Browse > Article

Src Redox Regulation: There Is More Than Meets the Eye  

Chiarugi, Paola (Department of Biochemical Sciences, University of Florence, and Centre for Research, Transfer and High Education 'Study at Molecular and Clinical Level of Chronic, Inflammatory, Degenerative and Neoplastic Disorders for the Development on Novel Therapies')
Abstract
Src-family kinases are critically involved in the control of cytoskeleton organization and in the generation of integrin-dependent signaling responses, inducing tyrosine phosphorylation of many signaling and cytoskeletal proteins. Activity of the Src family of tyrosine kinases is tightly controlled by inhibitory phosphorylation of a carboxy-terminal tyrosine residue, inducing an inactive conformation through binding with its SH2 domain. Dephosphorylation of C-ter tyrosine, as well as its deletion of substitution with phenylalanine in oncogenic Src kinases, leads to autophosphorylation at a tyrosine in the activation loop, thereby leading to enhanced Src activity. Beside this phophorylation/dephosphorylation circuitry, cysteine oxidation has been recently reported as a further mechanism of enzyme activation. Mounting evidence describes Src activation via its redox regulation as a key outcome in several circumstances, including growth factor and cytokines signaling, integrin-mediated cell adhesion and motility, membrane receptor cross-talk as well in cell transformation and tumor progression. Among the plethora of data involving Src kinase in physiological and pathophysiological processes, this review will give emphasis to the redox component of the regulation of this master kinase.
Keywords
cell adhesion; cell adhesion and growth factor signaling; hydrogen peroxide; oncogenic Src; Src;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
Times Cited By Web Of Science : 14  (Related Records In Web of Science)
연도 인용수 순위
1 Chen, Y.H., Pouyssegur, J., Courtneidge, S.A., and Obberghen- Schilling, E. (1994). Activation of Src family kinase activity by the G protein-coupled thrombin receptor in growth-responsive fibroblasts. J. Biol. Chem. 269, 27372-27377
2 Chiarugi, P. (2003). Reactive oxygen species as mediators of cell adhesion. Ital. J. Biochem. 52, 28-32
3 Cloutier, J.F., and Veillette, A. (1996). Association of inhibitory tyrosine protein kinase P50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells. EMBO J. 15, 4909-4918
4 Cohen, P. (2002). Protein kinases-the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1, 309-315   DOI   ScienceOn
5 Finkel, T. (1998). Oxygen radicals and signaling. Curr. Opin. Cell Biol. 10, 248-253   DOI   ScienceOn
6 Finkel, T. (2006). Intracellular redox regulation by the family of small GTPases. Antioxid Redox Signal. 8, 1857-1863   DOI   ScienceOn
7 Frame, M.C. (2002). Src in cancer: Deregulation and consequences for cell behaviour. Biochim. Biophys. Acta 1602, 114- 130
8 Haklar, G., Sayin-Ozveri, E., Yuksel, M., Aktan, A.O., and Yalcin, A.S. (2001). Different kinds of reactive oxygen and nitrogen species were detected in colon and breast tumors. Cancer Lett. 165, 219-224   DOI   ScienceOn
