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Erschienen in: Endocrine 2/2011

01.10.2011 | Review

Cross-talk and modulation of signaling between somatostatin and growth factor receptors

verfasst von: Ujendra Kumar

Erschienen in: Endocrine | Ausgabe 2/2011

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Abstract

The process of homo- and/or heterodimerization of G-protein coupled receptors (GPCRs) and receptor tyrosine kinase (RTK) families are crucial for implicating the fundamental properties of receptor proteins including receptor expression, trafficking, and desensitization as well as signal transduction. The members of GPCR and RTK family constitute largest cell surface receptor proteins and regulate physiological functions of cells in response to external and internal stimuli. Notably, GPCRs and RTKs play major role in regulation of several key cellular functions which are associated with several pathological conditions including cancer biology, neurodegenerative and cardiovascular diseases. The focus of this review is to highlight the recent findings on the possible cross-talk between somatostatin receptors (members of GPCR family) and growth factor receptors like epidermal growth factor receptors (members of RTK family). Furthermore, functional consequences of such an interaction in modulation of signaling pathways linked to pathological conditions specifically in cancer are discussed.
Literatur
1.
Zurück zum Zitat D. Fotiadis, Y. Liang, S. Filipek, D.A. Saperstein, A. Engel, K. Palczewski, Atomic-force microscopy: rhodopsin dimers in native disc membranes. Nature 421(6919), 127–128 (2003)PubMedCrossRef D. Fotiadis, Y. Liang, S. Filipek, D.A. Saperstein, A. Engel, K. Palczewski, Atomic-force microscopy: rhodopsin dimers in native disc membranes. Nature 421(6919), 127–128 (2003)PubMedCrossRef
2.
Zurück zum Zitat M. Bouvier, N. Heveker, R. Jockers, S. Marullo, G. Milligan, BRET analysis of GPCR oligomerization: newer does not mean better. Nat. Methods 4(1), 3–4 (2007). author reply 4PubMedCrossRef M. Bouvier, N. Heveker, R. Jockers, S. Marullo, G. Milligan, BRET analysis of GPCR oligomerization: newer does not mean better. Nat. Methods 4(1), 3–4 (2007). author reply 4PubMedCrossRef
3.
Zurück zum Zitat G. Milligan, G protein-coupled receptor dimerization: function and ligand pharmacology. Mol. Pharmacol. 66(1), 1–7 (2004)PubMedCrossRef G. Milligan, G protein-coupled receptor dimerization: function and ligand pharmacology. Mol. Pharmacol. 66(1), 1–7 (2004)PubMedCrossRef
4.
Zurück zum Zitat U. Kumar, M. Grant, Somatostatin and somatostatin receptors. Results Probl. Cell Differ. 50, 137–184 (2010)PubMed U. Kumar, M. Grant, Somatostatin and somatostatin receptors. Results Probl. Cell Differ. 50, 137–184 (2010)PubMed
5.
Zurück zum Zitat Y. Yarden, M.X. Sliwkowski, Untangling the ErbB signalling network. Nat. Rev. Mol. Cell Biol. 2(2), 127–137 (2001)PubMedCrossRef Y. Yarden, M.X. Sliwkowski, Untangling the ErbB signalling network. Nat. Rev. Mol. Cell Biol. 2(2), 127–137 (2001)PubMedCrossRef
6.
7.
Zurück zum Zitat H. Daub, C. Wallasch, A. Lankenau, A. Herrlich, A. Ullrich, Signal characteristics of G protein-transactivated EGF receptor. EMBO J. 16(23), 7032–7044 (1997)PubMedCrossRef H. Daub, C. Wallasch, A. Lankenau, A. Herrlich, A. Ullrich, Signal characteristics of G protein-transactivated EGF receptor. EMBO J. 16(23), 7032–7044 (1997)PubMedCrossRef
8.
Zurück zum Zitat L.M. Luttrell, Y. Daaka, R.J. Lefkowitz, Regulation of tyrosine kinase cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11, 177–183 (1999)PubMedCrossRef L.M. Luttrell, Y. Daaka, R.J. Lefkowitz, Regulation of tyrosine kinase cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11, 177–183 (1999)PubMedCrossRef
9.
Zurück zum Zitat F.S. Lee, M.V. Chao, Activation of Trk neurotrophin receptors in the absence of neurotrophins. Proc. Natl. Acad. Sci. USA 98(6), 3555–3560 (2001)PubMedCrossRef F.S. Lee, M.V. Chao, Activation of Trk neurotrophin receptors in the absence of neurotrophins. Proc. Natl. Acad. Sci. USA 98(6), 3555–3560 (2001)PubMedCrossRef
10.
Zurück zum Zitat K.L. Pierce, L.M. Luttrell, R.J. Lefkowitz, New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades. Oncogene 20(13), 1532–1539 (2001)PubMedCrossRef K.L. Pierce, L.M. Luttrell, R.J. Lefkowitz, New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades. Oncogene 20(13), 1532–1539 (2001)PubMedCrossRef
11.
Zurück zum Zitat P.O. Hackel, E. Zwick, N. Prenzel, A. Ullrich, Epidermal growth factor receptors: critical mediators of multiple receptor pathways. Curr. Opin. Cell Biol. 11(2), 184–189 (1999)PubMedCrossRef P.O. Hackel, E. Zwick, N. Prenzel, A. Ullrich, Epidermal growth factor receptors: critical mediators of multiple receptor pathways. Curr. Opin. Cell Biol. 11(2), 184–189 (1999)PubMedCrossRef
12.
Zurück zum Zitat B. Hellman, A. Lernmark, Inhibition of the in vitro secretion of insulin by an extract of pancreatic alpha-1 cells. Endocrinology 84(6), 1484–1488 (1969)PubMedCrossRef B. Hellman, A. Lernmark, Inhibition of the in vitro secretion of insulin by an extract of pancreatic alpha-1 cells. Endocrinology 84(6), 1484–1488 (1969)PubMedCrossRef
13.
Zurück zum Zitat L. Krulich, A.P. Dhariwal, S.M. McCann, Stimulatory and inhibitory effects of purified hypothalamic extracts on growth hormone release from rat pituitary in vitro. Endocrinology 83(4), 783–790 (1968)PubMedCrossRef L. Krulich, A.P. Dhariwal, S.M. McCann, Stimulatory and inhibitory effects of purified hypothalamic extracts on growth hormone release from rat pituitary in vitro. Endocrinology 83(4), 783–790 (1968)PubMedCrossRef
14.
Zurück zum Zitat Y.C. Patel, S. Reichlin, Somatostatin in hypothalamus, extrahypothalamic brain, and peripheral tissues of the rat. Endocrinology 102(2), 523–530 (1978)PubMedCrossRef Y.C. Patel, S. Reichlin, Somatostatin in hypothalamus, extrahypothalamic brain, and peripheral tissues of the rat. Endocrinology 102(2), 523–530 (1978)PubMedCrossRef
15.
Zurück zum Zitat Y.C. Patel, Somatostatin and its receptor family. Front. Neuroendocrinol. 20(3), 157–198 (1999)PubMedCrossRef Y.C. Patel, Somatostatin and its receptor family. Front. Neuroendocrinol. 20(3), 157–198 (1999)PubMedCrossRef
16.
