Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

Lee, Seung-Rock; Kwon, Ki-Sun; Kim, Seung-Ryul; Rhee, Sue Goo

doi:10.1074/jbc.273.25.15366

Cited by 969Protein Tyrosine PhosphatasesRedox biology and oxidative stressProtein Kinase Regulation and GTPase Signaling

Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

Open access

Lee, Seung-Rock, Kwon, Ki-Sun, Kim, Seung-Ryul, Rhee, Sue Goo·1998·Journal of Biological Chemistry

DOI 10.1074/jbc.273.25.15366

Open this paper in CoChat — free account

Abstract

Stimulation of various cells with growth factors results in a transient increase in the intracellular concentration of H2O2 that is required for growth factor-induced protein tyrosine phosphorylation. The effect of H2O2 produced in response to epidermal growth factor (EGF) on the activity of protein-tyrosine phosphatase 1B (PTP1B) was investigated in A431 human epidermoid carcinoma cells. H2O2 inactivated recombinant PTP1B in vitro by oxidizing its catalytic site cysteine, most likely to sulfenic acid. The oxidized enzyme was reactivated more effectively by thioredoxin than by glutaredoxin or glutathione at their physiological concentrations. Oxidation by H2O2 prevented modification of the catalytic cysteine of PTP1B by iodoacetic acid, suggesting that it should be possible to monitor the oxidation state of PTP1B in cells by measuring the incorporation of radioactivity into the enzyme after lysis of the cells in the presence of radiolabeled iodoacetic acid. The amount of such radioactivity associated with PTP1B immunoprecipitated from A431 cells that had been stimulated with EGF for 10 min was 27% less than that associated with PTP1B from unstimulated cells. The amount of iodoacetic acid-derived radioactivity associated with PTP1B reached a minimum 10 min after stimulation of cells with EGF and returned to base line values by 40 min, suggesting that the oxidation of PTP1B is reversible in cells. These results indicate that the activation of a receptor tyrosine kinase by binding of the corresponding growth factor may not be sufficient to increase the steady state level of protein tyrosine phosphorylation in cells and that concurrent inhibition of protein-tyrosine phosphatases by H2O2 might also be required.

Integrity signals

Registry

Crossref · 10.1074/jbc.273.25.15366

Cites

53 of 53 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Protein tyrosine phosphatase 1B was the first phosphatase demonstrated to be inhibited by ROS under physiological conditions.
“Protein tyrosine phosphatase 1B was the first phosphatase demonstrated to be inhibited by ROS under physiological conditions 49, 50.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [49]

