Abstract
Through a variety of rapidly recruited intracellular mediators steroid receptors enact quick changes in the function of cells in different settings. Emerging evidence indicates that the interaction with the extracellular environment and cell movement are regulated by sex steroids through such rapid mechanisms. Exposure of different cell types to estrogen, progesterone or other steroids results in swift changes in the morphology of the cells, primarily because of changes in the position and organization of actin fibers. These changes are coupled with the formation of a variety of specialized cell membrane structures that are necessary for the cell interaction with high-molecular weight extracellular proteins or nearby cells, and thus to move around or to cross-talk with neighbor cells. Prominent actions on horizontal cell movement or on the ability to invade matrices have also been observed during exposure to estrogen or other steroids, which indicate that these steroids are powerful regulators of cell movement. Many of these actions are enacted via the rapid activation on extra-nuclear signaling cascades of sex steroid receptors that lead to the recruitment of small GTPases such as RhoA or Rac, which therefore drive the changes in actin positioning. These actions of sex steroids appear to be fundamental for migration and invasion in endocrine-sensitive breast cancer cells, and may therefore have relevance for local progression and metastasis. The characterization of these rapid actions of estrogens and other steroids will help to understand the effects of these hormones in the setting of breast cancer metastasis, and may eventually lead to new therapeutic strategies.
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References
Henderson BE, Feigelson HS (2000) Hormonal carcinogenesis. Carcinogenesis 21:427–433
Alam SM, Rajendran M, Ouyang S, Veeramani S, Zhang L, Lin MF (2009) A novel role of Shc adaptor proteins in steroid hormone-regulated cancers. Endocr Relat Cancer 16:1–16
Kelsey JL, Gammon MD, John EM (1993) Reproductive factors and breast cancer. Epidemiol Rev 15:36–47
Verkooijen HM, Bouchardy C, Vinh-Hung V, Rapiti E, Hartman M (2009) The incidence of breast cancer and changes in the use of hormone replacement therapy: a review of the evidence. Maturitas 64:80–85
Russo J, Russo IH (2006) The role of estrogen in the initiation of breast cancer. J Steroid Biochem Mol Biol 102:89–96
Braun S, Auer D, Marth C (2009) The prognostic impact of bone marrow micrometastases in women with breast cancer. Cancer Invest 27:598–603
Fu XD, Giretti MS, Baldacci C, Garibaldi S, Flamini M, Sanchez AM, Gadducci A, Genazzani AR, Simoncini T (2008) Extra-nuclear signaling of progesterone receptor to breast cancer cell movement and invasion through the actin cytoskeleton. PLoS One 3:e2790
Janni W, Hepp P (2010) Adjuvant aromatase inhibitor therapy: outcomes and safety. Cancer Treat Rev 36:249–261
Collaborative Group on Hormonal Factors in Breast Cancer (1997) Breast cancer and hormone replacement therapy: collaborative reanalysis of data from 51 epidemiological studies of 52,705 women with breast cancer and 108,411 women without breast cancer. Lancet 350:1047–1059
DiSaia PJ (1996) Hormone replacement therapy in the gynecologic and breast cancer patient. Cancer Control 3:101–106
Fuqua SA (2001) The role of estrogen receptor in breast cancer metastasis. J Mammary Gland Biol Neoplasia 6:407–417
Poole AJ, Li Y, Kim Y, Lin SC, Lee WH, Lee EY (2006) Prevention of Brca1-mediated mammary tumorigenesis in mice by a progesterone antagonist. Science 314:1467–1470
