메뉴 건너뛰기




Volumn 95, Issue , 2016, Pages 96-111

Redox regulation of epidermal growth factor receptor signaling during the development of pulmonary hypertension

Author keywords

Catalase; EGFR; Oxidative stress; Proliferation; Pulmonary hypertension

Indexed keywords

CATALASE; DIMER; DODECYL SULFATE SODIUM; EPIDERMAL GROWTH FACTOR RECEPTOR; GEFITINIB; LIGAND; MONOCROTALINE; MONOCROTALINE PYRROLE; PROTEIN KINASE P60; TYROSINE;

EID: 84962245418     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2016.02.029     Document Type: Article
Times cited : (29)

References (57)
  • 2
    • 84859644104 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species in pulmonary hypertension
    • D.M. Tabima, S. Frizzell, and M.T. Gladwin Reactive oxygen and nitrogen species in pulmonary hypertension Free Radic. Biol. Med. 52 2012 1970 1986
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1970-1986
    • Tabima, D.M.1    Frizzell, S.2    Gladwin, M.T.3
  • 3
    • 78449287448 scopus 로고    scopus 로고
    • Reactive oxygen species signaling in pulmonary vascular smooth muscle
    • F. Perez-Vizcaino, A. Cogolludo, and L. Moreno Reactive oxygen species signaling in pulmonary vascular smooth muscle Respir. Physiol. Neurobiol. 174 2010 212 220
    • (2010) Respir. Physiol. Neurobiol. , vol.174 , pp. 212-220
    • Perez-Vizcaino, F.1    Cogolludo, A.2    Moreno, L.3
  • 5
    • 84863479133 scopus 로고    scopus 로고
    • Xanthine oxidase inhibition for the treatment of cardiovascular disease: A systematic review and meta-analysis
    • P. Higgins, J. Dawson, K.R. Lees, K. McArthur, T.J. Quinn, and M.R. Walters Xanthine oxidase inhibition for the treatment of cardiovascular disease: a systematic review and meta-analysis Cardiovasc. Ther. 30 2012 217 226
    • (2012) Cardiovasc. Ther. , vol.30 , pp. 217-226
    • Higgins, P.1    Dawson, J.2    Lees, K.R.3    McArthur, K.4    Quinn, T.J.5    Walters, M.R.6
  • 6
    • 81055143945 scopus 로고    scopus 로고
    • ENOS uncoupling in pulmonary hypertension
    • L.V. d'Uscio eNOS uncoupling in pulmonary hypertension Cardiovasc. Res. 92 2011 359 360
    • (2011) Cardiovasc. Res. , vol.92 , pp. 359-360
    • D'Uscio, L.V.1
  • 7
    • 84861045926 scopus 로고    scopus 로고
    • Mitochondria: Redox metabolism and dysfunction
    • J. Kang, and S. Pervaiz Mitochondria: redox metabolism and dysfunction Biochem. Res. Int. 2012 896751
    • (2012) Biochem. Res. Int.
    • Kang, J.1    Pervaiz, S.2
  • 8
    • 79961193678 scopus 로고    scopus 로고
    • Superoxide dismutases: Role in redox signaling, vascular function, and diseases
    • T. Fukai, and M. Ushio-Fukai Superoxide dismutases: role in redox signaling, vascular function, and diseases Antioxid. Redox Signal. 15 2011 1583 1606
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 1583-1606
    • Fukai, T.1    Ushio-Fukai, M.2
  • 9
    • 84866320015 scopus 로고    scopus 로고
    • Effects of peroxisomal catalase inhibition on mitochondrial function
    • P.A. Walton, and M. Pizzitelli Effects of peroxisomal catalase inhibition on mitochondrial function Front. Physiol. 3 2012 108
    • (2012) Front. Physiol. , vol.3 , pp. 108
    • Walton, P.A.1    Pizzitelli, M.2
  • 10
    • 80052000670 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 in health and disease: From molecular mechanisms to therapeutic opportunities
    • E. Lubos, J. Loscalzo, and D.E. Handy Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities Antioxid. Redox Signal. 15 2011 1957 1997
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 1957-1997
    • Lubos, E.1    Loscalzo, J.2    Handy, D.E.3
  • 11
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • J. Lu, and A. Holmgren The thioredoxin antioxidant system Free Radic. Biol. Med. 66 2014 75 87
    • (2014) Free Radic. Biol. Med. , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2
  • 12
    • 40849135997 scopus 로고    scopus 로고
    • Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: Issues and considerations
    • E. Schroder, and P. Eaton Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: issues and considerations Curr. Opin. Pharmacol. 8 2008 153 159
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 153-159
    • Schroder, E.1    Eaton, P.2
  • 13
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • S.G. Rhee, Y.S. Bae, S.R. Lee, J. Kwon, Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci STKE 2000:pe1.