9 Hermiston, M.L., Xu, Z., and Weiss, A. (2003). CD45: a critical regulator of signaling thresholds in immune cells. Annu. Rev. Immunol. 21, 107-137   DOI   ScienceOn
10 Hunter, T., and Sefton, B.M. (1980). Transforming gene product of Rous Sarcoma virus phosphorylates tyrosine. Proc. Natl. Acad. Sci. USA 77, 1311-1315
11 Lambeth, J.D., Kawahara, T., and Diebold, B. (2007). Regulation of Nox and Duox enzymatic activity and expression. Free Radic. Biol. Med. 43, 319-331   DOI   ScienceOn
12 Luttrell, L.M., Hawes, B.E., van Biesen, T., Luttrell, D.K., Lansing, T.J., and Lefkowitz, R.J. (1996). Role of C-Src tyrosine kinase in G protein-coupled receptor- and Gbetagamma subunitmediated activation of mitogen-activated protein kinases. J. Biol. Chem. 271, 19443-19450   DOI   ScienceOn
13 Meredith, J.E. Jr., Fazeli, B., and Schwartz, M.A. (1993). The extracellular matrix as a cell survival factor. Mol. Biol. Cell 4, 953- 961   DOI
14 Okada, M., Nada, S., Yamanashi, Y., Yamamoto, T., and Nakagawa, H. (1991). CSK: a protein-tyrosine kinase involved in regulation of Src family kinases. J. Biol. Chem. 266, 24249-24252
15 Rhee, S.G., Kang, S.W., Jeong, W., Chang, T.S., Yang, K.S., and Woo, H.A. (2005). Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17, 183-189   DOI   ScienceOn
16 Senga, T., Miyazaki, K., Machida, K., Iwata, H., Matsuda, S., Nakashima, I., and Hamaguchi, M. (2000). Clustered cysteine residues in the kinase domain of V-Src: critical role for protein stability, cell transformation and sensitivity to herbimycin A. Oncogene 19, 273-279   DOI
17 Slomiany, B.L., and Slomiany, A. (2004). Src-kinase-dependent epidermal growth factor receptor transactivation in salivary mucin secretion in response to beta-adrenergic G-proteincoupled receptor activation. Inflammopharmacology 12, 233- 245   DOI   ScienceOn
18 Smart, J.E., Oppermann, H., Czernilofsky, A.P., Purchio, A.F., Erikson, R.L., and Bishop, J.M. (1981). Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous Sarcoma virus (Pp60v-Src) and its normal cellular homologue (Pp60c-Src). Proc. Natl. Acad. Sci. USA 78, 6013-6017
19 van Vliet, C., Bukczynska, P.E., Puryer, M.A., Sadek, C.M., Shields, B.J., Tremblay, M.L., and Tiganis, T. (2005). Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase. Nat. Immunol. 6, 253-260   DOI   ScienceOn
20 Wei, L., Yang, Y., Zhang, X., and Yu, Q. (2004). Altered regulation of Src upon cell detachment protects human lung adenocarcinoma cells from Anoikis. Oncogene 23, 9052-9061   DOI   ScienceOn
21 Moro, L., Dolce, L., Cabodi, S., Bergatto, E., Boeri, E.E., Smeriglio, M., Turco, E., Retta, S.F., Giuffrida, M.G., Venturino, M., et al. (2002). Integrin-induced epidermal growth factor (EGF) receptor activation requires C-Src and P130Cas and leads to phosphorylation of specific EGF receptor tyrosines. J. Biol. Chem. 277, 9405-9414   DOI   ScienceOn
22 Ghose, R., Shekhtman, A., Goger, M.J., Ji, H., and Cowburn, D. (2001). A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Nat. Struct. Biol. 8, 998-1004   DOI   ScienceOn
23 Loza-Coll, M.A., Perera, S., Shi, W., and Filmus, J. (2005). A transient increase in the activity of Src-family kinases induced by cell detachment delays Anoikis of intestinal epithelial cells. Oncogene 24, 1727-1737   DOI   ScienceOn
