Inhibition of protein tyrosine phosphatase activity by diamide is reversed by epidermal growth factor in fibroblasts
- 16 December 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 295 (1-3) , 146-148
- https://doi.org/10.1016/0014-5793(91)81405-w
Abstract
Diamide (azodicarboxylic acid bis(dimethylamide)) inhibits protein tyrosine phosphatase activity in fibroblasts without altering protein tyrosine kinase activity associated with the epidermal growth factor receptor. The loss of protein tyrosine phosphatase activity caused by diamide is reversed by 2-mercaptoethanol or epidermal growth factorKeywords
This publication has 11 references indexed in Scilit:
- Redox regulation of a protein tyrosine kinase in the endoplasmic reticulumCell, 1991
- Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane EnzymesScience, 1991
- Signal transduction by receptors with tyrosine kinase activityPublished by Elsevier ,1990
- EGF induces tyrosine phosphorylation of phospholipase C-II: A potential mechanism for EGF receptor signalingCell, 1989
- Phosphotyrosyl protein phosphatasesBiochemical Journal, 1989
- Purification of the major protein-tyrosine-phosphatases of human placenta.Journal of Biological Chemistry, 1988
- Chicken epidermal growth factor (EGF) receptor: cDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor alpha.Molecular and Cellular Biology, 1988
- Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routingCell, 1987
- Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.Proceedings of the National Academy of Sciences, 1987
- Identification, purification, and characterization of phosphotyrosine-specific protein phosphatases from cultured chicken embryo fibroblasts.Molecular and Cellular Biology, 1984