    • (2000) Sci STKE , pp. pe1
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 14
    • 33847660853 scopus 로고    scopus 로고
    • 2 in studies of signal transduction
    • 2 in studies of signal transduction Free Radic. Biol. Med. 42 2007 926 932
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 926-932
    • Forman, H.J.1
  • 15
    • 0037514194 scopus 로고    scopus 로고
    • Mechanisms of oxidative stress and vascular dysfunction
    • Z.S. Nedeljkovic, N. Gokce, and J. Loscalzo Mechanisms of oxidative stress and vascular dysfunction Postgrad. Med. J. 79 2003 195 198 (quiz pp. 198-200)
    • (2003) Postgrad. Med. J. , vol.79
    • Nedeljkovic, Z.S.1    Gokce, N.2    Loscalzo, J.3
  • 16
    • 0026515446 scopus 로고
    • Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression
    • G.N. Rao, and B.C. Berk Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression Circ. Res. 70 1992 593 599
    • (1992) Circ. Res. , vol.70 , pp. 593-599
    • Rao, G.N.1    Berk, B.C.2
  • 19
    • 2342492317 scopus 로고    scopus 로고
    • Review of epidermal growth factor receptor biology
    • R.S. Herbst Review of epidermal growth factor receptor biology Int. J. Radiat. Oncol. Biol. Phys. 59 2004 21 26
    • (2004) Int. J. Radiat. Oncol. Biol. Phys. , vol.59 , pp. 21-26
    • Herbst, R.S.1
  • 20
    • 84875943954 scopus 로고    scopus 로고
    • Enhanced depolarization-induced pulmonary vasoconstriction following chronic hypoxia requires EGFR-dependent activation of NAD(P)H oxidase 2
    • C.E. Norton, B.R. Broughton, N.L. Jernigan, B.R. Walker, and T.C. Resta Enhanced depolarization-induced pulmonary vasoconstriction following chronic hypoxia requires EGFR-dependent activation of NAD(P)H oxidase 2 Antioxid. Redox Signal. 18 2013 1777 1788
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1777-1788
    • Norton, C.E.1    Broughton, B.R.2    Jernigan, N.L.3    Walker, B.R.4    Resta, T.C.5
  • 22
    • 22544484537 scopus 로고    scopus 로고
    • Epidermal growth factor receptor blockade mediates smooth muscle cell apoptosis and improves survival in rats with pulmonary hypertension
    • S.L. Merklinger, P.L. Jones, E.C. Martinez, and M. Rabinovitch Epidermal growth factor receptor blockade mediates smooth muscle cell apoptosis and improves survival in rats with pulmonary hypertension Circulation 112 2005 423 431
    • (2005) Circulation , vol.112 , pp. 423-431
    • Merklinger, S.L.1    Jones, P.L.2    Martinez, E.C.3    Rabinovitch, M.4
  • 23
    • 77950335263 scopus 로고    scopus 로고
    • Hypoxia-induced proliferation of human pulmonary microvascular endothelial cells depends on epidermal growth factor receptor tyrosine kinase activation
    • I.T. Toby, L.G. Chicoine, H. Cui, B. Chen, and L.D. Nelin Hypoxia-induced proliferation of human pulmonary microvascular endothelial cells depends on epidermal growth factor receptor tyrosine kinase activation Am. J. Physiol. 298 2010 L600 L606
    • (2010) Am. J. Physiol. , vol.298 , pp. L600-L606
    • Toby, I.T.1    Chicoine, L.G.2    Cui, H.3    Chen, B.4    Nelin, L.D.5
  • 26
    • 1442299824 scopus 로고    scopus 로고
    • Molecular mechanisms of nitric oxide-induced growth arrest and apoptosis in fetal pulmonary arterial smooth muscle cells
    • S. Wedgwood, and S.M. Black Molecular mechanisms of nitric oxide-induced growth arrest and apoptosis in fetal pulmonary arterial smooth muscle cells Nitric Oxide 9 2003 201 210
    • (2003) Nitric Oxide , vol.9 , pp. 201-210
    • Wedgwood, S.1    Black, S.M.2
  • 27
    • 1942485280 scopus 로고    scopus 로고
    • Nitric oxide decreases endothelin-1 secretion through the activation of soluble guanylate cyclase