24 Marikovsky, M., Breuing, K., Liu, P.Y., Eriksson, E., Higashiyama, S., Farber, P., Abraham, J., and Klagsbrun, M. (1993). Appearance of Heparin-binding EGF-like growth factor in wound fluid as a response to injury. Proc. Natl. Acad. Sci. USA 90, 3889-3893
25 Frisch, S.M., and Francis, H. (1994). Disruption of epithelial cellmatrix interactions induces Apoptosis. J. Cell Biol. 124, 619-626   DOI
26 Block, K., Eid, A., Griendling, K.K., Lee, D.Y., Wittrant, Y., and Gorin, Y. (2008). Nox4 NAD(P)H oxidase mediates Src-dependent tyrosine phosphorylation of PDK-1 in response to angiotensin II. role in mesangial cell hypertrophy and fibronectin expression. J. Biol. Chem. 283, 24061-24076   DOI   ScienceOn
27 Schafer, B., Gschwind, A., and Ullrich, A. (2004). Multiple G-proteincoupled Receptor signals converge on the epidermal growth factor receptor to promote migration and invasion. Oncogene 23, 991-999   DOI   ScienceOn
28 Waters, C.M., Connell, M.C., Pyne, S., and Pyne, N.J. (2005). CSrc is involved in regulating signal transmission from PDGFbeta receptor-GPCR(s) complexes in mammalian cells. Cell Signal 17, 263-277   DOI   ScienceOn
29 Chiarugi, P., and Fiaschi, T. (2007). Redox signalling in anchoragedependent cell growth. Cell Signal. 19, 672-682   DOI   ScienceOn
30 Ferraro, D., Corso, S., Fasano, E., Panieri, E., Santangelo, R., Borrello, S., Giordano, S., Pani, G., and Galeotti, T. (2006). Prometastatic signaling by C-Met through RAC-1 and reactive oxygen species (ROS). Oncogene 25, 3689-3698   DOI   ScienceOn
31 Giannoni, E., Buricchi, F., Raugei, G., Ramponi, G., and Chiarugi, P. (2005). Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth. Mol. Cell. Biol. 25, 6391-6403   DOI   ScienceOn
32 Leu, T.H., Su, S.L., Chuang, Y.C., and Maa, M.C. (2003). Direct inhibitory effect of curcumin on Src and focal adhesion kinase activity. Biochem. Pharmacol. 66, 2323-2331   DOI   ScienceOn
33 Saito, S., Frank, G.D., Mifune, M., Ohba, M., Utsunomiya, H., Motley, E.D., Inagami, T., and Eguchi, S. (2002). Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase C-delta and C-Src. J. Biol. Chem. 277, 44695-44700   DOI   ScienceOn
34 Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609   DOI   ScienceOn
35 Moro, L., Venturino, M., Bozzo, C., Silengo, L., Altruda, F., Beguinot, L., Tarone, G., and Defilippi, P. (1998). Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion- dependent cell survival. EMBO J. 17, 6622-6632   DOI   ScienceOn
36 Chiarugi, P. (2005). PTPs versus PTKs: the redox side of the coin. Free Radic. Res. 39, 353-364   DOI   ScienceOn
37 Koch, C.A., Anderson, D., Moran, M.F., Ellis, C., and Pawson, T. (1991). SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252, 668-674   DOI
38 Le Gall, M., Chambard, J.C., Breittmayer, J.P., Grall, D., Pouyssegur, J., and Obberghen-Schilling, E. (2000). The P42/ P44 MAP kinase pathway prevents apoptosis induced by anchorage and serum removal. Mol. Biol. Cell 11, 1103-1112   DOI
39 Rytomaa, M., Lehmann, K., and Downward, J. (2000). Matrix detachment induces caspase-dependent cytochrome c release from mitochondria: inhibition by PKB/Akt but not Raf signalling. Oncogene 19, 4461-4468   DOI