Tissue sulfhydryl groups
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,383 · see citing works
Requirement for Generation of H 2 O 2 for Platelet-Derived Growth Factor Signal Transduction
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968 · see citing works
Mitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588 · see citing works
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208 · see citing works
Self-citation
Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane Enzymes
Fischer, E. H., Charbonneau, H., & Tonks, N. K. (1991) · Science · doi:10.1126/science.1650499 · Cited by 969 · see citing works
Mechanism of Inhibition of Protein-tyrosine Phosphatases by Vanadate and Pervanadate
Huyer, G., Liu, S., Kelly, J., Moffat, J., Payette, P., Kennedy, B. P., Tsaprailis, G., Gresser, M. J., & Ramachandran, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.843 · Cited by 815 · see citing works
Development of “substrate-trapping” mutants to identify physiological substrates of protein tyrosine phosphatases
Flint, A. J., Tiganis, T., Barford, D., & Tonks, N. K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1680 · Cited by 775 · see citing works
CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B
Barford, D., Flint, A. J., & Tonks, N. K. (1994) · Science · doi:10.1126/science.8128219 · Cited by 762 · see citing works
Rat liver thioredoxin and thioredoxin reductase: purification and characterization
Luthman, M., & Holmgren, A. (1982) · Biochemistry · doi:10.1021/bi00269a003 · Cited by 603 · see citing works
The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
Frangioni, J. V., Beahm, P. H., Shifrin, V. I., Jost, C. A., & Neel, B. G. (1992) · Cell · doi:10.1016/0092-8674(92)90190-n · Cited by 596 · see citing works
Purification of the major protein-tyrosine-phosphatases of human placenta.
Tonks, N. K., Diltz, C. D., & Fischer, E. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68702-2 · Cited by 570 · see citing works
From Form to Function: Signaling by Protein Tyrosine Phosphatases
Tonks, N. K., & Neel, B. G. (1996) · Cell · doi:10.1016/s0092-8674(00)81357-4 · Cited by 537 · see citing works
Involvement of Reactive Oxygen Species in Cytokine and Growth Factor Induction of c-fos Expression in Chondrocytes
Lo, Y. Y. C., & Cruz, T. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11727 · Cited by 530 · see citing works
Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents.
Knebel, A., Rahmsdorf, H. J., Ullrich, A., & Herrlich, P. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00916.x · Cited by 514 · see citing works
Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.
Gladyshev, V. N., Jeang, K.-T., & Stadtman, T. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.6146 · Cited by 471 · see citing works
Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate.
Guan, K., & Dixon, J. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47335-3 · Cited by 460 · see citing works
The insulinomimetic agents H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells.
Heffetz, D., Bushkin, I., Dror, R., & Zick, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39885-0 · Cited by 429 · see citing works
The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase.
Björnstedt, M., Xue, J., Huang, W., Åkesson, B., & Holmgren, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43889-6 · Cited by 364 · see citing works
Isolation of phosphorylated peptides and proteins on ion exchange papers
Glass, D. B., Masaracchia, R. A., Feramisco, J. R., et al. (1978) · Analytical Biochemistry · doi:10.1016/0003-2697(78)90707-8 · Cited by 356 · see citing works
Form and Function in Protein Dephosphorylation
Denu, J. M., Stuckey, J. A., Saper, M. A., & Dixon, J. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81356-2 · Cited by 330 · see citing works
Calpain‐catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP‐1B) in human platelets.
Frangioni, J. V., Oda, A., Smith, M., et al. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06174.x · Cited by 305 · see citing works
Active site labeling of the Yersinia protein tyrosine phosphatase: The determination of the pKa of the active site cysteine and the function of the conserved histidine 402
Zhang, Z. Y., & Dixon, J. E. (1993) · Biochemistry · doi:10.1021/bi00087a012 · Cited by 275 · see citing works
Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins.
Charbonneau, H., Tonks, N. K., Kumar, S., Diltz, C. D., Harrylock, M., Cool, D. E., Krebs, E. G., Fischer, E. H., & Walsh, K. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5252 · Cited by 274 · see citing works
Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate In vitro
Hecht, D., & Zick, Y. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91123-8 · Cited by 273 · see citing works
Dimerization-Induced Inhibition of Receptor Protein Tyrosine Phosphatase Function Through an Inhibitory Wedge
Majeti, R., Bilwes, A. M., Noel, J. P., et al. (1998) · Science · doi:10.1126/science.279.5347.88 · Cited by 266 · see citing works
Protein-Tyrosine Phosphatase 1B Complexes with the Insulin Receptor in Vivo and Is Tyrosine-phosphorylated in the Presence of Insulin
Bandyopadhyay, D., Kusari, A. B., Kenner, K. A., Liu, F., Chernoff, J., Gustafson, T. A., & Kusari, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1639 · Cited by 258 · see citing works
Formation and reactions of sulfenic acids in proteins
Allison, W. S. (1976) · Accounts of Chemical Research · doi:10.1021/ar50104a003 · Cited by 255 · see citing works
