메뉴 건너뛰기




Volumn 71, Issue , 2014, Pages 49-60

Endosomal H2O2 production leads to localized cysteine sulfenic acid formation on proteins during lysophosphatidic acid-mediated cell signaling

Author keywords

Cysteine modifications; Lipid mediators; LPA signaling; Proliferative signaling; Protein oxidation

Indexed keywords

CYSTEINE; CYSTEINE SULFENIC ACID; HYDROGEN PEROXIDE; LYSOPHOSPHATIDIC ACID; PROTEIN; PROTEIN KINASE B; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG; 3-(2,6-DIMETHYL-4-CARBAMOYLPHENYL)PROPANOIC ACID; AKT2 PROTEIN, HUMAN; BENZAMIDE DERIVATIVE; CYSTEINESULFENIC ACID; EARLY ENDOSOME ANTIGEN 1; LYSOPHOSPHATIDIC ACID RECEPTOR; LYSOPHOSPHOLIPID; PHENYLPROPIONIC ACID DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE 1B; PTPN1 PROTEIN, HUMAN; SULFENIC ACID DERIVATIVE; VESICULAR TRANSPORT PROTEIN;

EID: 84898402832     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.03.017     Document Type: Article
Times cited : (38)

References (59)
  • 1
    • 3042523481 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates ovarian cancer cell migration via a Ras-MEK kinase 1 pathway
    • DOI 10.1158/0008-5472.CAN-04-0060
    • D. Bian, S. Su, C. Mahanivong, R.K. Cheng, Q. Han, Z.K. Pan, P. Sun, and S. Huang Lysophosphatidic acid stimulates ovarian cancer cell migration via a Ras-MEK kinase 1 pathway Cancer Res. 64 2004 4209 4217 (Pubitemid 38802425)
    • (2004) Cancer Research , vol.64 , Issue.12 , pp. 4209-4217
    • Bian, D.1    Su, S.2    Mahanivong, C.3    Cheng, R.K.4    Han, Q.5    Pan, Z.K.6    Sun, P.7    Huang, S.8
  • 3
    • 0037031878 scopus 로고    scopus 로고
    • Role for 18:1 Lysophosphatidic acid as an autocrine mediator in prostate cancer cells
    • DOI 10.1074/jbc.M203864200
    • Y. Xie, T.C. Gibbs, Y.V. Mukhin, and K.E. Meier Role for 18:1 lysophosphatidic acid as an autocrine mediator in prostate cancer cells J. Biol. Chem. 277 2002 32516 32526 (Pubitemid 34984755)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32516-32526
    • Xie, Y.1    Gibbs, T.C.2    Mukhin, Y.V.3    Meier, K.E.4
  • 6
    • 4544357634 scopus 로고    scopus 로고
    • Lysophosphatidic acid promotes survival of androgen-insensitive prostate cancer PC3 cells via activation of NF-κB
    • DOI 10.1002/pros.20083
    • G.V. Raj, J.A. Sekula, R. Guo, J.F. Madden, and Y. Daaka Lysophosphatidic acid promotes survival of androgen-insensitive prostate cancer PC3 cells via activation of NF-kappaB Prostate 61 2004 105 113 (Pubitemid 39244697)
    • (2004) Prostate , vol.61 , Issue.2 , pp. 105-113
    • Raj, G.V.1    Sekula, J.A.2    Guo, R.3    Madden, J.F.4    Daaka, Y.5
  • 7
    • 78650178412 scopus 로고    scopus 로고
    • Reactive oxygen species mediate lysophosphatidic acid induced signaling in ovarian cancer cells
    • J.A. Saunders, L.C. Rogers, C. Klomsiri, L.B. Poole, and L.W. Daniel Reactive oxygen species mediate lysophosphatidic acid induced signaling in ovarian cancer cells Free Radic. Biol. Med. 49 2010 2058 2067
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 2058-2067
    • Saunders, J.A.1    Rogers, L.C.2    Klomsiri, C.3    Poole, L.B.4    Daniel, L.W.5
  • 8
    • 70449769732 scopus 로고    scopus 로고
    • ATX-LPA receptor axis in inflammation and cancer
    • S. Liu, M. Murph, N. Panupinthu, and G.B. Mills ATX-LPA receptor axis in inflammation and cancer Cell Cycle 8 2009 3695 3701
    • (2009) Cell Cycle , vol.8 , pp. 3695-3701