40 Duchene, J., Schanstra, J.P., Pecher, C., Pizard, A., Susini, C., Esteve, J.P., Bascands, J.L., and Girolami, J.P. (2002), A novel protein-protein interaction between a G protein-coupled receptor and the phosphatase SHP-2 is involved in bradykinin-induced inhibition of cell proliferation. J. Biol. Chem. 277, 40375-40383   DOI   ScienceOn
41 Luttrell, D.K., and Luttrell, L.M. (2004), Not so strange bedfellows: G-protein-coupled receptors and Src family kinases. Oncogene 23, 7969-7978   DOI   ScienceOn
42 Shin, E.A., Kim, K.H., Han, S.I., Ha, K.S., Kim, J.H., Kang, K.I., Kim, H.D., and Kang, H.S. (1999). Arachidonic acid induces the activation of the stress-activated protein kinase, membrane ruffling and H2O2 production via a small GTPase Rac1. FEBS Lett. 452, 355-359   DOI   ScienceOn
43 Assoian, R.K. (1997). Control of the G1 phase cyclin-dependent kinases by mitogenic growth factors and the extracellular matrix. Cytokine Growth Factor Rev. 8, 165-170   DOI   ScienceOn
44 Chiarugi, P., and Buricchi, F. (2007). Protein tyrosine phosphorylation and reversible oxidation: Two cross-talking posttranslation modifications. Antioxid Redox Signal. 9 1-24   DOI   ScienceOn
45 Minetti, M., Mallozzi, C., and Di Stasi, A.M. (2002). Peroxynitrite activates kinases of the Src family and upregulates tyrosine phosphorylation signaling. Free Radic. Biol. Med. 33, 744-754   DOI   ScienceOn
46 Payne, S.L., Fogelgren, B., Hess, A.R., Seftor, E.A., Wiley, E.L., Fong, S.F., Csiszar, K., Hendrix, M.J., and Kirschmann, D.A. (2005). Lysyl oxidase regulates breast cancer cell migration and adhesion through a hydrogen peroxide-mediated mechanism. Cancer Res. 65, 11429-11436   DOI   ScienceOn
47 Gonfloni, S., Williams, J.C., Hattula, K., Weijland, A., Wierenga, R.K., and Superti-Furga, G. (1997). The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16, 7261-7271   DOI   ScienceOn
48 Gupta, A., Rosenberger, S.F., and Bowden, G.T. (1999). Increased ROS levels contribute to elevated transcription factor and MAP kinase activities in malignantly progressed mouse keratinocyte cell lines. Carcinogenesis 20, 2063-2073   DOI   ScienceOn
49 Daulhac, L., Kowalski-Chauvel, A., Pradayrol, L., Vaysse, N., and Seva, C. (1999). Src-family tyrosine kinases in activation of ERK-1 and P85/P110-phosphatidylinositol 3-kinase by G/CCKB receptors. J. Biol. Chem. 274, 20657-20663   DOI
50 Montezano, A.C., Callera, G.E., Yogi, A., He, Y., Tostes, R.C., He, G., Schiffrin, E.L., and Touyz, R.M. (2008). Aldosterone and angiotensin II synergistically stimulate migration in vascular smooth muscle cells through C-Src-regulated redox-sensitive RhoA pathways. Arterioscler Thromb Vasc. Biol. 25, 1511-1518
51 Bell, E.L., and Chandel, N.S. (2007). Mitochondrial oxygen sensing: regulation of hypoxia-inducible factor by mitochondrial generated reactive oxygen species. Essays Biochem. 43, 17-27   DOI   ScienceOn
52 Hurley, T.R., Hyman, R., and Sefton, B.M. (1993). Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the Lck, Fyn, and C-Src tyrosine protein kinases. Mol. Cell. Biol. 13,
53 Rhee, S.G. (1999). Redox signaling: Hydrogen peroxide as intracellular messenger. Exp. Mol. Med. 31, 53-59   DOI   ScienceOn