Vanzulli SI, Soldati R, Meiss R, Colombo L, Molinolo AA, Lanari C (2005) Estrogen or antiprogestin treatment induces complete regression of pulmonary and axillary metastases in an experimental model of breast cancer progression. Carcinogenesis 26:1055–1063
Kato S, Pinto M, Carvajal A, Espinoza N, Monso C, Sadarangani A, Villalon M, Brosens JJ, White JO, Richer JK, Horwitz KB, Owen GI (2005) Progesterone increases tissue factor gene expression, procoagulant activity, and invasion in the breast cancer cell line ZR-75–1. J Clin Endocrinol Metab 90:1181–1188
Hyder SM, Chiappetta C, Stancel GM (2001) Pharmacological and endogenous progestins induce vascular endothelial growth factor expression in human breast cancer cells. Int J Cancer 92:469–473
Zhang Y, Ma B, Fan Q (2010) Mechanisms of breast cancer bone metastasis. Cancer Lett 292:1–7
Berridge MJ, Bootman MD, Lipp P (1998) Calcium–a life and death signal. Nature 395:645–648
Cutini P, Selles J, Massheimer V (2009) Cross-talk between rapid and long term effects of progesterone on vascular tissue. J Steroid Biochem Mol Biol 115:36–43
Rauschemberger MB, Selles J, Massheimer V (2008) The direct action of estrone on vascular tissue involves genomic and non-genomic action. Life Sci 82:115–123
Migliaccio A, Castoria G, Di Domenico M, de Falco A, Bilancio A, Lombardi M, Barone MV, Ametrano D, Zannini MS, Abbondanza C, Auricchio F (2000) Steroid-induced androgen receptor-oestradiol receptor beta-Src complex triggers prostate cancer cell proliferation. EMBO J 19:5406–5417
Kousteni S, Bellido T, Plotkin LI, O’Brien CA, Bodenner DL, Han L, Han K, DiGregorio GB, Katzenellenbogen JA, Katzenellenbogen BS, Roberson PK, Weinstein RS, Jilka RL, Manolagas SC (2001) Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity. Cell 104:719–730
Unni E, Sun S, Nan B, McPhaul MJ, Cheskis B, Mancini MA, Marcelli M (2004) Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence. Cancer Res 64:7156–7168
Ray P, Ghosh SK, Zhang DH, Ray A (1997) Repression of interleukin-6 gene expression by 17 beta-estradiol: inhibition of the DNA-binding activity of the transcription factors NF-IL6 and NF-kappa B by the estrogen receptor. FEBS Lett 409:79–85
Jakacka M, Ito M, Weiss J, Chien PY, Gehm BD, Jameson JL (2001) Estrogen receptor binding to DNA is not required for its activity through the nonclassical AP1 pathway. J Biol Chem 276:13615–13621
Safe S (2001) Transcriptional activation of genes by 17 beta-estradiol through estrogen receptor-Sp1 interactions. Vitam Horm 62:231–252
Fortunati N (1999) Sex hormone-binding globulin: not only a transport protein. What news is around the corner? J Endocrinol Invest 22:223–234
Rosner W, Hryb DJ, Khan MS, Nakhla AM, Romas NA (1999) Androgen and estrogen signaling at the cell membrane via G-proteins and cyclic adenosine monophosphate. Steroids 64:100–106
Fortunati N, Fissore F, Fazzari A, Becchis M, Comba A, Catalano MG, Berta L, Frairia R (1996) Sex steroid binding protein exerts a negative control on estradiol action in MCF-7 cells (human breast cancer) through cyclic adenosine 3’, 5’-monophosphate and protein kinase A. Endocrinology 137:686–692
Nakhla AM, Romas NA, Rosner W (1997) Estradiol activates the prostate androgen receptor and prostate-specific antigen secretion through the intermediacy of sex hormone-binding globulin. J Biol Chem 272:6838–6841
Armen TA, Gay CV (2000) Simultaneous detection and functional response of testosterone and estradiol receptors in osteoblast plasma membranes. J Cell Biochem 79:620–627
Kampa M, Papakonstanti EA, Hatzoglou A, Stathopoulos EN, Stournaras C, Castanas E (2002) The human prostate cancer cell line LNCaP bears functional membrane testosterone receptors that increase PSA secretion and modify actin cytoskeleton. FASEB J 16:1429–1431