    • Liu, S.1    Murph, M.2    Panupinthu, N.3    Mills, G.B.4
  • 10
    • 80053027028 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates the proliferation of ovarian cancer cells via the gep proto-oncogene Galpha(12)
    • Z.G. Goldsmith, J.H. Ha, M. Jayaraman, and D.N. Dhanasekaran Lysophosphatidic acid stimulates the proliferation of ovarian cancer cells via the gep proto-oncogene Galpha(12) Genes Cancer 2 2011 563 575
    • (2011) Genes Cancer , vol.2 , pp. 563-575
    • Goldsmith, Z.G.1    Ha, J.H.2    Jayaraman, M.3    Dhanasekaran, D.N.4
  • 11
    • 69449095279 scopus 로고    scopus 로고
    • Signal transduction responses to lysophosphatidic acid and sphingosine 1-phosphate in human prostate cancer cells
    • T.C. Gibbs, M.V. Rubio, Z. Zhang, Y. Xie, K.R. Kipp, and K.E. Meier Signal transduction responses to lysophosphatidic acid and sphingosine 1-phosphate in human prostate cancer cells Prostate 69 2009 1493 1506
    • (2009) Prostate , vol.69 , pp. 1493-1506
    • Gibbs, T.C.1    Rubio, M.V.2    Zhang, Z.3    Xie, Y.4    Kipp, K.R.5    Meier, K.E.6
  • 13
    • 85104535450 scopus 로고    scopus 로고
    • Imaging of intracellular hydrogen peroxide production with HyPer upon stimulation of HeLa cells with epidermal growth factor
    • K.N. Markvicheva, E.A. Bogdanova, D.B. Staroverov, S. Lukyanov, and V.V. Belousov Imaging of intracellular hydrogen peroxide production with HyPer upon stimulation of HeLa cells with epidermal growth factor Methods Mol. Biol. 476 2009 76 83
    • (2009) Methods Mol. Biol. , vol.476 , pp. 76-83
    • Markvicheva, K.N.1    Bogdanova, E.A.2    Staroverov, D.B.3    Lukyanov, S.4    Belousov, V.V.5
  • 15
    • 0028806450 scopus 로고
    • Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway
    • Q. Chen, N. Olashaw, and J. Wu Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway J. Biol. Chem. 270 1995 28499 28502
    • (1995) J. Biol. Chem. , vol.270 , pp. 28499-28502
    • Chen, Q.1    Olashaw, N.2    Wu, J.3
  • 16
    • 33846276947 scopus 로고    scopus 로고
    • Pitavastatin inhibits lysophosphatidic acid-induced proliferation and monocyte chemoattractant protein-1 expression in aortic smooth muscle cells by suppressing Rac-1-mediated reactive oxygen species generation
    • DOI 10.1016/j.vph.2006.11.002, PII S1537189106006483
    • U. Kaneyuki, S. Ueda, S. Yamagishi, S. Kato, T. Fujimura, R. Shibata, A. Hayashida, J. Yoshimura, M. Kojiro, K. Oshima, and S. Okuda Pitavastatin inhibits lysophosphatidic acid-induced proliferation and monocyte chemoattractant protein-1 expression in aortic smooth muscle cells by suppressing Rac-1-mediated reactive oxygen species generation Vasc. Pharmacol. 46 2007 286 292 (Pubitemid 46124092)
    • (2007) Vascular Pharmacology , vol.46 , Issue.4 , pp. 286-292
    • Kaneyuki, U.1    Ueda, S.2    Yamagishi, S.-i.3    Kato, S.4    Fujimura, T.5    Shibata, R.6    Hayashida, A.7    Yoshimura, J.8    Kojiro, M.9    Oshima, K.10    Okuda, S.11
  • 17
    • 65349113056 scopus 로고    scopus 로고
    • Signaling components of redox active endosomes: The redoxosomes
    • F.D. Oakley, D. Abbott, Q. Li, and J. Engelhardt Signaling components of redox active endosomes: the redoxosomes Antioxid. Redox Signal. 11 2009 1313 1333
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1313-1333
    • Oakley, F.D.1    Abbott, D.2    Li, Q.3    Engelhardt, J.4
  • 20
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • DOI 10.1126/science.1130481
