[HTML][HTML] Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor …
P Chiarugi, T Fiaschi, ML Taddei, D Talini… - Journal of Biological …, 2001 - ASBMB
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. Our previous results
demonstrated that in vitro LMW-PTP is oxidized by either H 2 O 2 or nitric oxide with the …
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. Our previous results
demonstrated that in vitro LMW-PTP is oxidized by either H 2 O 2 or nitric oxide with the …