54 Sun, G., Ramdas, L., Wang, W., Vinci, J., McMurray, J., and Budde, R.J. (2002). Effect of autophosphorylation on the catalytic and regulatory properties of protein tyrosine kinase Src. Arch. Biochem. Biophys. 397, 11-17   DOI   ScienceOn
55 Fan, C., Li, Q., Ross, D., and Engelhardt, J.F. (2003). Tyrosine phosphorylation of I Kappa B Alpha activates NF Kappa B through a redox-regulated and C-Src-dependent mechanism following hypoxia/reoxygenation. J. Biol. Chem. 278, 2072-2080   DOI   ScienceOn
56 Chiarugi, P., and Cirri, P. (2003). Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction. Trends Biochem. Sci. 28, 509-514   DOI   ScienceOn
57 Kodama, H., Fukuda, K., Takahashi, E., Tahara, S., Tomita, Y., Ieda, M., Kimura, K., Owada, K.M., Vuori, K., and Ogawa, S. (2003). Selective involvement of P130Cas/Crk/Pyk2/c-Src in endothelin-1-induced JNK activation. Hypertension 41, 1372-1379   DOI   ScienceOn
58 Baker, M., Gamble, J., Tooze, R., Higgins, D., Yang, F.T., O'Brien, P.C., Coleman, N., Pingel, S., Turner, M., and Alexander, D.R. (2000). Development of T-Leukaemias in CD45 tyrosine phosphatase- deficient mutant Lck mice. EMBO J. 19, 4644-4654   DOI   ScienceOn
59 Bickers, D.R., and Athar, M. (2006). Oxidative stress in the pathogenesis of skin disease. J. Invest Dermatol. 126, 2565-2575   DOI   ScienceOn
60 Chiarugi, P. (2008). From anchorage dependent proliferation to survival: Lessons from redox signalling. IUBMB Life 60, 301-307   DOI   ScienceOn
61 Irby, R.B., Mao, W., Coppola, D., Kang, J., Loubeau, J.M., Trudeau, W., Karl, R., Fujita, D.J., Jove, R., and Yeatman, T.J. (1999). Activating SRC mutation in a subset of advanced human colon cancers. Nat. Genet. 21, 187-190   DOI   ScienceOn
62 ten Freyhaus, H., Huntgeburth, M., Wingler, K., Schnitker, J., Baumer, A.T., Vantler, M., Bekhite, M.M., Wartenberg, M., Sauer, H., and Rosenkranz, S. (2006). Novel Nox inhibitor VAS2870 attenuates PDGF-Dependent smooth muscle cell chemotaxis, but Not proliferation. Cardiovasc Res. 71, 331-341   DOI   ScienceOn
63 Laczko, R., Szauter, K.M., Jansen, M.K., Hollosi, P., Muranyi, M., Molnar, J., Fong, K.S., Hinek, A., and Csiszar, K. (2007). Active Lysyl oxidase (LOX) correlates with focal adhesion kinase (FAK)/paxillin activation and migration in invasive astrocytes. Neuropathol. Appl. Neurobiol. 33, 631-643   DOI   ScienceOn
64 Resh, M.D. (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16   DOI   ScienceOn
65 Lluis, J.M., Buricchi, F., Chiarugi, P., Morales, A., and Fernandez- Checa, J.C. (2007). Dual role of mitochondrial reactive oxygen species in hypoxia signaling: Activation of nuclear factor- {Kappa}B Via C-SRC and oxidant-dependent cell death. Cancer Res. 67, 7368-7377   DOI   ScienceOn
66 Taddei, M.L., Parri, M., Mello, T., Catalano, A., Levine, A.D., Raugei, G., Ramponi, G., and Chiarugi, P. (2007). Integrin-mediated cell adhesion and spreading engage different sources of reactive oxygen species. Antioxid Redox Signal 9, 469-481   DOI   ScienceOn
67 Ushio-Fukai, M., Griendling, K.K., Becker, P.L., Hilenski, L., Halleran, S., and Alexander, R.W. (2001). Epidermal growth factor receptor transactivation by angiotensin II requires reactive oxygen species in vascular smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 21, 489-495   DOI   ScienceOn