Zurück zum Zitat J. Epelbaum, P. Dournaud, M. Fodor, C. Viollet, The neurobiology of somatostatin. Crit. Rev. Neurobiol. 8(1–2), 25–44 (1994)PubMed J. Epelbaum, P. Dournaud, M. Fodor, C. Viollet, The neurobiology of somatostatin. Crit. Rev. Neurobiol. 8(1–2), 25–44 (1994)PubMed
17.
Zurück zum Zitat Y.C. Patel, Molecular pharmacology of somatostatin receptor subtypes. J. Endocrinol. Invest. 20(6), 348–367 (1997)PubMed Y.C. Patel, Molecular pharmacology of somatostatin receptor subtypes. J. Endocrinol. Invest. 20(6), 348–367 (1997)PubMed
18.
Zurück zum Zitat U. Kumar, D. Laird, C.B. Srikant, E. Escher, Y.C. Patel, Expression of the five somatostatin receptor (SSTR1–5) subtypes in rat pituitary somatotrophes: quantitative analysis by double-layer immunofluorescence confocal microscopy. Endocrinology 138(10), 4473–4476 (1997)PubMedCrossRef U. Kumar, D. Laird, C.B. Srikant, E. Escher, Y.C. Patel, Expression of the five somatostatin receptor (SSTR1–5) subtypes in rat pituitary somatotrophes: quantitative analysis by double-layer immunofluorescence confocal microscopy. Endocrinology 138(10), 4473–4476 (1997)PubMedCrossRef
19.
Zurück zum Zitat K.V. Sorensen, S.E. Christensen, A.P. Hansen, E. Pedersen, H. Orskov, Cerebrospinal fluid somatostatin inversely correlated with disease activity in multiple sclerosis. Lancet 1(8331), 988 (1983)PubMedCrossRef K.V. Sorensen, S.E. Christensen, A.P. Hansen, E. Pedersen, H. Orskov, Cerebrospinal fluid somatostatin inversely correlated with disease activity in multiple sclerosis. Lancet 1(8331), 988 (1983)PubMedCrossRef
20.
Zurück zum Zitat D. Hoyer, H. Lubbert, C. Bruns, Molecular pharmacology of somatostatin receptors. Naunyn Schmiedebergs Arch Pharmacol 350(5), 441–453 (1994)PubMedCrossRef D. Hoyer, H. Lubbert, C. Bruns, Molecular pharmacology of somatostatin receptors. Naunyn Schmiedebergs Arch Pharmacol 350(5), 441–453 (1994)PubMedCrossRef
21.
Zurück zum Zitat A. Schonbrunn, H. Tashjian Jr., Characterization of functional receptors for somatostatin in rat pituitary cells in culture. J. Biol. Chem. 253(18), 6473–6483 (1978)PubMed A. Schonbrunn, H. Tashjian Jr., Characterization of functional receptors for somatostatin in rat pituitary cells in culture. J. Biol. Chem. 253(18), 6473–6483 (1978)PubMed
22.
Zurück zum Zitat K.D. Pfleger, K.A. Eidne, Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells. Biochem. J. 385(Pt 3), 625–637 (2005)PubMed K.D. Pfleger, K.A. Eidne, Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells. Biochem. J. 385(Pt 3), 625–637 (2005)PubMed
23.
Zurück zum Zitat S. Bulenger, S. Marullo, M. Bouvier, Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26(3), 131–137 (2005)PubMedCrossRef S. Bulenger, S. Marullo, M. Bouvier, Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26(3), 131–137 (2005)PubMedCrossRef
24.
Zurück zum Zitat M. Duran-Prado, M.M. Malagon, F. Gracia-Navarro, J.P. Castano, Dimerization of G protein-coupled receptors: new avenues for somatostatin receptor signalling, control and functioning. Mol. Cell. Endocrinol. 286(1–2), 63–68 (2008)PubMedCrossRef M. Duran-Prado, M.M. Malagon, F. Gracia-Navarro, J.P. Castano, Dimerization of G protein-coupled receptors: new avenues for somatostatin receptor signalling, control and functioning. Mol. Cell. Endocrinol. 286(1–2), 63–68 (2008)PubMedCrossRef
25.
Zurück zum Zitat J.M. Gripentrog, K.P. Kantele, A.J. Jesaitis, H.M. Miettinen, Experimental evidence for lack of homodimerization of the G protein-coupled human N-formyl peptide receptor. J. Immunol. 171(6), 3187–3193 (2003)PubMed J.M. Gripentrog, K.P. Kantele, A.J. Jesaitis, H.M. Miettinen, Experimental evidence for lack of homodimerization of the G protein-coupled human N-formyl peptide receptor. J. Immunol. 171(6), 3187–3193 (2003)PubMed
26.
Zurück zum Zitat B.H. Meyer, J.M. Segura, K.L. Martinez, R. Hovius, N. George, K. Johnsson, H. Vogel, FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl. Acad. Sci. USA 103(7), 2138–2143 (2006)PubMedCrossRef B.H. Meyer, J.M. Segura, K.L. Martinez, R. Hovius, N. George, K. Johnsson, H. Vogel, FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl. Acad. Sci. USA 103(7), 2138–2143 (2006)PubMedCrossRef
27.
Zurück zum Zitat M. Grant, B. Collier, U. Kumar, Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a role in receptor trafficking. J. Biol. Chem. 279(35), 36179–36183 (2004)PubMedCrossRef M. Grant, B. Collier, U. Kumar, Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a role in receptor trafficking. J. Biol. Chem. 279(35), 36179–36183 (2004)PubMedCrossRef
28.
Zurück zum Zitat M. Pfeiffer, T. Koch, H. Schroder, M. Klutzny, S. Kirscht, H.J. Kreienkamp, V. Hollt, S. Schulz, Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A). J. Biol. Chem. 276(17), 14027–14036 (2001)PubMed M. Pfeiffer, T. Koch, H. Schroder, M. Klutzny, S. Kirscht, H.J. Kreienkamp, V. Hollt, S. Schulz, Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A). J. Biol. Chem. 276(17), 14027–14036 (2001)PubMed
29.
Zurück zum Zitat M.A. Ayoub, C. Couturier, E. Lucas-Meunier, S. Angers, P. Fossier, M. Bouvier, R. Jockers, Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 277(24), 21522–21528 (2002)PubMedCrossRef M.A. Ayoub, C. Couturier, E. Lucas-Meunier, S. Angers, P. Fossier, M. Bouvier, R. Jockers, Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 277(24), 21522–21528 (2002)PubMedCrossRef
30.
Zurück zum Zitat M. Rocheville, D.C. Lange, U. Kumar, R. Sasi, R.C. Patel, Y.C. Patel, Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J. Biol. Chem. 275(11), 7862–7869 (2000)PubMedCrossRef M. Rocheville, D.C. Lange, U. Kumar, R. Sasi, R.C. Patel, Y.C. Patel, Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J. Biol. Chem. 275(11), 7862–7869 (2000)PubMedCrossRef
31.
Zurück zum Zitat M. Grant, R.C. Patel, U. Kumar, The role of subtype-specific ligand binding and the C-tail domain in dimer formation of human somatostatin receptors. J. Biol. Chem. 279(37), 38636–38643 (2004)PubMedCrossRef M. Grant, R.C. Patel, U. Kumar, The role of subtype-specific ligand binding and the C-tail domain in dimer formation of human somatostatin receptors. J. Biol. Chem. 279(37), 38636–38643 (2004)PubMedCrossRef
32.
