TY - JOUR
T1 - Oxidative modification of protein tyrosine phosphatases.
AU - Wu, Ru Feng
AU - Terada, Lance S.
PY - 2006/4/25
Y1 - 2006/4/25
N2 - Our understanding of the biological effects of reactive oxidants has deepened considerably over the past decade. Less the indiscriminate loose cannons we previously imagined, both superoxide and hydrogen peroxide appear to target relatively specific molecular structures. Perhaps the most consequential of such targets within proteins is the reduced sulfhydryl of cysteine residues. Because protein tyrosine phosphatases (PTPs) all harbor an absolutely conserved catalytic cysteine residue, oxidation of this residue inactivates PTPs, rendering tyrosine kinase signaling pathways highly sensitive to the local redox environment. Therefore, tyrosine phosphorylation-dependent signaling involving receptor tyrosine kinases, mitogen-activated protein kinases, Abl, Src, and Pyk2 is known to be initiated or amplified by reactive oxidants. We describe a nonradioisotopic method that discriminates between reduced and oxidatively modified tyrosine phosphatases, thus facilitating studies that may mechanistically link oxidant activity with specific signaling pathways.
AB - Our understanding of the biological effects of reactive oxidants has deepened considerably over the past decade. Less the indiscriminate loose cannons we previously imagined, both superoxide and hydrogen peroxide appear to target relatively specific molecular structures. Perhaps the most consequential of such targets within proteins is the reduced sulfhydryl of cysteine residues. Because protein tyrosine phosphatases (PTPs) all harbor an absolutely conserved catalytic cysteine residue, oxidation of this residue inactivates PTPs, rendering tyrosine kinase signaling pathways highly sensitive to the local redox environment. Therefore, tyrosine phosphorylation-dependent signaling involving receptor tyrosine kinases, mitogen-activated protein kinases, Abl, Src, and Pyk2 is known to be initiated or amplified by reactive oxidants. We describe a nonradioisotopic method that discriminates between reduced and oxidatively modified tyrosine phosphatases, thus facilitating studies that may mechanistically link oxidant activity with specific signaling pathways.
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U2 - 10.1126/stke.3322006pl2
DO - 10.1126/stke.3322006pl2
M3 - Article
C2 - 16639034
AN - SCOPUS:33745482974
SN - 1937-9145
VL - 2006
SP - pl2
JO - Science's STKE : signal transduction knowledge environment
JF - Science's STKE : signal transduction knowledge environment
IS - 332
ER -