68 Akhand, A.A., Pu, M., Senga, T., Kato, M., Suzuki, H., Miyata, T., Hamaguchi, M., and Nakashima, I. (1999). Nitric oxide controls Src kinase activity through a sulfhydryl group modificationmediated Tyr-527-independent and Tyr-416-linked mechanism. J. Biol. Chem. 274, 25821-25826   DOI
69 Catarzi, S., Giannoni, E., Favilli, F., Meacci, E., Iantomasi, T., and Vincenzini, M.T. (2007). Sphingosine 1-phosphate stimulation of NADPH oxidase activity: Relationship with platelet-derived growth factor receptor and C-Src kinase. Biochim. Biophys. Acta 1770, 872-883   DOI   ScienceOn
70 Sabe, H., Hamaguchi, M., and Hanafusa, H. (1997). Cell to substratum adhesion is involved in V-Src-induced cellular protein tyrosine phosphorylation: Implication for the adhesion-regulated protein tyrosine phosphatase activity. Oncogene 14, 1779-1788   DOI
71 Redondo, P.C., Salido, G.M., Pariente, J.A., and Rosado, J.A. (2004). Dual effect of hydrogen peroxide on store-mediated calcium entry in human platelets. Biochem. Pharmacol. 67, 1065- 1076
72 Ayrapetov, M.K., Wang, Y.H., Lin, X., Gu, X., Parang, K., and Sun, G. (2006). Conformational basis for SH2-Tyr(P)527 binding in src inactivation. J. Biol. Chem. 281, 23776-23784   DOI   ScienceOn
73 Gianni, D., Bohl, B., Courtneidge, S.A., and Bokoch, G.M. (2008). The involvement of the tyrosine kinase C-Src in the regulation of reactive oxygen species generation mediated by NADPH oxidase- 1. Mol. Biol. Cell 19, 2984-2994   DOI   ScienceOn
74 Radisky, D.C., Levy, D.D., Littlepage, L.E., Liu, H., Nelson, C.M., Fata, J.E., Leake, D., Godden, E.L., Albertson, D.G., Nieto, M.A., et al. (2005). Rac1b and reactive oxygen species mediate MMP- 3-induced EMT and genomic instability. Nature 436, 123-127   DOI   ScienceOn
75 Xu, W., Harrison, S.C., and Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase C-Src. Nature 385, 595-602   DOI   ScienceOn
76 Rosado, J.A., Redondo, P.C., Salido, G.M, Gomez-Arteta, E., Sage, S.O., and Pariente, J.A. (2004). Hydrogen peroxide generation induces Pp60src activation in human platelets: evidence for the involvement of this pathway in store-mediated calcium entry. J. Biol. Chem. 279, 1665-1675   DOI   ScienceOn
77 Giannoni, E., Buricchi, F., Grimaldi, G., Parri, M., Cialdai, F., Taddei, M.L., Raugei, G., Ramponi, G., and Chiarugi, P. (2008). Redox regulation of Anoikis: Reactive oxygen species as essential mediators of cell survival. Cell Death Differ. 15, 867-878   DOI   ScienceOn
78 Nakamura, K., Hori, T., Sato, N., Sugie, K., Kawakami, T., and Yodoi, J. (1993). Redox regulation of a Src family protein tyrosine kinase P56lck in T cells. Oncogene 8, 3133-3139
79 Parsons, S.J., and Parsons, J.T. (2004), Src family kinases, key regulators of signal transduction. Oncogene 23, 7906-7909   DOI   ScienceOn
80 Frame, M.C., Fincham, V.J., Carragher, N.O., and Wyke, J.A. (2002). V-Src's hold over actin and cell adhesions. Nat. Rev. Mol. Cell. Biol. 3, 233-245   DOI   ScienceOn
81 Trouba, K.J., Hamadeh, H.K., Amin, R.P., and Germolec, D.R. (2002). Oxidative stress and its role in skin disease. Antioxid Redox Signal 4, 665-673   DOI   ScienceOn