Kim HP, Lee JY, Jeong JK, Bae SW, Lee HK, Jo I (1999) Nongenomic stimulation of nitric oxide release by estrogen is mediated by estrogen receptor alpha localized in caveolae. Biochem Biophys Res Commun 263:257–262
Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP (2001) Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation. J Biol Chem 276:13442–13451
Lu Q, Pallas DC, Surks HK, Baur WE, Mendelsohn ME, Karas RH (2004) Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha. Proc Natl Acad Sci U S A 101:17126–17131
Song RX, Zhang Z, Santen RJ (2005) Estrogen rapid action via protein complex formation involving ERalpha and Src. Trends Endocrinol Metab 16:347–353
Lieberherr M, Grosse B (1994) Androgens increase intracellular calcium concentration and inositol 1, 4, 5-trisphosphate and diacylglycerol formation via a pertussis toxin-sensitive G-protein. J Biol Chem 269:7217–7223
Benten WP, Lieberherr M, Giese G, Wunderlich F (1998) Estradiol binding to cell surface raises cytosolic free calcium in T cells. FEBS Lett 422:349–353
Kelly MJ, Lagrange AH, Wagner EJ, Ronnekleiv OK (1999) Rapid effects of estrogen to modulate G protein-coupled receptors via activation of protein kinase A and protein kinase C pathways. Steroids 64:64–75
Estrada M, Espinosa A, Muller M, Jaimovich E (2003) Testosterone stimulates intracellular calcium release and mitogen-activated protein kinases via a G protein-coupled receptor in skeletal muscle cells. Endocrinology 144:3586–3597
Pierce KL, Premont RT, Lefkowitz RJ (2002) Seven-transmembrane receptors. Nat Rev Mol Cell Biol 3:639–650
Prossnitz ER, Arterburn JB, Smith HO, Oprea TI, Sklar LA, Hathaway HJ (2008) Estrogen signaling through the transmembrane G protein-coupled receptor GPR30. Annu Rev Physiol 70:165–190
Prossnitz ER, Arterburn JB, Sklar LA (2007) GPR30: A G protein-coupled receptor for estrogen. Mol Cell Endocrinol 265–266:138–142
Luttrell LM, Hawes BE, van Biesen T, Luttrell DK, Lansing TJ, Lefkowitz RJ (1996) Role of c-Src tyrosine kinase in G protein-coupled receptor- and Gbetagamma subunit-mediated activation of mitogen-activated protein kinases. J Biol Chem 271:19443–19450
Levin ER (2005) Integration of the extranuclear and nuclear actions of estrogen. Mol Endocrinol 19:1951–1959
Hammes SR, Levin ER (2007) Extranuclear steroid receptors: nature and actions. Endocr Rev 28:726–741
Meng TC, Lee MS, Lin MF (2000) Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells. Oncogene 19:2664–2677
Meyer G, Feldman EL (2002) Signaling mechanisms that regulate actin-based motility processes in the nervous system. J Neurochem 83:490–503
Kedrin D, van Rheenen J, Hernandez L, Condeelis J, Segall JE (2007) Cell motility and cytoskeletal regulation in invasion and metastasis. J Mammary Gland Biol Neoplasia 12:143–152
Yamazaki D, Kurisu S, Takenawa T (2005) Regulation of cancer cell motility through actin reorganization. Cancer Sci 96:379–386
Giretti MS, Simoncini T (2008) Rapid regulatory actions of sex steroids on cell movement through the actin cytoskeleton. Steroids 73:895–900
Giretti MS, Fu XD, De Rosa G, Sarotto I, Baldacci C, Garibaldi S, Mannella P, Biglia N, Sismondi P, Genazzani AR, Simoncini T (2008) Extra-nuclear signalling of estrogen receptor to breast cancer cytoskeletal remodelling, migration and invasion. PLoS One 3:e2238
Fu XD, Giretti MS, Goglia L, Flamini MI, Sanchez AM, Baldacci C, Garibaldi S, Sitruk-Ware R, Genazzani AR, Simoncini T (2008) Comparative actions of progesterone, medroxyprogesterone acetate, drospirenone and nestorone on breast cancer cell migration and invasion. BMC Cancer 8:166
Louvet-Vallee S (2000) ERM proteins: from cellular architecture to cell signaling. Biol Cell 92:305–316
