cells
- 1 July 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 326 (1-3) , 294-298
- https://doi.org/10.1016/0014-5793(93)81811-d
Abstract
Having determined the complete amino acid sequence of a cytosolic phosphatase purified from bovine liver, we studied the role of this enzyme (referred to as ‘PTPase’) in the control of cell proliferation. We used NIH/3T3 fibroblasts, both normal and transformed by the oncogenes v‐erbB, v‐src, and v‐raf: a synthetic gene coding for PTPase was transfected into, and overexpressed in, normal and transformed NIH/3T3 cells with resulting inhibition of cell growth. Inhibition of proliferation correlated with the level of foreign PTPase; growth in soft agar was also inhibited in transformants overexpressing the enzyme. However, PTPase overexpression did not inhibit the rapid turnover of inositol lipids stimulated by platelet‐derived growth factor. We conclude that this novel PTPase is active on cell type‐specific signalling substrates that control normal and transformed fibroblast proliferation.Keywords
This publication has 18 references indexed in Scilit:
- Differential role of four cysteines on the activity of a low Mr phosphotyrosine protein phosphataseFEBS Letters, 1992
- A thousand and two protein tyrosine phosphatasesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1992
- Overexpression of a synthetic phosphotyrosine protein phosphatase gene inhibits normal and transformed cell growthInternational Journal of Cancer, 1992
- Rat liver lowMr phosphotyrosine protein phosphatase isoenzymes: Purification and amino acid sequencesProtein Journal, 1992
- Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heartBiochemistry, 1992
- Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane EnzymesScience, 1991
- The possibility of participation of different protein kinases in the regulation of degradation of Glp6[125I]Tyr8SP6–11 with different endopeptidases in subcellular fractions of rat brainInternational Journal of Biochemistry, 1991
- Purification and characterization of a low-molecular-weight acid phosphatase—A phosphotyrosyl-protein phosphatase from bovine heartArchives of Biochemistry and Biophysics, 1990
- The 18 kDa cytosolic acid phosphatase from bovine liver has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptorFEBS Letters, 1989
- Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.The Journal of cell biology, 1987