    • L.K. Kelly, S. Wedgwood, R.H. Steinhorn, and S.M. Black Nitric oxide decreases endothelin-1 secretion through the activation of soluble guanylate cyclase Am. J. Physiol. 286 2004 L984 L991
    • (2004) Am. J. Physiol. , vol.286 , pp. L984-L991
    • Kelly, L.K.1    Wedgwood, S.2    Steinhorn, R.H.3    Black, S.M.4
  • 28
    • 13644260463 scopus 로고    scopus 로고
    • Endothelin-1 decreases endothelial NOS expression and activity through ETA receptor-mediated generation of hydrogen peroxide
    • S. Wedgwood, and S.M. Black Endothelin-1 decreases endothelial NOS expression and activity through ETA receptor-mediated generation of hydrogen peroxide Am. J. Physiol. 288 2005 L480 L487
    • (2005) Am. J. Physiol. , vol.288 , pp. L480-L487
    • Wedgwood, S.1    Black, S.M.2
  • 29
    • 1442330336 scopus 로고    scopus 로고
    • S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity
    • K. Ravi, L.A. Brennan, S. Levic, P.A. Ross, and S.M. Black S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity Proc. Natl. Acad. Sci. USA 101 2004 2619 2624
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2619-2624
    • Ravi, K.1    Brennan, L.A.2    Levic, S.3    Ross, P.A.4    Black, S.M.5
  • 30
    • 73549099528 scopus 로고    scopus 로고
    • Shear stress stimulates nitric oxide signaling in pulmonary arterial endothelial cells via a reduction in catalase activity: Role of protein kinase C delta
    • S. Kumar, N. Sud, F.V. Fonseca, Y. Hou, and S.M. Black Shear stress stimulates nitric oxide signaling in pulmonary arterial endothelial cells via a reduction in catalase activity: role of protein kinase C delta Am. J. Physiol. 298 2010 L105 L116
    • (2010) Am. J. Physiol. , vol.298 , pp. L105-L116
    • Kumar, S.1    Sud, N.2    Fonseca, F.V.3    Hou, Y.4    Black, S.M.5
  • 32
    • 84928476077 scopus 로고    scopus 로고
    • New ways to boost molecular dynamics simulations
    • E. Krieger, and G. Vriend New ways to boost molecular dynamics simulations J. Comput. Chem. 36 2015 996 1007
    • (2015) J. Comput. Chem. , vol.36 , pp. 996-1007
    • Krieger, E.1    Vriend, G.2
  • 33
    • 0033601370 scopus 로고    scopus 로고
    • Pharmacological rescue of mutant p53 conformation and function
    • (New York, NY)
    • B.A. Foster, H.A. Coffey, M.J. Morin, and F. Rastinejad Pharmacological rescue of mutant p53 conformation and function Science (New York, NY) 286 1999 2507 2510
    • (1999) Science , vol.286 , pp. 2507-2510
    • Foster, B.A.1    Coffey, H.A.2    Morin, M.J.3    Rastinejad, F.4
  • 34
    • 0014428296 scopus 로고
    • Toxicity of pyrrolizidine alkaloids
    • A.R. Mattocks Toxicity of pyrrolizidine alkaloids Nature 217 1968 723 728
    • (1968) Nature , vol.217 , pp. 723-728
    • Mattocks, A.R.1
  • 35
    • 28444450886 scopus 로고    scopus 로고
    • Monocrotaline pyrrole targets proteins with and without cysteine residues in the cytosol and membranes of human pulmonary artery endothelial cells
    • M.W. Lame, A.D. Jones, D.W. Wilson, and H.J. Segall Monocrotaline pyrrole targets proteins with and without cysteine residues in the cytosol and membranes of human pulmonary artery endothelial cells Proteomics 5 2005 4398 4413
    • (2005) Proteomics , vol.5 , pp. 4398-4413
    • Lame, M.W.1    Jones, A.D.2    Wilson, D.W.3    Segall, H.J.4
  • 36
    • 0038236523 scopus 로고    scopus 로고
    • Structure-function study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression
    • M. Ueda, H. Kinoshita, S.I. Maeda, W. Zou, and A. Tanaka Structure-function study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression Appl. Microbiol. Biotechnol. 61 2003 488 494
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 488-494
