Article
Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation.
The Journal of biological chemistry - 7 Sept 2001
Chiarugi P, Fiaschi T, Taddei M L, Talini D, Giannoni E, Raugei G, Ramponi G
Abstract excerpt
Low molecular weight protein tyrosine phosphatase (LMW-PTP) is an enzyme involved in platelet-derived growth factor (PDGF)-induced mitogenesis and cytoskeleton rearrangement because it is able to bind and dephosphorylate the activated receptor. LMW-PTP presents two cysteines in positions 12 and 17, both belonging to the catalytic pocket; this is a unique feature of LMW-PTP among all protein tyrosine phosphatases....
Topics
- 3T3 Cells
- Animals
- Blotting, Northern
- Blotting, Western
- Catalysis
- Cell Line
- Culture Media, Serum-Free
- Cysteine
- Enzyme Activation
- Glutathione
- Humans
- Hydrogen Peroxide
- Isoenzymes