    • 2, a necessary evil for cell signaling Science 312 2006 1882 1883 (Pubitemid 43993698)
    • (2006) Science , vol.312 , Issue.5782 , pp. 1882-1883
    • Rhee, S.G.1
  • 21
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signaling-mediated cysteine oxidation
    • L.B. Poole, and K.J. Nelson Discovering mechanisms of signaling-mediated cysteine oxidation Curr. Opin. Chem. Biol. 12 2008 18 24
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 18-24
    • Poole, L.B.1    Nelson, K.J.2
  • 22
    • 84893738731 scopus 로고    scopus 로고
    • Chemical approaches to detect and analyze protein sulfenic acids
    • C.M. Furdui, and L.B. Poole Chemical approaches to detect and analyze protein sulfenic acids Mass Spectrom. Rev. 33 2014 126 146
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 126-146
    • Furdui, C.M.1    Poole, L.B.2
  • 23
    • 84880105471 scopus 로고    scopus 로고
    • Cysteine-mediated redox signaling: Chemistry, biology, and tools for discovery
    • C.E. Paulsen, and K.S. Carroll Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Chem. Rev. 113 2013 4633 4679
    • (2013) Chem. Rev. , vol.113 , pp. 4633-4679
    • Paulsen, C.E.1    Carroll, K.S.2
  • 24
    • 79958059617 scopus 로고    scopus 로고
    • Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins
    • A. Hall, K. Nelson, L.B. Poole, and P.A. Karplus Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins Antioxid. Redox Signal. 15 2011 795 815
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 795-815
    • Hall, A.1    Nelson, K.2    Poole, L.B.3    Karplus, P.A.4
  • 25
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • DOI 10.1038/nchembio.85, PII NCHEMBIO85
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286 (Pubitemid 351550893)
    • (2008) Nature Chemical Biology , vol.4 , Issue.5 , pp. 278-286
    • Winterbourn, C.C.1
  • 26
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • N.J. Adimora, D.P. Jones, and M.L. Kemp A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses Antioxid. Redox Signal. 13 2010 731 743
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 731-743
    • Adimora, N.J.1    Jones, D.P.2    Kemp, M.L.3
  • 28
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • S.E. Leonard, K.G. Reddie, and K.S. Carroll Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells ACS Chem. Biol. 4 2009 783 799
    • (2009) ACS Chem. Biol. , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 30
    • 77954072854 scopus 로고    scopus 로고
    • Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids
    • D.S. Rehder, and C.R. Borges Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids BMC Biochem. 11 2010 25
    • (2010) BMC Biochem. , vol.11 , pp. 25
    • Rehder, D.S.1    Borges, C.R.2
  • 33
    • 34248525914 scopus 로고    scopus 로고
    • Quantitative fluorescence microscopy and image deconvolution
    • J.R. Swedlow Quantitative fluorescence microscopy and image deconvolution Methods Cell Biol. 81 2007 447 465
    • (2007) Methods Cell Biol. , vol.81 , pp. 447-465
    • Swedlow, J.R.1
  • 34
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • DOI 10.1111/j.1365-2818.2006.01706.x
    • S. Bolte, and F.P. Cordelieres A guided tour into subcellular colocalization analysis in light microscopy J. Microsc. 224 2006 213 232 (Pubitemid 46010930)
    • (2006) Journal of Microscopy , vol.224 , Issue.3 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 35
    • 0027163023 scopus 로고
    • Signalling properties of lysophosphatidic acid
    • DOI 10.1016/0165-6147(93)90021-B
    • M.E. Durieux, and K.R. Lynch Signalling properties of lysophosphatidic acid Trends Pharmacol. Sci 14 1993 249 254 (Pubitemid 23172511)
    • (1993) Trends in Pharmacological Sciences , vol.14 , Issue.6 , pp. 249-254
    • Durieux, M.E.1    Lynch, K.R.2
  • 36
    • 0034654394 scopus 로고    scopus 로고
    • Involvement of lipoxygenase in lysophosphatidic acid-stimulated hydrogen peroxide release in human HaCaT keratinocytes
    • DOI 10.1042/0264-6021:3460751
    • M. Sekharam, J.M. Cunnick, and J. Wu Involvement of lipoxygenase in lysophosphatidic acid-stimulated hydrogen peroxide release in human HaCaT keratinocytes Biochem. J. 346 Pt 3 2000 751 758 (Pubitemid 30171037)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 751-758
    • Sekharam, M.1    Cunnick, J.M.2    Wu, J.3
  • 39
    • 29244461715 scopus 로고    scopus 로고
    • 1 lysophosphatidic acid receptors
    • DOI 10.1242/jcs.02634
    • N.M. Urs, K.T. Jones, P.D. Salo, J.E. Severin, J. Trejo, and H. Radhakrishna A requirement for membrane cholesterol in the beta-arrestin- and clathrin-dependent endocytosis of LPA1 lysophosphatidic acid receptors J. Cell Sci. 118 2005 5291 5304 (Pubitemid 41819591)
    • (2005) Journal of Cell Science , vol.118 , Issue.22 , pp. 5291-5304
    • Urs, N.M.1    Jones, K.T.2    Salo, P.D.3    Severin, J.E.4    Trejo, J.5    Radhakrishna, H.6
  • 40
    • 0035966064 scopus 로고    scopus 로고
    • A single amino acid determines lysophospholipid specificity of the S1P1 (EDG1) and LPA1 (EDG2) phospholipid growth factor receptors
    • D.A. Wang, Z. Lorincz, D.L. Bautista, K. Liliom, G. Tigyi, and A.L. Parrill A single amino acid determines lysophospholipid specificity of the S1P1 (EDG1) and LPA1 (EDG2) phospholipid growth factor receptors J. Biol. Chem. 276 2001 49213 49220
    • (2001) J. Biol. Chem. , vol.276 , pp. 49213-49220
    • Wang, D.A.1    Lorincz, Z.2    Bautista, D.L.3    Liliom, K.4    Tigyi, G.5    Parrill, A.L.6
  • 41
    • 50249090428 scopus 로고    scopus 로고
    • Sharpening the edges of understanding the structure/function of the LPA1 receptor: Expression in cancer and mechanisms of regulation
    • M.M. Murph, G.H. Nguyen, H. Radhakrishna, and G.B. Mills Sharpening the edges of understanding the structure/function of the LPA1 receptor: expression in cancer and mechanisms of regulation Biochim. Biophys. Acta 1781 2008 547 557
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 547-557
    • Murph, M.M.1    Nguyen, G.H.2    Radhakrishna, H.3    Mills, G.B.4
  • 42
    • 47749151450 scopus 로고    scopus 로고
    • Biological roles for the NOX family NADPH oxidases
    • W.M. Nauseef Biological roles for the NOX family NADPH oxidases J. Biol. Chem. 283 2008 16961 16965
    • (2008) J. Biol. Chem. , vol.283 , pp. 16961-16965
    • Nauseef, W.M.1
  • 47
    • 64349117191 scopus 로고    scopus 로고
    • Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines
    • C.Y. Chen, D. Willard, and J. Rudolph Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines Biochemistry 48 2009 1399 1409
    • (2009) Biochemistry , vol.48 , pp. 1399-1409
    • Chen, C.Y.1    Willard, D.2    Rudolph, J.3
  • 48
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • DOI 10.1038/nature01680
    • A. Salmeen, J.N. Andersen, M.P. Myers, T.C. Meng, J.A. Hinks, N.K. Tonks, and D. Barford Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate Nature 423 2003 769 773 (Pubitemid 36735701)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.-C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 49
    • 0034607968 scopus 로고    scopus 로고
    • Requirement of SHP2 binding to Grb2-associated binder-1 for mitogen- activated protein kinase activation in response to lysophosphatidic acid and epidermal growth factor
    • DOI 10.1074/jbc.275.18.13842
    • J.M. Cunnick, J.F. Dorsey, T. Munoz-Antonia, L. Mei, and J. Wu Requirement of SHP2 binding to Grb2-associated binder-1 for mitogen-activated protein kinase activation in response to lysophosphatidic acid and epidermal growth factor J. Biol. Chem. 275 2000 13842 13848 (Pubitemid 30257458)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13842-13848
    • Cunnick, J.M.1    Dorsey, J.F.2    Munoz-Antonia, T.3    Mei, L.4    Wu, J.5
  • 50
    • 84865072624 scopus 로고    scopus 로고
    • Lysophosphatidic acid modulates the association of PTP1B with N-cadherin/catenin complex in SKOV3 ovarian cancer cells
    • R.Y. Huang, C.C. Wen, C.K. Liao, S.H. Wang, L.Y. Chou, and J.C. Wu Lysophosphatidic acid modulates the association of PTP1B with N-cadherin/catenin complex in SKOV3 ovarian cancer cells Cell Biol. Int. 36 2012 833 841
    • (2012) Cell Biol. Int. , vol.36 , pp. 833-841
    • Huang, R.Y.1    Wen, C.C.2    Liao, C.K.3    Wang, S.H.4    Chou, L.Y.5    Wu, J.C.6
  • 54
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • DOI 10.1126/science.1080405
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653 (Pubitemid 36520591)
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 55
    • 84864778316 scopus 로고    scopus 로고
    • The reversible formation of cysteine sulfenic acid promotes B-cell activation and proliferation
    • K.E. Crump, D.G. Juneau, L.B. Poole, K.M. Haas, and J.M. Grayson The reversible formation of cysteine sulfenic acid promotes B-cell activation and proliferation Eur. J. Immunol. 42 2012 2152 2164
    • (2012) Eur. J. Immunol. , vol.42 , pp. 2152-2164
    • Crump, K.E.1    Juneau, D.G.2    Poole, L.B.3    Haas, K.M.4    Grayson, J.M.5
  • 56
    • 80053458043 scopus 로고    scopus 로고
    • Oxidation of Akt2 kinase promotes cell migration and regulates G1-S transition in the cell cycle
    • R. Wani, N.S. Bharathi, J. Field, A.W. Tsang, and C.M. Furdui Oxidation of Akt2 kinase promotes cell migration and regulates G1-S transition in the cell cycle Cell Cycle 10 2011 3263 3268
    • (2011) Cell Cycle , vol.10 , pp. 3263-3268
    • Wani, R.1    Bharathi, N.S.2    Field, J.3    Tsang, A.W.4    Furdui, C.M.5
  • 57
    • 65349157681 scopus 로고    scopus 로고
    • Compartmentalization of redox signaling through NADPH oxidase-derived ROS
    • M. Ushio-Fukai Compartmentalization of redox signaling through NADPH oxidase-derived ROS Antioxid. Redox Signal. 11 2009 1289 1299
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1289-1299
    • Ushio-Fukai, M.1
  • 58
    • 84855372404 scopus 로고    scopus 로고
    • Dissection of aberrant GPCR signaling in tumorigenesis - A systems biology approach
    • J. Wu, N. Xie, X. Zhao, E.C. Nice, and C. Huang Dissection of aberrant GPCR signaling in tumorigenesis - a systems biology approach Cancer Genomics Proteomics 9 2012 37 50
    • (2012) Cancer Genomics Proteomics , vol.9 , pp. 37-50
    • Wu, J.1    Xie, N.2    Zhao, X.3    Nice, E.C.4    Huang, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.