    • Ueda, M.1    Kinoshita, H.2    Maeda, S.I.3    Zou, W.4    Tanaka, A.5
  • 37
    • 0033610890 scopus 로고    scopus 로고
    • Peroxynitrite induces covalent dimerization of epidermal growth factor receptors in A431 epidermoid carcinoma cells
    • A. van der Vliet, M. Hristova, C.E. Cross, J.P. Eiserich, and T. Goldkorn Peroxynitrite induces covalent dimerization of epidermal growth factor receptors in A431 epidermoid carcinoma cells J. Biol. Chem. 273 1998 31860 31866
    • (1998) J. Biol. Chem. , vol.273 , pp. 31860-31866
    • Van Der Vliet, A.1    Hristova, M.2    Cross, C.E.3    Eiserich, J.P.4    Goldkorn, T.5
  • 38
    • 0033573921 scopus 로고    scopus 로고
    • Mechanism of biological synergy between cellular Src and epidermal growth factor receptor
    • D.A. Tice, J.S. Biscardi, A.L. Nickles, and S.J. Parsons Mechanism of biological synergy between cellular Src and epidermal growth factor receptor Proc. Natl. Acad. Sci. USA 96 1999 1415 1420
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1415-1420
    • Tice, D.A.1    Biscardi, J.S.2    Nickles, A.L.3    Parsons, S.J.4
  • 39
    • 0345138451 scopus 로고    scopus 로고
    • Functional implication of the interaction between EGF receptor and c-Src
    • T.H. Leu, and M.C. Maa Functional implication of the interaction between EGF receptor and c-Src Front. Biosci. 8 2003 s28 s38
    • (2003) Front. Biosci. , vol.8 , pp. s28-s38
    • Leu, T.H.1    Maa, M.C.2
  • 41
    • 26444552166 scopus 로고    scopus 로고
    • PDGF signaling in pulmonary arterial hypertension
    • R.J. Barst PDGF signaling in pulmonary arterial hypertension J. Clin. Invest. 115 2005 2691 2694
    • (2005) J. Clin. Invest. , vol.115 , pp. 2691-2694
    • Barst, R.J.1
  • 42
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein-transactivated EGF receptor
    • H. Daub, C. Wallasch, A. Lankenau, A. Herrlich, and A. Ullrich Signal characteristics of G protein-transactivated EGF receptor EMBO J. 16 1997 7032 7044
    • (1997) EMBO J. , vol.16 , pp. 7032-7044
    • Daub, H.1    Wallasch, C.2    Lankenau, A.3    Herrlich, A.4    Ullrich, A.5
  • 43
    • 0030837027 scopus 로고    scopus 로고
    • The m1 muscarinic acetylcholine receptor transactivates the EGF receptor to modulate ion channel activity
    • W. Tsai, A.D. Morielli, and E.G. Peralta The m1 muscarinic acetylcholine receptor transactivates the EGF receptor to modulate ion channel activity EMBO J. 16 1997 4597 4605
    • (1997) EMBO J. , vol.16 , pp. 4597-4605
    • Tsai, W.1    Morielli, A.D.2    Peralta, E.G.3
  • 44
    • 40449095964 scopus 로고    scopus 로고
    • Epidermal growth factor receptor exposed to cigarette smoke is aberrantly activated and undergoes perinuclear trafficking
    • E.M. Khan, R. Lanir, A.R. Danielson, and T. Goldkorn Epidermal growth factor receptor exposed to cigarette smoke is aberrantly activated and undergoes perinuclear trafficking FASEB J. 22 2008 910 917
    • (2008) FASEB J. , vol.22 , pp. 910-917
    • Khan, E.M.1    Lanir, R.2    Danielson, A.R.3    Goldkorn, T.4
  • 45
    • 0029763774 scopus 로고    scopus 로고
    • Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases
    • G.N. Rao Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases Oncogene 13 1996 713 719
    • (1996) Oncogene , vol.13 , pp. 713-719
    • Rao, G.N.1
  • 46
    • 80051503287 scopus 로고    scopus 로고
    • EGF receptor exposed to oxidative stress acquires abnormal phosphorylation and aberrant activated conformation that impairs canonical dimerization
    • S. Filosto, E.M. Khan, E. Tognon, C. Becker, M. Ashfaq, T. Ravid, and T. Goldkorn EGF receptor exposed to oxidative stress acquires abnormal phosphorylation and aberrant activated conformation that impairs canonical dimerization PLoS One 6 2011 e23240