Zurück zum Zitat M. Duran-Prado, C. Bucharles, B.J. Gonzalez, R. Vazquez-Martinez, A.J. Martinez-Fuentes, S. Garcia-Navarro, S.J. Rhodes, H. Vaudry, M.M. Malagon, J.P. Castano, Porcine somatostatin receptor 2 displays typical pharmacological sst2 features but unique dynamics of homodimerization and internalization. Endocrinology 148(1), 411–421 (2007)PubMedCrossRef M. Duran-Prado, C. Bucharles, B.J. Gonzalez, R. Vazquez-Martinez, A.J. Martinez-Fuentes, S. Garcia-Navarro, S.J. Rhodes, H. Vaudry, M.M. Malagon, J.P. Castano, Porcine somatostatin receptor 2 displays typical pharmacological sst2 features but unique dynamics of homodimerization and internalization. Endocrinology 148(1), 411–421 (2007)PubMedCrossRef
33.
Zurück zum Zitat S.A. War, R.K. Somvanshi, U. Kumar, Somatostatin receptor-3 mediated intracellular signaling and apoptosis is regulated by its cytoplasmic terminal. Biochim. Biophys. Acta 1813(3), 390–402 (2011)PubMedCrossRef S.A. War, R.K. Somvanshi, U. Kumar, Somatostatin receptor-3 mediated intracellular signaling and apoptosis is regulated by its cytoplasmic terminal. Biochim. Biophys. Acta 1813(3), 390–402 (2011)PubMedCrossRef
34.
Zurück zum Zitat R.K. Somvanshi, S. Billova, G. Kharmate, P.S. Rajput, U. Kumar, C-tail mediated modulation of somatostatin receptor type-4 homo- and heterodimerizations and signaling. Cell. Signal. 21(9), 1396–1414 (2009)PubMedCrossRef R.K. Somvanshi, S. Billova, G. Kharmate, P.S. Rajput, U. Kumar, C-tail mediated modulation of somatostatin receptor type-4 homo- and heterodimerizations and signaling. Cell. Signal. 21(9), 1396–1414 (2009)PubMedCrossRef
35.
Zurück zum Zitat A. Baragli, H. Alturaihi, H.L. Watt, A. Abdallah, U. Kumar, Heterooligomerization of human dopamine receptor 2 and somatostatin receptor 2 co-immunoprecipitation and fluorescence resonance energy transfer analysis. Cell. Signal. 19(11), 2304–2316 (2007)PubMedCrossRef A. Baragli, H. Alturaihi, H.L. Watt, A. Abdallah, U. Kumar, Heterooligomerization of human dopamine receptor 2 and somatostatin receptor 2 co-immunoprecipitation and fluorescence resonance energy transfer analysis. Cell. Signal. 19(11), 2304–2316 (2007)PubMedCrossRef
36.
Zurück zum Zitat M. Grant, H. Alturaihi, P. Jaquet, B. Collier, U. Kumar, Cell growth inhibition and functioning of human somatostatin receptor type 2 are modulated by receptor heterodimerization. Mol. Endocrinol. 22(10), 2278–2292 (2008)PubMedCrossRef M. Grant, H. Alturaihi, P. Jaquet, B. Collier, U. Kumar, Cell growth inhibition and functioning of human somatostatin receptor type 2 are modulated by receptor heterodimerization. Mol. Endocrinol. 22(10), 2278–2292 (2008)PubMedCrossRef
37.
Zurück zum Zitat M. Pfeiffer, T. Koch, H. Schroder, M. Laugsch, V. Hollt, S. Schulz, Heterodimerization of somatostatin and opioid receptors cross-modulates phosphorylation, internalization, and desensitization. J. Biol. Chem. 277(22), 19762–19772 (2002)PubMedCrossRef M. Pfeiffer, T. Koch, H. Schroder, M. Laugsch, V. Hollt, S. Schulz, Heterodimerization of somatostatin and opioid receptors cross-modulates phosphorylation, internalization, and desensitization. J. Biol. Chem. 277(22), 19762–19772 (2002)PubMedCrossRef
38.
Zurück zum Zitat M. Rocheville, D.C. Lange, U. Kumar, S.C. Patel, R.C. Patel, Y.C. Patel, Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science 288(5463), 154–157 (2000)PubMedCrossRef M. Rocheville, D.C. Lange, U. Kumar, S.C. Patel, R.C. Patel, Y.C. Patel, Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science 288(5463), 154–157 (2000)PubMedCrossRef
39.
Zurück zum Zitat R.K. Somvanshi, N. Chaudhari, X. Qiu, U. Kumar, Heterodimerization of beta2 adrenergic receptor and somatostatin receptor 5: implications in modulation of signaling pathway. J. Mol. Signal. 6, 9 (2011) R.K. Somvanshi, N. Chaudhari, X. Qiu, U. Kumar, Heterodimerization of beta2 adrenergic receptor and somatostatin receptor 5: implications in modulation of signaling pathway. J. Mol. Signal. 6, 9 (2011)
40.
Zurück zum Zitat R.K. Somvanshi, S.A. War, N. Chaudhari, X. Qiu, U. Kumar, Receptor specific crosstalk and modulation of signaling upon heterodimerization between beta1-adrenergic receptor and somatostatin receptor-5. Cell. Signal. 23(5), 794–811 (2011)PubMedCrossRef R.K. Somvanshi, S.A. War, N. Chaudhari, X. Qiu, U. Kumar, Receptor specific crosstalk and modulation of signaling upon heterodimerization between beta1-adrenergic receptor and somatostatin receptor-5. Cell. Signal. 23(5), 794–811 (2011)PubMedCrossRef
41.
Zurück zum Zitat G. Kharmate, P.S. Rajput, H.L. Watt, R.K. Somvanshi, N. Chaudhari, X. Qiu, U. Kumar, Dissociation of epidermal growth factor receptor and ErbB2 heterodimers in the presence of somatostatin receptor 5 modulate signaling pathways. Endocrinology 152(3), 931–945 (2011)PubMedCrossRef G. Kharmate, P.S. Rajput, H.L. Watt, R.K. Somvanshi, N. Chaudhari, X. Qiu, U. Kumar, Dissociation of epidermal growth factor receptor and ErbB2 heterodimers in the presence of somatostatin receptor 5 modulate signaling pathways. Endocrinology 152(3), 931–945 (2011)PubMedCrossRef
42.
Zurück zum Zitat G. Kharmate, P.S. Rajput, H.L. Watt, R.K. Somvanshi, N. Chaudhari, X. Qiu, U. Kumar, Role of somatostatin receptor 1 and 5 on epidermal growth factor receptor mediated signaling. Biochim. Biophys. Acta 1813(6), 1172–1189 (2011)PubMedCrossRef G. Kharmate, P.S. Rajput, H.L. Watt, R.K. Somvanshi, N. Chaudhari, X. Qiu, U. Kumar, Role of somatostatin receptor 1 and 5 on epidermal growth factor receptor mediated signaling. Biochim. Biophys. Acta 1813(6), 1172–1189 (2011)PubMedCrossRef
43.
Zurück zum Zitat H.L. Watt, G.D. Kharmate, U. Kumar, Somatostatin receptors 1 and 5 heterodimerize with epidermal growth factor receptor: agonist-dependent modulation of the downstream MAPK signalling pathway in breast cancer cells. Cell. Signal. 21(3), 428–439 (2009)PubMedCrossRef H.L. Watt, G.D. Kharmate, U. Kumar, Somatostatin receptors 1 and 5 heterodimerize with epidermal growth factor receptor: agonist-dependent modulation of the downstream MAPK signalling pathway in breast cancer cells. Cell. Signal. 21(3), 428–439 (2009)PubMedCrossRef
44.
Zurück zum Zitat M. Grant, U. Kumar, The role of G-proteins in the dimerisation of human somatostatin receptor types 2 and 5. Regul. Pept. 159(1–3), 3–8 (2010)PubMedCrossRef M. Grant, U. Kumar, The role of G-proteins in the dimerisation of human somatostatin receptor types 2 and 5. Regul. Pept. 159(1–3), 3–8 (2010)PubMedCrossRef
45.