82 Kagan, H.M., and Li, W. (2003). Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell. J. Cell Biochem. 88, 660-672   DOI   ScienceOn
83 Klimova, T., and Chandel, N.S. (2008). Mitochondrial complex III regulates hypoxic activation of HIF. Cell Death Differ. 15, 660- 666   DOI   ScienceOn
84 Paige, L.A., Nadler, M.J., Harrison, M.L., Cassady, J.M., and Geahlen, R.L. (1993). Reversible palmitoylation of the proteintyrosine kinase P56lck. J. Biol. Chem. 268, 8669-8674
85 von Wichert, G., Jiang, G., Kostic, A., De Vos, K., Sap, J., and Sheetz, M.P. (2003). RPTP-Alpha acts as a transducer of mechanical force on Alphav/Beta3-integrin-cytoskeleton linkages. J. Cell Biol. 161, 143-153   DOI   ScienceOn
86 Cook, P.W., Pittelkow, M.R., Keeble, W.W., Graves-Deal, R., Coffey, R.J. Jr., and Shipley, G.D. (1992). Amphiregulin messenger RNA is elevated in psoriatic epidermis and gastrointestinal carcinomas. Cancer Res. 52, 3224-3227
87 Li, A.E., Ito, H., Rovira, I.I., Kim, K.S., Takeda, K., Yu, Z.Y., Ferrans, V.J., and Finkel, T. (1999). A role for reactive oxygen species in endothelial cell Anoikis. Circ. Res. 85, 304-310   DOI   ScienceOn
88 Szatrowski, T.P., and Nathan, C.F. (1991). Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51, 794-798
89 Catarzi, S., Biagioni, C., Giannoni, E., Favilli, F., Marcucci, T., Iantomasi, T., and Vincenzini, M.T. (2005). Redox regulation of platelet-derived-growth-factor-receptor: Role of NADPH-oxidase and C-Src tyrosine kinase. Biochim. Biophys. Acta 1745, 166- 175   DOI   ScienceOn
90 Gilmore, A.P. (2005). Anoikis. Cell Death Differ. 15, 1473-1477
91 Hamaguchi, M., Yamagata, S., Thant, A.A., Xiao, H., Iwata, H., Mazaki, T., and Hanafusa, H. (1995). Augmentation of metalloproteinase (Gelatinase) activity secreted from Rous Sarcoma virus- infected cells correlates with transforming activity of Src. Oncogene 10, 1037-1043
92 Kato, M., Iwashita, T., Takeda, K., Akhand, A.A., Liu, W., Yoshihara, M., Asai, N., Suzuki, H., Takahashi, M., and Nakashima, I. (2000). Ultraviolet light induces redox reaction-mediated dimerization and superactivation of oncogenic Ret tyrosine kinases. Mol. Biol. Cell 11, 93-101   DOI
93 Su, J., Muranjan, M., and Sap, J. (1999). Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin- mediated responses in fibroblasts. Curr. Biol. 9, 505-511   DOI   ScienceOn
94 Sun, G., Sharma, A.K., and Budde, R.J. (1998). Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation. Oncogene 17, 1587-1595   DOI
95 Benhar, M., Engelberg, D., and Levitzki, A. (2002). ROS, stressactivated kinases and stress signaling in cancer. EMBO Rep. 3, 420-425   DOI   ScienceOn
96 Boggon, T.J., and Eck, M.J. (2004). Structure and regulation of Src family kinases. Oncogene 23, 7918-7927   DOI   ScienceOn
97 Cooper, J.A., and Howell, B. (1993). The when and how of Src regulation. Cell 73, 1051-1054
98 Kodama, H., Fukuda, K., Takahashi, T., Sano, M., Kato, T., Tahara, S., Hakuno, D., Sato, T., Manabe, T., Konishi, F., et al. (2002). Role of EGF receptor and Pyk2 in endothelin-1-induced ERK activation in Rat cardiomyocytes. J. Mol. Cell Cardiol. 34, 139- 150   DOI   ScienceOn