    • (2011) PLoS One , vol.6
    • Filosto, S.1    Khan, E.M.2    Tognon, E.3    Becker, C.4    Ashfaq, M.5    Ravid, T.6    Goldkorn, T.7
  • 47
    • 0033150608 scopus 로고    scopus 로고
    • Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite
    • L.A. MacMillan-Crow, and J.A. Thompson Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite Arch. Biochem. Biophys. 366 1999 82 88
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 82-88
    • MacMillan-Crow, L.A.1    Thompson, J.A.2
  • 49
    • 25844457433 scopus 로고    scopus 로고
    • The epidermal growth factor receptor family
    • L.A. Bazley, and W.J. Gullick The epidermal growth factor receptor family Endocr. Relat. Cancer 12 Suppl. 1 2005 S17 S27
    • (2005) Endocr. Relat. Cancer , vol.12 , pp. S17-S27
    • Bazley, L.A.1    Gullick, W.J.2
  • 50
    • 0025153862 scopus 로고
    • Chimeric alpha- and beta-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the alpha-PDGF receptor that determine PDGF-AA binding specificity
    • M.A. Heidaran, J.H. Pierce, R.A. Jensen, T. Matsui, and S.A. Aaronson Chimeric alpha- and beta-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the alpha-PDGF receptor that determine PDGF-AA binding specificity J. Biol. Chem. 265 1990 18741 18744
    • (1990) J. Biol. Chem. , vol.265 , pp. 18741-18744
    • Heidaran, M.A.1    Pierce, J.H.2    Jensen, R.A.3    Matsui, T.4    Aaronson, S.A.5
  • 52
    • 0020743112 scopus 로고
    • On the denaturation of porcine erythrocyte catalase with alkali, urea, and guanidine hydrochloride in relation to its subunit structure
    • A. Takeda, K. Hirano, Y. Shiroya, and T. Samejima On the denaturation of porcine erythrocyte catalase with alkali, urea, and guanidine hydrochloride in relation to its subunit structure J. Biochem. 93 1983 967 975
    • (1983) J. Biochem. , vol.93 , pp. 967-975
    • Takeda, A.1    Hirano, K.2    Shiroya, Y.3    Samejima, T.4
  • 53
    • 0032125902 scopus 로고    scopus 로고
    • Alkaline unfolding and salt-induced folding of bovine liver catalase at high pH
    • S. Prajapati, V. Bhakuni, K.R. Babu, and S.K. Jain Alkaline unfolding and salt-induced folding of bovine liver catalase at high pH Eur. J. Biochem./FEBS 255 1998 178 184
    • (1998) Eur. J. Biochem./FEBS , vol.255 , pp. 178-184
    • Prajapati, S.1    Bhakuni, V.2    Babu, K.R.3    Jain, S.K.4
  • 54
    • 0019557353 scopus 로고
    • On the acid denaturation of porcine erythrocyte catalase in relation to its subunit structure
    • T. Samejima, T. Miyahara, A. Takeda, A. Hachimori, and K. Hirano On the acid denaturation of porcine erythrocyte catalase in relation to its subunit structure J. Biochem. 89 1981 1325 1332
    • (1981) J. Biochem. , vol.89 , pp. 1325-1332
    • Samejima, T.1    Miyahara, T.2    Takeda, A.3    Hachimori, A.4    Hirano, K.5
  • 55
    • 0036878975 scopus 로고    scopus 로고
    • The overexpression catalase reduces NO-mediated inhibition of endothelial NO synthase
    • L.A. Brennan, S. Wedgwood, and S.M. Black The overexpression catalase reduces NO-mediated inhibition of endothelial NO synthase IUBMB life 54 2002 261 265
    • (2002) IUBMB Life , vol.54 , pp. 261-265
    • Brennan, L.A.1    Wedgwood, S.2    Black, S.M.3
  • 56
    • 73349096261 scopus 로고    scopus 로고
    • Resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer
    • P.S. Hammerman, P.A. Janne, and B.E. Johnson Resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer Clin. Cancer Res. 15 2009 7502 7509
    • (2009) Clin. Cancer Res. , vol.15 , pp. 7502-7509
    • Hammerman, P.S.1    Janne, P.A.2    Johnson, B.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.