Protein-tyrosine phosphatases.
Stone, R. L., & Dixon, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31694-6 · Cited by 219 · see citing works
Cloning of a cDNA for a major human protein-tyrosine-phosphatase.
Chernoff, J., Schievella, A. R., Jost, C. A., Erikson, R. L., & Neel, B. G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.7.2735 · Cited by 218 · see citing works
Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells
Fernando, M. R., Nanri, H., YOSHITAKE, S., et al. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17363.x · Cited by 212 · see citing works
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
Su, X., Taddei, N., Stefani, M., Ramponi, G., & Nordlund, P. (1994) · Nature · doi:10.1038/370575a0 · Cited by 204 · see citing works
Intramolecular Regulation of Protein Tyrosine Phosphatase SH-PTP1: A New Function for Src Homology 2 Domains
Pei, D., Lorenz, U. M., Klingmüller, U., Neel, B. G., & Walsh, C. T. (1994) · Biochemistry · doi:10.1021/bi00255a030 · Cited by 198 · see citing works
Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor
Liu, F., & Chernoff, J. (1997) · Biochemical Journal · doi:10.1042/bj3270139 · Cited by 179 · see citing works
Roles of Aspartic Acid-181 and Serine-222 in Intermediate Formation and Hydrolysis of the Mammalian Protein-Tyrosine-Phosphatase PTP1
Lohse, D. L., Denu, J. M., Santoro, N., & Dixon, J. E. (1997) · Biochemistry · doi:10.1021/bi963094r · Cited by 179 · see citing works
Multi‐site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation.
Flint, A. J., Gebbink, M. F. B. G., Franza, B. R., HILL, D. E., & Tonks, N. K. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05843.x · Cited by 157 · see citing works
Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay
Holmgren, A., & Luthman, M. (1978) · Biochemistry · doi:10.1021/bi00612a031 · Cited by 151 · see citing works
Nitric oxide causes inactivation of the low molecular weight phosphotyrosine protein phosphatase.
Caselli, A., Camici, G. G., Manao, G., Moneti, G., Pazzagli, L., Cappugi, G., & Ramponi, G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31472-2 · Cited by 142 · see citing works
Role of Oxidative Stress in the Action of Vanadium Phosphotyrosine Phosphatase Inhibitors
Krejsa, C. M., Nadler, S. G., Esselstyn, J. M., Kavanagh, T. J., Ledbetter, J. A., & Schieven, G. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11541 · Cited by 141 · see citing works
Glutaredoxin from calf thymus. Purification to homogeneity.
Luthman, M., & Holmgren, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34484-3 · Cited by 134 · see citing works
Regulation of tyrosine phosphorylation in neutrophils by the NADPH oxidase. Role of reactive oxygen intermediates
Fialkow, L., Chan, C. K., Grinstein, S., & Downey, G. P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85312-7 · Cited by 131 · see citing works
Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase.
Pot, D., Woodford-Thomas, T. A., Remboutsika, E., Haun, R. S., & Dixon, J. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55047-x · Cited by 130 · see citing works
Effects of H2O2 on protein tyrosine phosphatase activity in HER14 cells
Sullivan, S. G., Chiu, D. T.-Y., Errasfa, M., Wang, J. M., Qi, J.-S., & Stern, A. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90042-6 · Cited by 122 · see citing works
The catalytic role of Cys124 in the dual specificity phosphatase VHR.
Zhou, G. W., Denu, J. M., Wu, L. J., & Dixon, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46898-6 · Cited by 119 · see citing works
The Catalytic Role of Aspartic Acid-92 in the Human Dual-Specific Protein-Tyrosine-Phosphatase Vaccinia H1-Related
Denu, J. M., Zhou, G. W., Guo, Y., et al. (1995) · Biochemistry · doi:10.1021/bi00010a031 · Cited by 112 · see citing works
Possible Differences in the Regenerative Roles Played by Thioltransferase and Thioredoxin for Oxidatively Damaged Proteins
Yoshitake, S.-I., Nanri, H., Fernando, M. R., et al. (1994) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124500 · Cited by 92 · see citing works
Inhibition of the activity of protein tyrosine phosphatase 1C by its SH2 domains
Townley, R., Shen, S. H., Banville, D., et al. (1993) · Biochemistry · doi:10.1021/bi00212a006 · Cited by 86 · see citing works
How Does Alendronate Inhibit Protein-tyrosine Phosphatases?
Skorey, K., Ly, H. D., Kelly, J., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22472 · Cited by 75 · see citing works
Calcium-dependent Signaling Pathways in T Cells
Rock, M. T., Brooks, W. H., & Roszman, T. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33377 · Cited by 69 · see citing works
Phosphorylation of Protein-tyrosine Phosphatase PTP-1B on Identical Sites Suggests Activation of a Common Signaling Pathway during Mitosis and Stress Response in Mammalian Cells
Shifrin, V. I., Davis, R. J., & Neel, B. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2957 · Cited by 49 · see citing works
Inhibition of CD45 during neutrophil activation
Fialkow, L., Chan, C. K., & Downey, G. P. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.11.5409 · Cited by 47 · see citing works
Purification and properties of bovine thioredoxin system
Martı́nez-Galisteo, E., Padilla, C. A., García-Alfonso, C., et al. (1993) · Biochimie · doi:10.1016/0300-9084(93)90131-b · Cited by 45 · see citing works
Nucleotide sequence of a cDNA encoding rat thioredoxin
Tonissen, K. F., Robins, A. J., & Wells, J. R. E. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.10.3973 · Cited by 30 · see citing works