Tsukita S, Yonemura S (1999) Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J Biol Chem 274:34507–34510
Sarrio D, Rodriguez-Pinilla SM, Dotor A, Calero F, Hardisson D, Palacios J (2006) Abnormal ezrin localization is associated with clinicopathological features in invasive breast carcinomas. Breast Cancer Res Treat 98:71–79
McGowan EM, Weinberger RP, Graham JD, Hill HD, Hughes JA, O’Neill GM, Clarke CL (2003) Cytoskeletal responsiveness to progestins is dependent on progesterone receptor A levels. J Mol Endocrinol 31:241–253
Ridley AJ, Allen WE, Peppelenbosch M, Jones GE (1999) Rho family proteins and cell migration. Biochem Soc Symp 65:111–123
Jiang P, Enomoto A, Takahashi M (2009) Cell biology of the movement of breast cancer cells: intracellular signalling and the actin cytoskeleton. Cancer Lett 284:122–130
Lu Q, Longo FM, Zhou H, Massa SM, Chen YH (2009) Signaling through Rho GTPase pathway as viable drug target. Curr Med Chem 16:1355–1365
Azios NG, Krishnamoorthy L, Harris M, Cubano LA, Cammer M, Dharmawardhane SF (2007) Estrogen and resveratrol regulate Rac and Cdc42 signaling to the actin cytoskeleton of metastatic breast cancer cells. Neoplasia 9:147–158
Chakravarty D, Nair SS, Santhamma B, Nair BC, Wang L, Bandyopadhyay A, Agyin JK, Brann D, Sun LZ, Yeh IT, Lee FY, Tekmal RR, Kumar R, Vadlamudi (2010) RK Extranuclear functions of ER impact invasive migration and metastasis by breast cancer cells. Cancer Res 70:4092–4101
Vadlamudi RK, Kumar R (2007) Functional and biological properties of the nuclear receptor coregulator PELP1/MNAR. Nucl Recept Signal 5:e004
Cheskis BJ, Greger J, Cooch N, McNally C, McLarney S, Lam HS, Rutledge S, Mekonnen B, Hauze D, Nagpal S, Freedman LP (2008) MNAR plays an important role in ERa activation of Src/MAPK and PI3K/Akt signaling pathways. Steroids 73:901–905
Nair SS, Mishra SK, Yang Z, Balasenthil S, Kumar R, Vadlamudi RK (2004) Potential role of a novel transcriptional coactivator PELP1 in histone H1 displacement in cancer cells. Cancer Res 64:6416–6423
Romer LH, Birukov KG, Garcia JG (2006) Focal adhesions: paradigm for a signaling nexus. Circ Res 98:606–616
van Nimwegen MJ, van de Water B (2007) Focal adhesion kinase: a potential target in cancer therapy. Biochem Pharmacol 73:597–609
Lark AL, Livasy CA, Dressler L, Moore DT, Millikan RC, Geradts J, Iacocca M, Cowan D, Little D, Craven RJ, Cance W (2005) High focal adhesion kinase expression in invasive breast carcinomas is associated with an aggressive phenotype. Mod Pathol 18:1289–1294
Luo M, Guan JL (2010) Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis. Cancer Lett 289:127–139
Fong YC, Liu SC, Huang CY, Li TM, Hsu SF, Kao ST, Tsai FJ, Chen WC, Chen CY, Tang CH (2009) Osteopontin increases lung cancer cells migration via activation of the alphavbeta3 integrin/FAK/Akt and NF-kappaB-dependent pathway. Lung Cancer 64:263–270
Hu XW, Meng D, Fang J (2008) Apigenin inhibited migration and invasion of human ovarian cancer A2780 cells through focal adhesion kinase. Carcinogenesis 29:2369–2376
Kaneda T, Sonoda Y, Ando K, Suzuki T, Sasaki Y, Oshio T, Tago M, Kasahara T (2008) Mutation of Y925F in focal adhesion kinase (FAK) suppresses melanoma cell proliferation and metastasis. Cancer Lett 270:354–361
van Nimwegen MJ, Verkoeijen S, van Buren L, Burg D, van de Water B (2005) Requirement for focal adhesion kinase in the early phase of mammary adenocarcinoma lung metastasis formation. Cancer Res 65:4698–4706
Luo M, Fan H, Nagy T, Wei H, Wang C, Liu S, Wicha MS, Guan JL (2009) Mammary epithelial-specific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells. Cancer Res 69:466–474
Pylayeva Y, Gillen KM, Gerald W, Beggs HE, Reichardt LF, Giancotti FG (2009) Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling. J Clin Invest 119:252–266
Lin VC, Ng EH, Aw SE, Tan MG, Bay BH (2000) ProgesteroneProgesterone induces focal adhesion in breast cancer cells MDA-MB-231 transfected with progesterone receptor complementary DNA. Mol Endocrinol 14:348–358
Lin VC, Woon CT, Aw SE, Guo C (2003) Distinct molecular pathways mediate progesterone-induced growth inhibition and focal adhesion. Endocrinology 144:5650–5657
Fu XD, Goglia L, Sanchez AM, Flamini M, Giretti MS, Tosi V, Genazzani AR, Simoncini T (2010) Progesterone receptor enhances breast cancer cell motility and invasion via extranuclear activation of focal adhesion kinase. Endocr Relat Cancer 17:431–443
Azios NG, Dharmawardhane SF (2005) Resveratrol and estradiol exert disparate effects on cell migration, cell surface actin structures, and focal adhesion assembly in MDA-MB-231 human breast cancer cells. Neoplasia 7:128–140
Kublickiene K, Fu XD, Svedas E, Landgren BM, Genazzani AR, Simoncini T (2008) Effects in postmenopausal women of estradiol and medroxyprogesterone alone and combined on resistance artery function and endothelial morphology and movement. J Clin Endocrinol Metab 93:1874–1883
Ishida H, Wada K, Masuda T, Okura M, Kohama K, Sano Y, Nakajima A, Kogo M, Kamisaki Y (2007) Critical role of estrogen receptor on anoikis and invasion of squamous cell carcinoma. Cancer Sci 98:636–643
Bartholomew PJ, Vinci JM, DePasquale JA (1998) Decreased tyrosine phosphorylation of focal adhesion kinase after estradiol treatment of MCF-7 human breast carcinoma cells. J Steroid Biochem Mol Biol 67:241–249
Sanchez AM, Flamini MI, Baldacci C, Goglia L, Genazzani AR, Simoncini T (2010) Estrogen receptor-{alpha} promotes breast cancer cell motility and invasion via focal adhesion kinase and N-WASP. Mol Endocrinol 24:2114–2125
Matsumoto K, Nakamura T, Kramer RH (1994) Hepatocyte growth factor/scatter factor induces tyrosine phosphorylation of focal adhesion kinase (p125FAK) and promotes migration and invasion by oral squamous cell carcinoma cells. J Biol Chem 269:31807–31813
Hsia DA, Mitra SK, Hauck CR, Streblow DN, Nelson JA, Ilic D, Huang S, Li E, Nemerow GR, Leng J, Spencer KS, Cheresh DA, Schlaepfer DD (2003) Differential regulation of cell motility and invasion by FAK. J Cell Biol 160:753–767
Reiske HR, Kao SC, Cary LA, Guan JL, Lai JF, Chen HC (1999) Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration. J Biol Chem 274:12361–12366
Thamilselvan V, Craig DH, Basson MD (2007) FAK association with multiple signal proteins mediates pressure-induced colon cancer cell adhesion via a Src-dependent PI3K/Akt pathway. FASEB J 21:1730–1741
Bailly M, Macaluso F, Cammer M, Chan A, Segall JE, Condeelis JS (1999) Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation. J Cell Biol 145:331–345
Higgs HN, Blanchoin L, Pollard TD (1999) Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry 38:15212–15222
Mullins RD, Heuser JA, Pollard TD (1998) The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc Natl Acad Sci U S A 95:6181–6186
Takenawa T, Suetsugu S (2007) The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat Rev Mol Cell Biol 8:37–48
Wu X, Suetsugu S, Cooper LA, Takenawa T, Guan JL (2004) Focal adhesion kinase regulation of N-WASP subcellular localization and function. J Biol Chem 279:9565–9576
Mitra SK, Hanson DA, Schlaepfer DD (2005) Focal adhesion kinase: in command and control of cell motility. Nat Rev Mol Cell Biol 6:56–68
Flynn JF, Wong C, Wu JM (2009) Anti-EGFR therapy: mechanism and advances in clinical efficacy in breast cancer. J Oncol 2009:526963
Sabe H, Hashimoto S, Morishige M, Ogawa E, Hashimoto A, Nam JM, Miura K, Yano H, Onodera Y (2009) The EGFR-GEP100-Arf6-AMAP1 signaling pathway specific to breast cancer invasion and metastasis. Traffic 10:982–993
Kedrin D, Wyckoff J, Boimel PJ, Coniglio SJ, Hynes NE, Arteaga CL, Segall JE (2009) ERBB1 and ERBB2 have distinct functions in tumor cell invasion and intravasation. Clin Cancer Res 15:3733–3739
Cristofanilli M, Valero V, Mangalik A, Royce M, Rabinowitz I, Arena FP, Kroener JF, Curcio E, Watkins C, Bacus S, Cora EM, Anderson E, Magill PJ (2010) Phase II, randomized trial to compare anastrozole combined with gefitinib or placebo in postmenopausal women with hormone receptor-positive metastatic breast cancer. Clin Cancer Res 16:1904–1914
Filardo EJ, Quinn JA, Sabo E (2008) Association of the membrane estrogen receptor, GPR30, with breast tumor metastasis and transactivation of the epidermal growth factor receptor. Steroids 73:870–873
Fitzgibbons PL, Page DL, Weaver D, Thor AD, Allred DC, Clark GM, Ruby SG, O’Malley F, Simpson JF, Connolly JL, Hayes DF, Edge SB, Lichter A, Schnitt SJ (2000) Prognostic factors in breast cancer. College of american pathologists consensus statement 1999. Arch Pathol Lab Med 124:966–978
Pandey DP, Lappano R, Albanito L, Madeo A, Maggiolini M, Picard D (2009) Estrogenic GPR30 signalling induces proliferation and migration of breast cancer cells through CTGF. EMBO J 28:523–532
Ignatov A, Ignatov T, Roessner A, Costa SD, Kalinski T (2010) Role of GPR30 in the mechanisms of tamoxifen resistance in breast cancer MCF-7 cells. Breast Cancer Res Treat 123:87–96
Song RX, Barnes CJ, Zhang Z, Bao Y, Kumar R, Santen RJ (2004) The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor alpha to the plasma membrane. Proc Natl Acad Sci U S A 101:2076–2081
Pietras RJ (2003) Interactions between estrogen and growth factor receptors in human breast cancer and the tumor-associated vasculature. Breast J 9:361–373
Song RX, Chen Y, Zhang Z, Bao Y, Yue W, Wang JP, Fan P, Santen RJ (2010) Estrogen utilization of IGF-1-R and EGF-R to signal in breast cancer cells. J Steroid Biochem Mol Biol 118:219–230
Migliaccio A, Castoria G, Di Domenico M, Ciociola A, Lombardi M, De Falco A, Nanayakkara M, Bottero D, De Stasio R, Varricchio L, Auricchio F (2006) Crosstalk between EGFR and extranuclear steroid receptors. Ann N Y Acad Sci 1089:194–200
Planas-Silva MD, Bruggeman RD, Grenko RT, Stanley Smith J (2006) Role of c-Src and focal adhesion kinase in progression and metastasis of estrogen receptor-positive breast cancer. Biochem Biophys Res Commun 341:73–81
Rahman MA, Senga T, Ito S, Hyodo T, Hasegawa H, Hamaguchi (2010) M S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion. J Biol Chem 285:3806–3814
Hinton CV, Avraham S, Avraham HK (2010) Role of the CXCR4/CXCL12 signaling axis in breast cancer metastasis to the brain. Clin Exp Metastasis 27:97–105
Ali S, Lazennec G (2007) Chemokines: novel targets for breast cancer metastasis. Cancer Metastasis Rev 26:401–420
Bendrik C, Dabrosin C (2009) Estradiol increases IL-8 secretion of normal human breast tissue and breast cancer in vivo. J Immunol 182:371–378
Lin Y, Huang R, Chen L, Li S, Shi Q, Jordan C, Huang RP (2004) Identification of interleukin-8 as estrogen receptor-regulated factor involved in breast cancer invasion and angiogenesis by protein arrays. Int J Cancer 109:507–515
Seeger H, Wallwiener D, Mueck AO (2006) Different effects of estradiol and various antiestrogens on TNF-alpha-induced changes of biochemical markers for growth and invasion of human breast cancerbreast cancer cells. Life Sci 78:1464–1468
Sengupta S, Schiff R, Katzenellenbogen BS (2009) Post-transcriptional regulation of chemokine receptor CXCR4 by estrogen in HER2 overexpressing, estrogen receptor-positive breast cancer cells. Breast Cancer Res Treat 117:243–251
Ruoslahti E, Reed JC (1994) Anchorage dependence, integrins, and apoptosis. Cell 77:477–478
Hynes RO, Bader BL, Hodivala-Dilke K (1999) Integrins in vascular development. Braz J Med Biol Res 32:501–510
Desgrosellier JS, Cheresh DA (2010) Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer 10:9–22
Sisci D, Middea E, Morelli C, Lanzino M, Aquila S, Rizza P, Catalano S, Casaburi I, Maggiolini M, Ando S 17beta-Estradiol enhances alpha(5) integrin subunit gene expression through ERalpha-Sp1 interaction and reduces cell motility and invasion of ERalpha-positive breast cancer cells. Breast Cancer Res Treat
Lindberg K, Strom A, Lock JG, Gustafsson JA, Haldosen LA, Helguero LA (2010) Expression of estrogen receptor beta increases integrin alpha1 and integrin beta1 levels and enhances adhesion of breast cancer cells. J Cell Physiol 222:156–167
McGowan EM, Saad S, Bendall LJ, Bradstock KF, Clarke CL (2004) Effect of progesterone receptor a predominance on breast cancer cell migration into bone marrow fibroblasts. Breast Cancer Res Treat 83:211–220
Stevenson LE, Ravichandran KS, Frackelton AR Jr (1999) Shc dominant negative disrupts cell cycle progression in both G0–G1 and G2-M of ErbB2-positive breast cancer cells. Cell Growth Differ 10:61–71
Lee MS, Igawa T, Lin MF (2004) Tyrosine-317 of p52(Shc) mediates androgen-stimulated proliferation signals in human prostate cancer cells. Oncogene 23:3048–3058
Webster MA, Hutchinson JN, Rauh MJ, Muthuswamy SK, Anton M, Tortorice CG, Cardiff RD, Graham FL, Hassell JA, Muller WJ (1998) Requirement for both Shc and phosphatidylinositol 3′ kinase signaling pathways in polyomavirus middle T-mediated mammary tumorigenesis. Mol Cell Biol 18:2344–2359
McGlade J, Cheng A, Pelicci G, Pelicci PG, Pawson T (1992) Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc Natl Acad Sci U S A 89:8869–8873
Wary KK, Mariotti A, Zurzolo C, Giancotti FG (1998) A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell 94:625–634
Thomas D, Bradshaw RA (1997) Differential utilization of ShcA tyrosine residues and functional domains in the transduction of epidermal growth factor-induced mitogen-activated protein kinase activation in 293T cells and nerve growth factor-induced neurite outgrowth in PC12 cells. Identification of a new Grb2.Sos1 binding site. J Biol Chem 272:22293–22299
Collins LR, Ricketts WA, Yeh L, Cheresh D (1999) Bifurcation of cell migratory and proliferative signaling by the adaptor protein Shc. J Cell Biol 147:1561–1568
Zhou MM, Ravichandran KS, Olejniczak EF, Petros AM, Meadows RP, Sattler M, Harlan JE, Wade WS, Burakoff SJ, Fesik SW (1995) Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378:584–592
Sato K, Gotoh N, Otsuki T, Kakumoto M, Aoto M, Tokmakov AA, Shibuya M, Fukami Y (1997) Tyrosine residues 239 and 240 of Shc are phosphatidylinositol 4, 5-bisphosphate-dependent phosphorylation sites by c-Src. Biochem Biophys Res Commun 240:399–404
Guo Z, Dai B, Jiang T, Xu K, Xie Y, Kim O, Nesheiwat I, Kong X, Melamed J, Handratta VD, Njar VC, Brodie AM, Yu LR, Veenstra TD, Chen H, Qiu Y (2006) Regulation of androgen receptor activity by tyrosine phosphorylation. Cancer Cell 10:309–319
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Flamini, M.I., Sanchez, A.M., Fu, XD., Simoncini, T. (2012). Sex-Steroid Rapid Action and Its Role in Invasiveness and Metastasis of Breast Cancer. In: Castoria, G., Migliaccio, A. (eds) Advances in Rapid Sex-Steroid Action. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1764-4_6
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