Zurück zum Zitat R.C. Patel, U. Kumar, D.C. Lamb, J.S. Eid, M. Rocheville, M. Grant, A. Rani, T. Hazlett, S.C. Patel, E. Gratton, Y.C. Patel, Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells. Proc. Natl. Acad. Sci. USA 99(5), 3294–3299 (2002)PubMedCrossRef R.C. Patel, U. Kumar, D.C. Lamb, J.S. Eid, M. Rocheville, M. Grant, A. Rani, T. Hazlett, S.C. Patel, E. Gratton, Y.C. Patel, Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells. Proc. Natl. Acad. Sci. USA 99(5), 3294–3299 (2002)PubMedCrossRef
46.
Zurück zum Zitat Y.C. Patel, M.T. Greenwood, A. Warszynska, R. Panetta, C.B. Srikant, All five cloned human somatostatin receptors (hSSTR1–5) are functionally coupled to adenylyl cyclase. Biochem. Biophys. Res. Commun. 198(2), 605–612 (1994)PubMedCrossRef Y.C. Patel, M.T. Greenwood, A. Warszynska, R. Panetta, C.B. Srikant, All five cloned human somatostatin receptors (hSSTR1–5) are functionally coupled to adenylyl cyclase. Biochem. Biophys. Res. Commun. 198(2), 605–612 (1994)PubMedCrossRef
47.
Zurück zum Zitat M.A. Olayioye, R.M. Neve, H. Lane, N.E. Hynes, The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19(13), 3159–3167 (2000)PubMedCrossRef M.A. Olayioye, R.M. Neve, H. Lane, N.E. Hynes, The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19(13), 3159–3167 (2000)PubMedCrossRef
48.
Zurück zum Zitat D.C. Lev, L.S. Kim, V. Melnikova, M. Ruiz, H.N. Ananthaswamy, J.E. Price, Dual blockade of EGFR and ERK1/2 phosphorylation potentiates growth inhibition of breast cancer cells. Br. J. Cancer 91(4), 795–802 (2004)PubMed D.C. Lev, L.S. Kim, V. Melnikova, M. Ruiz, H.N. Ananthaswamy, J.E. Price, Dual blockade of EGFR and ERK1/2 phosphorylation potentiates growth inhibition of breast cancer cells. Br. J. Cancer 91(4), 795–802 (2004)PubMed
49.
Zurück zum Zitat S. Okubo, J. Kurebayashi, T. Otsuki, Y. Yamamoto, K. Tanaka, H. Sonoo, Additive antitumour effect of the epidermal growth factor receptor tyrosine kinase inhibitor gefitinib (Iressa, ZD1839) and the antioestrogen fulvestrant (Faslodex, ICI 182, 780) in breast cancer cells. Br. J. Cancer 90(1), 236–244 (2004)PubMedCrossRef S. Okubo, J. Kurebayashi, T. Otsuki, Y. Yamamoto, K. Tanaka, H. Sonoo, Additive antitumour effect of the epidermal growth factor receptor tyrosine kinase inhibitor gefitinib (Iressa, ZD1839) and the antioestrogen fulvestrant (Faslodex, ICI 182, 780) in breast cancer cells. Br. J. Cancer 90(1), 236–244 (2004)PubMedCrossRef
50.
Zurück zum Zitat A. deFazio, Y.E. Chiew, R.L. Sini, P.W. Janes, R.L. Sutherland, Expression of c-erbB receptors, heregulin and oestrogen receptor in human breast cell lines. Int. J. Cancer 87(4), 487–498 (2000)PubMedCrossRef A. deFazio, Y.E. Chiew, R.L. Sini, P.W. Janes, R.L. Sutherland, Expression of c-erbB receptors, heregulin and oestrogen receptor in human breast cell lines. Int. J. Cancer 87(4), 487–498 (2000)PubMedCrossRef
52.
Zurück zum Zitat H.K. Gan, M. Lappas, D.X. Cao, A. Cvrljevdic, A.M. Scott, T.G. Johns, Targeting a unique EGFR epitope with monoclonal antibody 806 activates NF-kappaB and initiates tumour vascular normalization. J. Cell Mol. Med. 13(9B), 3993–4001 (2009)PubMedCrossRef H.K. Gan, M. Lappas, D.X. Cao, A. Cvrljevdic, A.M. Scott, T.G. Johns, Targeting a unique EGFR epitope with monoclonal antibody 806 activates NF-kappaB and initiates tumour vascular normalization. J. Cell Mol. Med. 13(9B), 3993–4001 (2009)PubMedCrossRef
53.
Zurück zum Zitat D. Gerber, N. Sal-Man, Y. Shai, Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization. J. Biol. Chem. 279(20), 21177–21182 (2004)PubMedCrossRef D. Gerber, N. Sal-Man, Y. Shai, Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization. J. Biol. Chem. 279(20), 21177–21182 (2004)PubMedCrossRef
54.
Zurück zum Zitat A.W. Burgess, H.S. Cho, C. Eigenbrot, K.M. Ferguson, T.P. Garrett, D.J. Leahy, M.A. Lemmon, M.X. Sliwkowski, C.W. Ward, S. Yokoyama, An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol. Cell 12(3), 541–552 (2003)PubMedCrossRef A.W. Burgess, H.S. Cho, C. Eigenbrot, K.M. Ferguson, T.P. Garrett, D.J. Leahy, M.A. Lemmon, M.X. Sliwkowski, C.W. Ward, S. Yokoyama, An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol. Cell 12(3), 541–552 (2003)PubMedCrossRef
55.
Zurück zum Zitat T.P. Garrett, N.M. McKern, M. Lou, T.C. Elleman, T.E. Adams, G.O. Lovrecz, M. Kofler, R.N. Jorissen, E.C. Nice, A.W. Burgess, C.W. Ward, The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol. Cell 11(2), 495–505 (2003)PubMedCrossRef T.P. Garrett, N.M. McKern, M. Lou, T.C. Elleman, T.E. Adams, G.O. Lovrecz, M. Kofler, R.N. Jorissen, E.C. Nice, A.W. Burgess, C.W. Ward, The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol. Cell 11(2), 495–505 (2003)PubMedCrossRef
56.
Zurück zum Zitat L.N. Klapper, M.H. Kirschbaum, M. Sela, Y. Yarden, Biochemical and clinical implications of the ErbB/HER signaling network of growth factor receptors. Adv. Cancer Res. 77, 25–79 (2000)PubMedCrossRef L.N. Klapper, M.H. Kirschbaum, M. Sela, Y. Yarden, Biochemical and clinical implications of the ErbB/HER signaling network of growth factor receptors. Adv. Cancer Res. 77, 25–79 (2000)PubMedCrossRef
57.
Zurück zum Zitat K.L. Carraway 3rd, L.C. Cantley, A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell 78(1), 5–8 (1994)PubMedCrossRef K.L. Carraway 3rd, L.C. Cantley, A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell 78(1), 5–8 (1994)PubMedCrossRef
58.
Zurück zum Zitat J.L. Gilmore, D.J. Riese 2nd, secErbB4-26/549 antagonizes ligand-induced ErbB4 tyrosine phosphorylation. Oncol. Res. 14(11–12), 589–602 (2004)PubMed J.L. Gilmore, D.J. Riese 2nd, secErbB4-26/549 antagonizes ligand-induced ErbB4 tyrosine phosphorylation. Oncol. Res. 14(11–12), 589–602 (2004)PubMed
59.
Zurück zum Zitat K.L. Carraway 3rd, S.P. Soltoff, A.J. Diamonti, L.C. Cantley, Heregulin stimulates mitogenesis and phosphatidylinositol 3-kinase in mouse fibroblasts transfected with erbB2/neu and erbB3. J. Biol. Chem. 270(13), 7111–7116 (1995)PubMedCrossRef K.L. Carraway 3rd, S.P. Soltoff, A.J. Diamonti, L.C. Cantley, Heregulin stimulates mitogenesis and phosphatidylinositol 3-kinase in mouse fibroblasts transfected with erbB2/neu and erbB3. J. Biol. Chem. 270(13), 7111–7116 (1995)PubMedCrossRef
60.
Zurück zum Zitat B.D. Cohen, P.A. Kiener, J.M. Green, L. Foy, H.P. Fell, K. Zhang, The relationship between human epidermal growth-like factor receptor expression and cellular transformation in NIH3T3 cells. J. Biol. Chem. 271(48), 30897–30903 (1996)PubMedCrossRef B.D. Cohen, P.A. Kiener, J.M. Green, L. Foy, H.P. Fell, K. Zhang, The relationship between human epidermal growth-like factor receptor expression and cellular transformation in NIH3T3 cells. J. Biol. Chem. 271(48), 30897–30903 (1996)PubMedCrossRef