Flagged first, then by citations

Sorted by citations

Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413 · see citing works
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
ROS function in redox signaling and oxidative stress
Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931 · see citing works
Role of nrf2 in oxidative stress and toxicity
Ma, Q. (2013) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140320 · Cited by 4,903 · see citing works
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373 · see citing works
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Griendling, K. K., Sorescu, D., & Ushio-Fukai, M. (2000) · Circulation Research · doi:10.1161/01.res.86.5.494 · Cited by 2,886 · see citing works
Signal transduction by reactive oxygen species
Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322 · see citing works
The thioredoxin antioxidant system
Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055 · see citing works
Redox regulation of cell survival
Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781 · see citing works
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works
Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040 · see citing works
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
Alpha-lipoic acid as a dietary supplement: Molecular mechanisms and therapeutic potential
Shay, K. P., Moreau, R. F., Smith, E. J., Smith, A. R., & Hagen, T. M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.07.026 · Cited by 976 · see citing works
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951 · see citing works
Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
Forman, H. J., & Torres, M. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206007 · Cited by 891 · see citing works
ATP Activates a Reactive Oxygen Species-dependent Oxidative Stress Response and Secretion of Proinflammatory Cytokines in Macrophages
Cruz, C. M., Rinna, A., Forman, H. J., Ventura, A. L. M., Persechini, P. M., & Ojcius, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608083200 · Cited by 786 · see citing works
Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784 · see citing works
Self-citation
Redox signaling: hydrogen peroxide as intracellular messenger
Rhee, S. G. (1999) · Experimental & Molecular Medicine · doi:10.1038/emm.1999.9 · Cited by 701 · see citing works
Self-citation
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633 · see citing works
Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
Self-citation
Redox signaling and the MAP kinase pathways
Torres, M., & Forman, H. J. (2003) · BioFactors · doi:10.1002/biof.5520170128 · Cited by 580 · see citing works
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542 · see citing works
Mathematical Models of Protein Kinase Signal Transduction
Heinrich, R., Neel, B. G., & Rapoport, T. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00528-2 · Cited by 511 · see citing works
Molecular Mechanisms and Clinical Implications of Reversible Protein S -Glutathionylation
Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., & Shelton, M. D. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523 · see citing works
Insulin-stimulated Hydrogen Peroxide Reversibly Inhibits Protein-tyrosine Phosphatase 1B in Vivo and Enhances the Early Insulin Action Cascade
Mahadev, K., Zilbering, A., Zhu, L., & Goldstein, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100109200 · Cited by 509 · see citing works
Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495 · see citing works
Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1
Arnold, R. S., Shi, J., Murad, E., Whalen, A. M., Sun, C. Q., Polavarapu, R., Parthasarathy, S., Petros, J. A., & Lambeth, J. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101505898 · Cited by 486 · see citing works
Molecular imaging of hydrogen peroxide produced for cell signaling
Miller, E. W., Tulyathan, O., Isacoff, E. Y., & Chang, C. J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio871 · Cited by 450 · see citing works
Role for mitochondrial oxidants as regulators of cellular metabolism
Nemoto, S., Takeda, K., Yu, Z.-X., Ferrans, V. J., & Finkel, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7311-7318.2000 · Cited by 393 · see citing works
Controlled Elimination of Intracellular H 2 O2: Regulation of Peroxiredoxin, Catalase, and Glutathione Peroxidase via Post-translational Modification
Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works
Self-citation
Thiol-based redox switches in eukaryotic proteins
Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373 · see citing works
Reactive oxygen species and insulin resistance: the good, the bad and the ugly
Tiganis, T. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.11.006 · Cited by 256 · see citing works
Role of insulin-induced reactive oxygen species in the insulin signaling pathway
Goldstein, B. J., Mahadev, K., Wu, X., Zhu, L., & Motoshima, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1021 · Cited by 238 · see citing works
Oxidative Stress and Huntington’s Disease: The Good, the Bad, and the Ugly
Kumar, A., & Ratan, R. R. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160205 · Cited by 236 · see citing works
The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal
Forman, H. J., Fukuto, J. M., Miller, T., Zhang, H., Rinna, A., & Levy, S. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.06.011 · Cited by 226 · see citing works
Nox enzymes as novel targets for drug development
Lambeth, J. D., Krause, K.-H., & Clark, R. A. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0123-6 · Cited by 212 · see citing works
The strength of receptor signaling is centrally controlled through a cooperative loop between Ca2+ and an oxidant signal
Singh, D. K., Kumar, D., Siddiqui, Z., Basu, S. K., Kumar, V., & Rao, K. V. S. (2005) · Cell · doi:10.1016/j.cell.2005.02.036 · Cited by 206 · see citing works
Global proteomic assessment of the classical protein-tyrosine phosphatome and “Redoxome”
Karisch, R., Fernandez, M., Taylor, P., Virtanen, C., St-Germain, J. R., Jin, L. L., Harris, I. S., Mori, J., Mak, T. W., Senis, Y. A., et al. (2011) · Cell · doi:10.1016/j.cell.2011.07.020 · Cited by 179 · see citing works
Redox Regulation of cAMP-responsive Element-binding Protein and Induction of Manganous Superoxide Dismutase in Nerve Growth Factor-dependent Cell Survival
Bedogni, B., Pani, G., Colavitti, R., Riccio, A., Borrello, S., Murphy, M., Smith, R., Eboli, M. L., & Galeotti, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301089200 · Cited by 124 · see citing works
Activation of p53 by Oxidative Stress Involves Platelet-derived Growth Factor-β Receptor-mediated Ataxia Telangiectasia Mutated (ATM) Kinase Activation
Chen, K., Albano, A., Ho, A., & Keaney, J. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304423200 · Cited by 95 · see citing works
[29] Redox regulation of protein tyrosine phosphatases by hydrogen peroxide: Detecting sulfenic acid intermediates and examining reversible inactivation
Denu, J. M., & Tanner, K. G. (2002) · Methods in Enzymology · doi:10.1016/s0076-6879(02)48648-x · Cited by 50 · see citing works
The mitochondrial reactive oxygen species regulator p66Shc controls PDGF-induced signaling and migration through protein tyrosine phosphatase oxidation
Frijhoff, J., Dagnell, M., Augsten, M., Beltrami, E., Giorgio, M., & Östman, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.022 · Cited by 43 · see citing works

