Effects of H2O2 on protein tyrosine phosphatase activity in HER14 cells

Stephen Gene Sullivan; Daniel T.Y. Chiu; Mourad Errasfa; Jamin M. Wang; Qi Jian-Shen Qi; Arnold Stern

doi:10.1016/0891-5849(94)90042-6

Effects of H₂O₂ on protein tyrosine phosphatase activity in HER14 cells

Stephen Gene Sullivan, Daniel T.Y. Chiu, Mourad Errasfa, Jamin M. Wang, Qi Jian-Shen Qi, Arnold Stern^*

^*Corresponding author for this work

Department of Medical Biotechnology and Laboratory Science

Research output: Contribution to journal › Journal Article › peer-review

105 Scopus citations

Abstract

Oxidative stress has been implicated in protein phosphorylation and dephosphorylation in cells. In our current studies, H₂O₂ was shown to reversibly inhibit protein tyrosine phosphatase (PTPase) activity in HER14 cells. H₂O₂ (150 mM) resulted in 40% inhibition of PTPase activity by 15 min and recovery from inhibition was nearly complete by 60 min. H₂O₂-induced inhibition or recovery of PTPase activity was not affected by cycloheximide, a protein synthesis inhibitor. L-Buthionine-[S,R]-sulfoximine (BSO), an inhibitor of glutathione synthesis, had no effect on H₂O₂-induced inhibition of PTPase activity but retarded the recovery of activity. Epidermal growth factor (EGF) and EGTA, a Ca²⁺ chelator, did not influence H₂O₂-induced inhibition or recovery of PTPase activity. These results suggest that at least 40% of fibroblast PTPase activity can be regulated by cellular redox activity.

Original language	English
Pages (from-to)	399-403
Number of pages	5
Journal	Free Radical Biology and Medicine
Volume	16
Issue number	3
DOIs	https://doi.org/10.1016/0891-5849(94)90042-6
State	Published - 03 1994

Keywords

Free radicals
HER14 cells
HO
Protein tyrosine phosphatase

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10.1016/0891-5849(94)90042-6

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title = "Effects of H2O2 on protein tyrosine phosphatase activity in HER14 cells",

abstract = "Oxidative stress has been implicated in protein phosphorylation and dephosphorylation in cells. In our current studies, H2O2 was shown to reversibly inhibit protein tyrosine phosphatase (PTPase) activity in HER14 cells. H2O2 (150 mM) resulted in 40% inhibition of PTPase activity by 15 min and recovery from inhibition was nearly complete by 60 min. H2O2-induced inhibition or recovery of PTPase activity was not affected by cycloheximide, a protein synthesis inhibitor. L-Buthionine-[S,R]-sulfoximine (BSO), an inhibitor of glutathione synthesis, had no effect on H2O2-induced inhibition of PTPase activity but retarded the recovery of activity. Epidermal growth factor (EGF) and EGTA, a Ca2+ chelator, did not influence H2O2-induced inhibition or recovery of PTPase activity. These results suggest that at least 40% of fibroblast PTPase activity can be regulated by cellular redox activity.",

keywords = "Free radicals, HER14 cells, HO, Protein tyrosine phosphatase",

author = "Sullivan, {Stephen Gene} and Chiu, {Daniel T.Y.} and Mourad Errasfa and Wang, {Jamin M.} and {Jian-Shen Qi}, Qi and Arnold Stern",

year = "1994",

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AU - Sullivan, Stephen Gene

AU - Chiu, Daniel T.Y.

AU - Errasfa, Mourad

AU - Wang, Jamin M.

AU - Jian-Shen Qi, Qi

AU - Stern, Arnold

PY - 1994/3

Y1 - 1994/3

N2 - Oxidative stress has been implicated in protein phosphorylation and dephosphorylation in cells. In our current studies, H2O2 was shown to reversibly inhibit protein tyrosine phosphatase (PTPase) activity in HER14 cells. H2O2 (150 mM) resulted in 40% inhibition of PTPase activity by 15 min and recovery from inhibition was nearly complete by 60 min. H2O2-induced inhibition or recovery of PTPase activity was not affected by cycloheximide, a protein synthesis inhibitor. L-Buthionine-[S,R]-sulfoximine (BSO), an inhibitor of glutathione synthesis, had no effect on H2O2-induced inhibition of PTPase activity but retarded the recovery of activity. Epidermal growth factor (EGF) and EGTA, a Ca2+ chelator, did not influence H2O2-induced inhibition or recovery of PTPase activity. These results suggest that at least 40% of fibroblast PTPase activity can be regulated by cellular redox activity.

AB - Oxidative stress has been implicated in protein phosphorylation and dephosphorylation in cells. In our current studies, H2O2 was shown to reversibly inhibit protein tyrosine phosphatase (PTPase) activity in HER14 cells. H2O2 (150 mM) resulted in 40% inhibition of PTPase activity by 15 min and recovery from inhibition was nearly complete by 60 min. H2O2-induced inhibition or recovery of PTPase activity was not affected by cycloheximide, a protein synthesis inhibitor. L-Buthionine-[S,R]-sulfoximine (BSO), an inhibitor of glutathione synthesis, had no effect on H2O2-induced inhibition of PTPase activity but retarded the recovery of activity. Epidermal growth factor (EGF) and EGTA, a Ca2+ chelator, did not influence H2O2-induced inhibition or recovery of PTPase activity. These results suggest that at least 40% of fibroblast PTPase activity can be regulated by cellular redox activity.

KW - Free radicals

KW - HER14 cells

KW - HO

KW - Protein tyrosine phosphatase

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SN - 0891-5849

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JO - Free Radical Biology and Medicine

JF - Free Radical Biology and Medicine

IS - 3

ER -

Effects of H₂O₂ on protein tyrosine phosphatase activity in HER14 cells

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