61.
Zurück zum Zitat P.M. Guy, J.V. Platko, L.C. Cantley, R.A. Cerione, K.L. Carraway 3rd, Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity. Proc. Natl. Acad. Sci. USA 91(17), 8132–8136 (1994)PubMedCrossRef P.M. Guy, J.V. Platko, L.C. Cantley, R.A. Cerione, K.L. Carraway 3rd, Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity. Proc. Natl. Acad. Sci. USA 91(17), 8132–8136 (1994)PubMedCrossRef
62.
Zurück zum Zitat T. Holbro, R.R. Beerli, F. Maurer, M. Koziczak, C.F. Barbas 3rd, N.E. Hynes, The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation. Proc. Natl. Acad. Sci. USA 100(15), 8933–8938 (2003)PubMedCrossRef T. Holbro, R.R. Beerli, F. Maurer, M. Koziczak, C.F. Barbas 3rd, N.E. Hynes, The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation. Proc. Natl. Acad. Sci. USA 100(15), 8933–8938 (2003)PubMedCrossRef
63.
Zurück zum Zitat R. Pinkas-Kramarski, M. Shelly, S. Glathe, B.J. Ratzkin, Y. Yarden, Neu differentiation factor/neuregulin isoforms activate distinct receptor combinations. J. Biol. Chem. 271(32), 19029–19032 (1996)PubMedCrossRef R. Pinkas-Kramarski, M. Shelly, S. Glathe, B.J. Ratzkin, Y. Yarden, Neu differentiation factor/neuregulin isoforms activate distinct receptor combinations. J. Biol. Chem. 271(32), 19029–19032 (1996)PubMedCrossRef
64.
Zurück zum Zitat K. Zhang, J. Sun, N. Liu, D. Wen, D. Chang, A. Thomason, S.K. Yoshinaga, Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2. J. Biol. Chem. 271(7), 3884–3890 (1996)PubMedCrossRef K. Zhang, J. Sun, N. Liu, D. Wen, D. Chang, A. Thomason, S.K. Yoshinaga, Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2. J. Biol. Chem. 271(7), 3884–3890 (1996)PubMedCrossRef
65.
Zurück zum Zitat J. Baulida, G. Carpenter, Heregulin degradation in the absence of rapid receptor-mediated internalization. Exp. Cell Res. 232(1), 167–172 (1997)PubMedCrossRef J. Baulida, G. Carpenter, Heregulin degradation in the absence of rapid receptor-mediated internalization. Exp. Cell Res. 232(1), 167–172 (1997)PubMedCrossRef
66.
Zurück zum Zitat Z. Wang, L. Zhang, T.K. Yeung, X. Chen, Endocytosis deficiency of epidermal growth factor (EGF) receptor-ErbB2 heterodimers in response to EGF stimulation. Mol. Biol. Cell 10(5), 1621–1636 (1999)PubMed Z. Wang, L. Zhang, T.K. Yeung, X. Chen, Endocytosis deficiency of epidermal growth factor (EGF) receptor-ErbB2 heterodimers in response to EGF stimulation. Mol. Biol. Cell 10(5), 1621–1636 (1999)PubMed
67.
Zurück zum Zitat H. Waterman, I. Sabanai, B. Geiger, Y. Yarden, Alternative intracellular routing of ErbB receptors may determine signaling potency. J. Biol. Chem. 273(22), 13819–13827 (1998)PubMedCrossRef H. Waterman, I. Sabanai, B. Geiger, Y. Yarden, Alternative intracellular routing of ErbB receptors may determine signaling potency. J. Biol. Chem. 273(22), 13819–13827 (1998)PubMedCrossRef
68.
Zurück zum Zitat A.E. Lenferink, R. Pinkas-Kramarski, M.L. van de Poll, M.J. van Vugt, L.N. Klapper, E. Tzahar, H. Waterman, M. Sela, E.J. van Zoelen, Y. Yarden, Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers. EMBO J. 17(12), 3385–3397 (1998)PubMedCrossRef A.E. Lenferink, R. Pinkas-Kramarski, M.L. van de Poll, M.J. van Vugt, L.N. Klapper, E. Tzahar, H. Waterman, M. Sela, E.J. van Zoelen, Y. Yarden, Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers. EMBO J. 17(12), 3385–3397 (1998)PubMedCrossRef
69.
Zurück zum Zitat R. Zandi, A.B. Larsen, P. Andersen, M.T. Stockhausen, H.S. Poulsen, Mechanisms for oncogenic activation of the epidermal growth factor receptor. Cell. Signal. 19(10), 2013–2023 (2007)PubMedCrossRef R. Zandi, A.B. Larsen, P. Andersen, M.T. Stockhausen, H.S. Poulsen, Mechanisms for oncogenic activation of the epidermal growth factor receptor. Cell. Signal. 19(10), 2013–2023 (2007)PubMedCrossRef
70.
Zurück zum Zitat E. Peles, R. Ben-Levy, E. Tzahar, N. Liu, D. Wen, Y. Yarden, Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships. EMBO J. 12(3), 961–971 (1993)PubMed E. Peles, R. Ben-Levy, E. Tzahar, N. Liu, D. Wen, Y. Yarden, Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships. EMBO J. 12(3), 961–971 (1993)PubMed
71.
Zurück zum Zitat G.D. Plowman, J.M. Green, J.M. Culouscou, G.W. Carlton, V.M. Rothwell, S. Buckley, Heregulin induces tyrosine phosphorylation of HER4/p180erbB4. Nature 366(6454), 473–475 (1993)PubMedCrossRef G.D. Plowman, J.M. Green, J.M. Culouscou, G.W. Carlton, V.M. Rothwell, S. Buckley, Heregulin induces tyrosine phosphorylation of HER4/p180erbB4. Nature 366(6454), 473–475 (1993)PubMedCrossRef
72.
Zurück zum Zitat M.X. Sliwkowski, G. Schaefer, R.W. Akita, J.A. Lofgren, V.D. Fitzpatrick, A. Nuijens, B.M. Fendly, R.A. Cerione, R.L. Vandlen, K.L. Carraway 3rd, Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J. Biol. Chem. 269(20), 14661–14665 (1994)PubMed M.X. Sliwkowski, G. Schaefer, R.W. Akita, J.A. Lofgren, V.D. Fitzpatrick, A. Nuijens, B.M. Fendly, R.A. Cerione, R.L. Vandlen, K.L. Carraway 3rd, Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J. Biol. Chem. 269(20), 14661–14665 (1994)PubMed
73.
Zurück zum Zitat X. Qian, C.M. LeVea, J.K. Freeman, W.C. Dougall, M.I. Greene, Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation. Proc. Natl. Acad. Sci. USA 91(4), 1500–1504 (1994)PubMedCrossRef X. Qian, C.M. LeVea, J.K. Freeman, W.C. Dougall, M.I. Greene, Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation. Proc. Natl. Acad. Sci. USA 91(4), 1500–1504 (1994)PubMedCrossRef
74.
Zurück zum Zitat S. Gavi, D. Yin, E. Shumay, H.Y. Wang, C.C. Malbon, Insulin-like growth factor-I provokes functional antagonism and internalization of beta1-adrenergic receptors. Endocrinology 148(6), 2653–2662 (2007)PubMedCrossRef S. Gavi, D. Yin, E. Shumay, H.Y. Wang, C.C. Malbon, Insulin-like growth factor-I provokes functional antagonism and internalization of beta1-adrenergic receptors. Endocrinology 148(6), 2653–2662 (2007)PubMedCrossRef
75.
Zurück zum Zitat F.S. Lee, Novel crosstalk between G protein-coupled receptors and NMDA receptors. Exp. Neurol. 183(2), 269–272 (2003)PubMedCrossRef F.S. Lee, Novel crosstalk between G protein-coupled receptors and NMDA receptors. Exp. Neurol. 183(2), 269–272 (2003)PubMedCrossRef
76.
Zurück zum Zitat J.A. Garcia-Sainz, M.T. Romero-Avila, C. Medina Ldel, Dissecting how receptor tyrosine kinases modulate G protein-coupled receptor function. Eur. J. Pharmacol. 648(1–3), 1–5 (2010)PubMedCrossRef J.A. Garcia-Sainz, M.T. Romero-Avila, C. Medina Ldel, Dissecting how receptor tyrosine kinases modulate G protein-coupled receptor function. Eur. J. Pharmacol. 648(1–3), 1–5 (2010)PubMedCrossRef
77.
Zurück zum Zitat U. Kumar, S.I. Grigorakis, H.L. Watt, R. Sasi, L. Snell, P. Watson, S. Chaudhari, Somatostatin receptors in primary human breast cancer: quantitative analysis of mRNA for subtypes 1–5 and correlation with receptor protein expression and tumor pathology. Breast Cancer Res. Treat. 92(2), 175–186 (2005)PubMedCrossRef U. Kumar, S.I. Grigorakis, H.L. Watt, R. Sasi, L. Snell, P. Watson, S. Chaudhari, Somatostatin receptors in primary human breast cancer: quantitative analysis of mRNA for subtypes 1–5 and correlation with receptor protein expression and tumor pathology. Breast Cancer Res. Treat. 92(2), 175–186 (2005)PubMedCrossRef
78.
Zurück zum Zitat H.L. Watt, U. Kumar, Colocalization of somatostatin receptors and epidermal growth factor receptors in breast cancer cells. Cancer Cell. Int. 6, 5 (2006)PubMedCrossRef H.L. Watt, U. Kumar, Colocalization of somatostatin receptors and epidermal growth factor receptors in breast cancer cells. Cancer Cell. Int. 6, 5 (2006)PubMedCrossRef
79.
Zurück zum Zitat J. Held-Feindt, F. Forstreuter, T. Pufe, R. Mentlein, Influence of the somatostatin receptor sst2 on growth factor signal cascades in human glioma cells. Brain Res. Mol. Brain Res. 87(1), 12–21 (2001)PubMedCrossRef J. Held-Feindt, F. Forstreuter, T. Pufe, R. Mentlein, Influence of the somatostatin receptor sst2 on growth factor signal cascades in human glioma cells. Brain Res. Mol. Brain Res. 87(1), 12–21 (2001)PubMedCrossRef
80.
Zurück zum Zitat M.T. Lee, C. Liebow, A.R. Kamer, A.V. Schally, Effects of epidermal growth factor and analogues of luteinizing hormone-releasing hormone and somatostatin on phosphorylation and dephosphorylation of tyrosine residues of specific protein substrates in various tumors. Proc. Natl. Acad. Sci. USA 88(5), 1656–1660 (1991)PubMedCrossRef M.T. Lee, C. Liebow, A.R. Kamer, A.V. Schally, Effects of epidermal growth factor and analogues of luteinizing hormone-releasing hormone and somatostatin on phosphorylation and dephosphorylation of tyrosine residues of specific protein substrates in various tumors. Proc. Natl. Acad. Sci. USA 88(5), 1656–1660 (1991)PubMedCrossRef
81.
Zurück zum Zitat S. Hart, O.M. Fischer, N. Prenzel, E. Zwick-Wallasch, M. Schneider, L. Hennighausen, A. Ullrich, GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways. Biol. Chem. 386(9), 845–855 (2005)PubMedCrossRef S. Hart, O.M. Fischer, N. Prenzel, E. Zwick-Wallasch, M. Schneider, L. Hennighausen, A. Ullrich, GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways. Biol. Chem. 386(9), 845–855 (2005)PubMedCrossRef
82.
Zurück zum Zitat E.J. Filardo, J.A. Quinn, K.I. Bland, A.R. Frackelton Jr., Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF. Mol. Endocrinol. 14(10), 1649–1660 (2000)PubMedCrossRef E.J. Filardo, J.A. Quinn, K.I. Bland, A.R. Frackelton Jr., Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF. Mol. Endocrinol. 14(10), 1649–1660 (2000)PubMedCrossRef
83.
Zurück zum Zitat N. Prenzel, E. Zwick, H. Daub, M. Leserer, R. Abraham, C. Wallasch, A. Ullrich, EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402(6764), 884–888 (1999)PubMed N. Prenzel, E. Zwick, H. Daub, M. Leserer, R. Abraham, C. Wallasch, A. Ullrich, EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402(6764), 884–888 (1999)PubMed
84.
Zurück zum Zitat H. Daub, F.U. Weiss, C. Wallash, A. Ullrich, Role of transactivation of the EGF receptor in signalling by G-protein coupled receptors. Nature 379, 557–560 (1996)PubMedCrossRef H. Daub, F.U. Weiss, C. Wallash, A. Ullrich, Role of transactivation of the EGF receptor in signalling by G-protein coupled receptors. Nature 379, 557–560 (1996)PubMedCrossRef
85.
Zurück zum Zitat D. Darmoul, V. Gratio, H. Devaud, M. Laburthe, Protease-activated receptor 2 in colon cancer: trypsin-induced MAPK phosphorylation and cell proliferation are mediated by epidermal growth factor receptor transactivation. J. Biol. Chem. 279(20), 20927–20934 (2004)PubMedCrossRef D. Darmoul, V. Gratio, H. Devaud, M. Laburthe, Protease-activated receptor 2 in colon cancer: trypsin-induced MAPK phosphorylation and cell proliferation are mediated by epidermal growth factor receptor transactivation. J. Biol. Chem. 279(20), 20927–20934 (2004)PubMedCrossRef
86.
Zurück zum Zitat H. Shankaran, H.S. Wiley, H. Resat, Modeling the effects of HER/ErbB1–3 coexpression on receptor dimerization and biological response. Biophys. J. 90(11), 3993–4009 (2006)PubMedCrossRef H. Shankaran, H.S. Wiley, H. Resat, Modeling the effects of HER/ErbB1–3 coexpression on receptor dimerization and biological response. Biophys. J. 90(11), 3993–4009 (2006)PubMedCrossRef
87.
Zurück zum Zitat N.E. Willmarth, A. Baillo, M.L. Dziubinski, K. Wilson, D.J. Riese Ii, S.P. Ethier, Altered EGFR localization and degradation in human breast cancer cells with an amphiregulin/EGFR autocrine loop. Cell. Signal. 21(2), 212–219 (2009)PubMedCrossRef N.E. Willmarth, A. Baillo, M.L. Dziubinski, K. Wilson, D.J. Riese Ii, S.P. Ethier, Altered EGFR localization and degradation in human breast cancer cells with an amphiregulin/EGFR autocrine loop. Cell. Signal. 21(2), 212–219 (2009)PubMedCrossRef
88.
Zurück zum Zitat N. Moghal, P.W. Sternberg, Multiple positive and negative regulators of signaling by the EGF-receptor. Curr. Opin. Cell Biol. 11(2), 190–196 (1999)PubMedCrossRef N. Moghal, P.W. Sternberg, Multiple positive and negative regulators of signaling by the EGF-receptor. Curr. Opin. Cell Biol. 11(2), 190–196 (1999)PubMedCrossRef
89.
Zurück zum Zitat W.J. Wu, S. Tu, R.A. Cerione, Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell 114(6), 715–725 (2003)PubMedCrossRef W.J. Wu, S. Tu, R.A. Cerione, Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell 114(6), 715–725 (2003)PubMedCrossRef
90.
Zurück zum Zitat T. Fukazawa, S. Miyake, V. Band, H. Band, Tyrosine phosphorylation of Cbl upon epidermal growth factor (EGF) stimulation and its association with EGF receptor and downstream signaling proteins. J. Biol. Chem. 271(24), 14554–14559 (1996)PubMedCrossRef T. Fukazawa, S. Miyake, V. Band, H. Band, Tyrosine phosphorylation of Cbl upon epidermal growth factor (EGF) stimulation and its association with EGF receptor and downstream signaling proteins. J. Biol. Chem. 271(24), 14554–14559 (1996)PubMedCrossRef
91.
Zurück zum Zitat T. Florio, S. Thellung, S. Arena, A. Corsaro, A. Bajetto, G. Schettini, P.J. Stork, Somatostatin receptor 1 (SSTR1)-mediated inhibition of cell proliferation correlates with the activation of the MAP kinase cascade: role of the phosphotyrosine phosphatase SHP-2. J. Physiol. Paris 94(3–4), 239–250 (2000)PubMedCrossRef T. Florio, S. Thellung, S. Arena, A. Corsaro, A. Bajetto, G. Schettini, P.J. Stork, Somatostatin receptor 1 (SSTR1)-mediated inhibition of cell proliferation correlates with the activation of the MAP kinase cascade: role of the phosphotyrosine phosphatase SHP-2. J. Physiol. Paris 94(3–4), 239–250 (2000)PubMedCrossRef
92.
Zurück zum Zitat T. Florio, H. Yao, K.D. Carey, T.J. Dillon, P.J. Stork, Somatostatin activation of mitogen-activated protein kinase via somatostatin receptor 1 (SSTR1). Mol. Endocrinol. 13(1), 24–37 (1999)PubMedCrossRef T. Florio, H. Yao, K.D. Carey, T.J. Dillon, P.J. Stork, Somatostatin activation of mitogen-activated protein kinase via somatostatin receptor 1 (SSTR1). Mol. Endocrinol. 13(1), 24–37 (1999)PubMedCrossRef
93.
Zurück zum Zitat H. Lahlou, N. Saint-Laurent, J.P. Esteve, A. Eychene, L. Pradayrol, S. Pyronnet, C. Susini, sst2 Somatostatin receptor inhibits cell proliferation through Ras-, Rap1-, and B-Raf-dependent ERK2 activation. J. Biol. Chem. 278(41), 39356–39371 (2003)PubMedCrossRef H. Lahlou, N. Saint-Laurent, J.P. Esteve, A. Eychene, L. Pradayrol, S. Pyronnet, C. Susini, sst2 Somatostatin receptor inhibits cell proliferation through Ras-, Rap1-, and B-Raf-dependent ERK2 activation. J. Biol. Chem. 278(41), 39356–39371 (2003)PubMedCrossRef
94.
Zurück zum Zitat A. Esparis-Ogando, E. Diaz-Rodriguez, J.C. Montero, L. Yuste, P. Crespo, A. Pandiella, Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2. Mol. Cell. Biol. 22(1), 270–285 (2002)PubMedCrossRef A. Esparis-Ogando, E. Diaz-Rodriguez, J.C. Montero, L. Yuste, P. Crespo, A. Pandiella, Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2. Mol. Cell. Biol. 22(1), 270–285 (2002)PubMedCrossRef
95.
Zurück zum Zitat J.C. Montero, A. Ocana, M. Abad, M.J. Ortiz-Ruiz, A. Pandiella, A. Esparis-Ogando, Expression of Erk5 in early stage breast cancer and association with disease free survival identifies this kinase as a potential therapeutic target. PLoS One 4(5), e5565 (2009)PubMedCrossRef J.C. Montero, A. Ocana, M. Abad, M.J. Ortiz-Ruiz, A. Pandiella, A. Esparis-Ogando, Expression of Erk5 in early stage breast cancer and association with disease free survival identifies this kinase as a potential therapeutic target. PLoS One 4(5), e5565 (2009)PubMedCrossRef
96.
Zurück zum Zitat N.E. Hynes, J.H. Dey, PI3K inhibition overcomes trastuzumab resistance: blockade of ErbB2/ErbB3 is not always enough. Cancer Cell 15(5), 353–355 (2009)PubMedCrossRef N.E. Hynes, J.H. Dey, PI3K inhibition overcomes trastuzumab resistance: blockade of ErbB2/ErbB3 is not always enough. Cancer Cell 15(5), 353–355 (2009)PubMedCrossRef
97.
Zurück zum Zitat B.N. Rexer, R. Ghosh, C.L. Arteaga, Inhibition of PI3K and MEK: it is all about combinations and biomarkers. Clin. Cancer Res. 15(14), 4518–4520 (2009)PubMedCrossRef B.N. Rexer, R. Ghosh, C.L. Arteaga, Inhibition of PI3K and MEK: it is all about combinations and biomarkers. Clin. Cancer Res. 15(14), 4518–4520 (2009)PubMedCrossRef
98.
Zurück zum Zitat B.N. Rexer, J.A. Engelman, C.L. Arteaga, Overcoming resistance to tyrosine kinase inhibitors: lessons learned from cancer cells treated with EGFR antagonists. Cell Cycle 8(1), 18–22 (2009)PubMedCrossRef B.N. Rexer, J.A. Engelman, C.L. Arteaga, Overcoming resistance to tyrosine kinase inhibitors: lessons learned from cancer cells treated with EGFR antagonists. Cell Cycle 8(1), 18–22 (2009)PubMedCrossRef
99.
Zurück zum Zitat K. Berns, H.M. Horlings, B.T. Hennessy, M. Madiredjo, E.M. Hijmans, K. Beelen, S.C. Linn, A.M. Gonzalez-Angulo, K. Stemke-Hale, M. Hauptmann, R.L. Beijersbergen, G.B. Mills, M.J. van de Vijver, R. Bernards, A functional genetic approach identifies the PI3K pathway as a major determinant of trastuzumab resistance in breast cancer. Cancer Cell 12(4), 395–402 (2007)PubMedCrossRef K. Berns, H.M. Horlings, B.T. Hennessy, M. Madiredjo, E.M. Hijmans, K. Beelen, S.C. Linn, A.M. Gonzalez-Angulo, K. Stemke-Hale, M. Hauptmann, R.L. Beijersbergen, G.B. Mills, M.J. van de Vijver, R. Bernards, A functional genetic approach identifies the PI3K pathway as a major determinant of trastuzumab resistance in breast cancer. Cancer Cell 12(4), 395–402 (2007)PubMedCrossRef
100.
Zurück zum Zitat C.B. Srikant, S.H. Shen, Octapeptide somatostatin analog SMS 201–995 induces translocation of intracellular PTP1C to membranes in MCF-7 human breast adenocarcinoma cells. Endocrinology 137(8), 3461–3468 (1996)PubMedCrossRef C.B. Srikant, S.H. Shen, Octapeptide somatostatin analog SMS 201–995 induces translocation of intracellular PTP1C to membranes in MCF-7 human breast adenocarcinoma cells. Endocrinology 137(8), 3461–3468 (1996)PubMedCrossRef
101.
Zurück zum Zitat C. Susini, L. Buscail, Rationale for the use of somatostatin analogs as antitumor agents. Ann. Oncol. 17(12), 1733–1742 (2006)PubMedCrossRef C. Susini, L. Buscail, Rationale for the use of somatostatin analogs as antitumor agents. Ann. Oncol. 17(12), 1733–1742 (2006)PubMedCrossRef
102.
Zurück zum Zitat M.P. Sanderson, P.J. Dempsey, A.J. Dunbar, Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGF-like factors. Growth Factors 24(2), 121–136 (2006)PubMedCrossRef M.P. Sanderson, P.J. Dempsey, A.J. Dunbar, Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGF-like factors. Growth Factors 24(2), 121–136 (2006)PubMedCrossRef
Metadaten
Titel
Cross-talk and modulation of signaling between somatostatin and growth factor receptors
verfasst von
Ujendra Kumar
Publikationsdatum
01.10.2011
Verlag
Springer US
Erschienen in
Endocrine / Ausgabe 2/2011
Print ISSN: 1355-008X
Elektronische ISSN: 1559-0100
DOI
https://doi.org/10.1007/s12020-011-9524-8

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Notfall-TEP der Hüfte ist auch bei 90-Jährigen machbar

26.04.2024 Hüft-TEP Nachrichten

Ob bei einer Notfalloperation nach Schenkelhalsfraktur eine Hemiarthroplastik oder eine totale Endoprothese (TEP) eingebaut wird, sollte nicht allein vom Alter der Patientinnen und Patienten abhängen. Auch über 90-Jährige können von der TEP profitieren.

Niedriger diastolischer Blutdruck erhöht Risiko für schwere kardiovaskuläre Komplikationen

25.04.2024 Hypotonie Nachrichten

Wenn unter einer medikamentösen Hochdrucktherapie der diastolische Blutdruck in den Keller geht, steigt das Risiko für schwere kardiovaskuläre Ereignisse: Darauf deutet eine Sekundäranalyse der SPRINT-Studie hin.

Bei schweren Reaktionen auf Insektenstiche empfiehlt sich eine spezifische Immuntherapie

Insektenstiche sind bei Erwachsenen die häufigsten Auslöser einer Anaphylaxie. Einen wirksamen Schutz vor schweren anaphylaktischen Reaktionen bietet die allergenspezifische Immuntherapie. Jedoch kommt sie noch viel zu selten zum Einsatz.

Therapiestart mit Blutdrucksenkern erhöht Frakturrisiko

25.04.2024 Hypertonie Nachrichten

Beginnen ältere Männer im Pflegeheim eine Antihypertensiva-Therapie, dann ist die Frakturrate in den folgenden 30 Tagen mehr als verdoppelt. Besonders häufig stürzen Demenzkranke und Männer, die erstmals Blutdrucksenker nehmen. Dafür spricht eine Analyse unter US-Veteranen.

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