Consumption of EGF by A431 cells: evidence for receptor recycling.
Masui, H., Castro, L., & Mendelsohn, J. M. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.120.1.85 · Cited by 82 · see citing works
Epidermal growth factor induces terminal differentiation in human epidermoid carcinoma cells
Konger, R. L., & Chan, T. (1993) · Journal of Cellular Physiology · doi:10.1002/jcp.1041560310 · Cited by 15 · see citing works
Epidermal Growth Factor Decreases the Level of DNA Topoisomerase $II{\alpha}$ in Human Carcinoma A431 Cells
Chang, J. (1998) · BMB Reports
Epidermal growth factor inhibits growth of A431 human epidermoid carcinoma in serum-free cell culture.
Barnes, D. W. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.93.1.1 · Cited by 283 · see citing works
Growth stimulation of A431 cells by epidermal growth factor: identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody.
Kawamoto, T., Sato, J. D., Le, A., Polikoff, J., SATO, G. H., & Mendelsohn, J. M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.5.1337 · Cited by 791 · see citing works

Authors: Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G.
Affiliations: National Institutes of Health (US)
Corresponding author: Rhee, Sue Goo
ORCID: Kwon, Ki-Sun
Rhee, Sue Goo
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1998-06
Volume: 273
Issue: 25
Pages: 15366-15372
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.273.25.15366
OpenAlex: W2136573391
Cited by: 969
References: 53
Citations by year: 2026: 7 · 2025: 11 · 2024: 11 · 2023: 14 · 2022: 20 · 2021: 29 · 2020: 27 · 2019: 28 · 2018: 19 · 2017: 29 · 2016: 33 · 2015: 32 · 2014: 30 · 2013: 43 · 2012: 50
FWCI: 10.81
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8177 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: PTP1B, epidermal growth factor, hydrogen peroxide, reversible enzyme inactivation, sulfenic acid, thioredoxin, glutaredoxin, glutathione, iodoacetate, tyrosine phosphorylation, receptor tyrosine kinase, A431 cells, redox regulation
MeSH terms: Amino Acid Sequence, Cell Line, Cysteine, Epidermal Growth Factor, Humans, Hydrogen Peroxide, Kinetics, Molecular Sequence Data, Molecular Weight, Placenta, Recombinant Proteins, Tumor Cells, Cultured, Protein Tyrosine Phosphatases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks