HER-2/neu signal transduction in human breast and ovarian cancer

Stem Cells

Volumn 15, Issue 1, 1997, Pages 1-8

  Reese, David M ^a   Slamon, Dennis J ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Breast cancer; Epidermal growth factor; erbB receptors; HER 2 neu; Heregulin; Ovarian cancer; Signal transduction

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE C; PROTEIN TYROSINE KINASE;

BREAST CANCER; GENE EXPRESSION REGULATION; GENE INDUCTION; HUMAN; HUMAN TISSUE; ONCOGENE NEU; OVARY CANCER; POINT MUTATION; PROTEIN PHOSPHORYLATION; PROTO ONCOGENE; RECEPTOR GENE; REVIEW; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

EID: 0031034106     PISSN: 10665099     EISSN: None     Source Type: Journal    
DOI: 10.1002/stem.150001     Document Type: Review

References (85)

1. Shih C, Padhy L, Murray M et al. Transforming genes of carcinomas and neuroblastomas introduced into mouse fibroblasts. Nature 1981;260:261-264.
2. Bargmann C, Hung M-C, Weinberg R. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell 1986;45:649-657.
3. Slamon DJ, Clark G, Wong S et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/nue oncogene. Science 1987;235:177-181.
4. Slamon DJ, Godolphin W, Jones L et al. Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer. Science 1989;244:707-711.
5. Venter D, Kumar S, Tuzi N et al. Overexpression of the c-erbB-2 oncoprotein in human breast carcinomas: immunohistochemical assessment correlates with gene amplification. Lancet 1987;2:69-72.
6. Natali P, Nicotra M, Brigotti A et al. Expression of the p185 encoded by HER2 oncogene in normal and transformed human tissues. Int J Cancer 1990;45:457-461.
7. Yonemura Y, Ninomiya I, Yamaguchi A et al. Evaluation of immunoreactivity for erbB-2 protein as a marker of poor short-term prognosis in gastric cancer. Cancer Res 1991;51:1034-1038.
8. Press MF, Pike MC, Hung G et al. Amplification and Overexpression of HER-2/neu in carcinomas of the salivary gland: correlation with poor prognosis. Cancer Res 1994;54:5675-5682.
9. Hudziak RM, Schlessinger J, Ullrich A. Increased expression of the putative growth factor receptor p185 HER2 causes transformation and tumor genesis of NIH 3T3 cells. Proc Natl Acad Sci USA 1987;84:7159-7163.
10. Di Fiore P, Pierce J, Kraus M et al. ErbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells. Science 1987;237:178-182.
11. Pietras R, Arboleda J, Reese D et al. HER-2 tyrosine kinase pathway targets estrogen receptor and promotes hormone-independent growth in human breast cancer cells. Oncogene 1995;10:2345-2446.
12. Schlessinger J, Ullrich A. Growth factor signalling by receptor tyrosine kinases. Neuron 1992;9:383-391.
13. Fantl W, Johnson D, Williams LT. Signalling by receptor tyrosine kinases. Annu Rev Biochem 1993;62:453-481.
14. Ullrich A, Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990;61:203-212.
15. Earp HS, Dawson TL, Li X et al. Heterodimerization and functional interaction between EGF receptor family members: a new signaling paradigm with implications for breast cancer research. Breast Cancer Res Treat 1995;35:115-132.
16. Carraway K, Cantley L. A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell 1994;78:5-8.
17. Guy PM, Platko JV, Cantley LC et al. Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity. Proc Natl Acad Sci USA 1994;91:8132-8136.
18. Riese D, van Raaij T, Plowman G et al. The cellular response to neuregulins is governed by complex interactions of the erbB receptor family. Mol Cell Biol 1995;15:5770-5776.
19. Kraus MH, Fedi P, Starks V et al. Demonstration of ligand-dependent signaling by the erbB3 tyrosine kinase and its constitutive activation in human breast tumor cells. Proc Natl Acad Sci USA 1993;90:2900-2904.
20. Lin C, Chen W, Lazar C et al. Protein Kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms. Cell 1986;44:839-848.
21. Yarden Y, Schlessinger J. Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry 1987;26:1434-1442.
22. Spivak-Kroizman T, Rotin D, Pinchasi D et al. Hetero-dimerization of c-erbB2 with different epidermal growth factor receptor mutants elicits stimulatory or inhibitory responses. J Biol Chem 1992;267:8056-8063.
23. Weiner DB, Liu J, Cohen JA et al. A point mutation in the neu oncogene mimics ligand induction of receptor aggregation. Nature 1989;339:230-231.
24. neu stimulates tyrosine phosphorylation in vivo. Mol Cell Biol 1988;8:3969-3973.
25. Bargmann C, Weinberg R. Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene. Proc Natl Acad Sci USA 1988;85:5394-5398.
26. Lofts F, Hurst HC, Sternberg MJ et al. Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo. Oncogene 1993;8:2813-2820.
27. Akiyama T, Matsuda S, Namba Y et al. The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain. Mol Cell Biol 1991;11:833-842.
28. DiGiovanna MP, Stem DF. Activation state-specific monoclonal antibody detects tyrosine phosphorylated p185neu/erbB-2 in a subset of human breast tumors overexpressing this receptor. Cancer Res 1995;55:1946-1955.
29. erbB2. Science 1992;256:1205-1210.
30. Peles E, Bacus S, Koski R et al. Isolation of the Neu/HER2 stimulatory ligand: a 44kd glycoprotein that induces differentiation of mammary tumor cells. Cell 1992;69:205-216.
31. Falls DG, Rosen KM, Cortas G et al. ARIA, a protein that stimulates acetylcholine receptor synthesis, is a member of the neu ligand family. Cell 1993;72:801-815.
32. Marchionni MA, Goodearl ADJ, Chen MS et al. Glial growth factors are alternatively spliced erbB2 ligands expressed in the nervous system. Nature 1993;362:312-318.
33. Carraway K, Sliwkowski M, Akita R et al. The erbB3 gene product is a receptor for heregulin. J Biol Chem 1994;269:14303-14306.
34. erbB4. Nature 1993;366:473-475.
35. Sliwkowski M, Schaefer G, Akita R et al. Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J Biol Chem 1994;269:14661-14665.
36. King C, Borrello I, Bellot F et al. EGF binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SKBR3. EMBO J 1988;7:1647-1651.
37. neu protein and EGF receptor modulates EGF receptor function. Cell 1990;61:1339-1347.
38. Qian X, Dougall WC, Hellmann ME et al. Kinase-deficient neu protein suppresses epidermal growth factor receptor function and abolishes cell transformation. Oncogene 1994;9:1507-1514.
39. Graus-Porta D, Beerli R, Hynes N. Single-chain antibody-mediated intracellular retention of erbB-2 impairs neu differentiation factor and epidermal growth factor signaling. Mol Cell Biol 1995;15:1182-1191.
40. Wallasch C, Weiss FU, Niederfellner G et al. Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. EMBO J 1995;14:4267-4275.
41. erbB4, a fourth member of the epidermal growth factor receptor family. Proc Natl Acad Sci USA 1993;90:1746-1750.
42. Chazin V, Kaleko M, Miller A et al. Transformation mediated by the human HER-2 gene independent of the epidermal growth factor receptor. Oncogene 1992;7:1859-1866.
43. Segatto O, Lonardo F, Pierce JH et al. The role of autophosphorylation in modulation of erbB-2 transforming function. New Biol 1990;2:187-195.
44. Mikami Y, Davis J, Dobashi K et al. Carboxyl-terminal deletion and point mutations decrease the transforming potential of the activated rat neu oncogene product. Proc Natl Acad Sci USA 1992;89:7335-7339.
45. Segatto O, Pelicci G, Giuli S et al. She products are substrates for erbB-2 kinase. Oncogene 1993;8:2105-2112.
46. Xie Y, Li K, Hung MC. Tyrosine phosphorylation of she protein and formation of shc/grb2 complex correlate to the transformation of NIH 3T3 cells mediated by the point-mutation activated neu. Oncogene 1995;10:2409-2413.
47. Shawver L, Mann E, Elliger S et al. Ligand-like effects induced by anti-c-erbB-2 antibodies do not correlate with and are not required for growth inhibition of human carcinoma cells. Cancer Res 1994;54:1367-1373.
48. Koch C, Anderson D, Moran M et al. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 1991;252:668-674.
49. Pawson T, Gish D. SH2 and SH3 domains: from structure to function. Cell 1992;71:359-362.
50. Bos JL. Ras oncogenes in human cancer: a review. Cancer Res 1989;49:4682-4689.
51. Johnson G, Vaillancourt R. Sequential protein kinase reactions controlling cell growth and differentiation. Curr Opin Cell Biol 1994;6:230-238.
52. Pelicci G, Lanfrancone L, Grignani J et al. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 1992;70:93-104.
53. Egan SE, Giddings BW, Brooks MW et al. Association of Sos Ras exchange protein with grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 1993;363:45-51.
54. Li N, Batzer A, Daly R et al. Guanine-nucleotide releasing factor hSos1 binds to grb2 and links receptor tyrosine kinases to ras signalling. Nature 1993;368:85-88.
55. Lange-Carter C, Pleiman C, Gardner A et al. A divergence in the MAP kinase regulatory network defined by MEK kinase and raf. Science 1993;260:315-319.
56. Janes PW, Daly RJ, deFazio A et al. Activation of the ras signalling pathway in human breast cancer cells overexpressing erbB-2. Oncogene 1994;9:3601-3608.
57. Levin W. Transcriptional activation in response to the HER-2/neu stimulatory ligand heregulin and inhibitory antibody 4D5 in human breast cancer cells. Master's thesis 1995. University of California, Los Angeles.
58. Kavanaugh WM, Williams LT. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 1994;266:1862-1865.
59. Kavanaugh WM, Turck CW, Williams LT. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 1995;268:1177-1179.
60. Noh DY, Shin SH, Rhee SG. Phosphoinositide-specific phospholipase C and mitogenic signaling. Biochim Biophys Acta 1995;1242:99-113.
61. Fazioli F, Kim U-H, Rhee S et al. The erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-g and GTP-ase activating protein does not correlate with erbB-2 mitogenic potency. Mol Cell Biol 1991;11:2040-2048.
62. Peles E, Ben-Levy R, Or E et al. Oncogenic forms of the neu/HER2 tyrosine kinase are permanently coupled to phospholipase Cg. EMBO J 1991;10:2077-2086.
63. Fry MJ, Waterfield MD. Structure and function of phosphatidylinositol 3-kinase: a potential second messenger in systems involved in growth control. Philos Trans R Soc Lond B Biol Sci 1993;340:337-344.
64. Kapeller R, Cantley LC. Phosphatidylinositol 3-kinase. Bioessays 1994;16:565-576.
65. Peles E, Lamprecht R, Ben-Levy R et al.Regulated coupling of the neu receptor to phosphatidylinositol 3-kinase and its release by oncogenic activation. J Biol Chem 1992;267:12266-12274.
66. Beerli R, Graus-Porta D, Woods-Cook K et al. Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2. Mol Cell Biol 1995;15:6496-6505.
67. Fedi P, Pierce J, Di Fiore P et al. Efficient coupling with phosphatidylinositol 3-kinase, but not phospholipase Cg or GTP-ase activating protein, distinguishes erbB-3 signaling from that of other erbB/EGFR family members. Mol Cell Biol 1994;14:3550-3558.
68. Prigent S, Gullick W, Identification of c-erbB-3 binding sites for phosphatidylinositol 3-kinase and SHC using an EGF receptor/c-erbB-3 chimera. EMBO J 1994;13:2831-2841.
69. Soltoff S, Carraway K, Prigent S et al. ErbB-3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor. Mol Cell Biol 1994;14:3550-3558.
70. Lewin B. Oncogenic conversion by regulatory changes in transcription factors. Cell 1991;64:303-312.
71. Mansour S, Matten W, Hermann A et al. Transformation of mammalian cells by constitutively active MAP kinase kinase. Science 1994;265:966-970.
72. Minden A, Lin A, McMahon M et al. Differential activation of ERK and JNK mitogen-activated protein kinases by raf-1 and MEKK. Science 1994;266:1719-1723.
73. Xia Z, Dickens M, Raingeaud J et al. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 1995;270:1326-1331.
74. Raitano A, Halpern J, Hanbuch T et al. The Bcr-abl leukemia oncogene activates Jun kinase and requires Jun for transformation. Proc Natl Acad Sci USA 1995;92:11746-11750.
75. Barone V, Courtneidge S. Myc but not fos rescue of PDGF signalling block caused by kinase inactive src. Nature 1995;378:509-511.
76. Kumar R, Shepard HM, Mendelsohn J. Regulation of phosphorylation of the c-erbB-2 /HER-2 gene product by a monoclonal antibody and serum growth factors in human mammary carcinoma cells. Mol Cell Biol 1991;11:979-986.
77. HER2 monoclonal antibodies. Cancer Immunol Immunother 1993;37:255-263.
78. Pietras R, Fendly B, Chazin V et al. Antibody to HER-2/neu receptor blocks DNA repair after cisplatin in human breast and ovarian cancer cells. Oncogene 1994;9:1829-1838.
79. HER2 monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis. Mol Cell Biol 1989;9:1165-1172.
80. HER2 for human cancer therapy. Proc Natl Acad Sci USA 1992;89:4285-4289.
81. HER-2 monoclonal antibody (rhuMAb HER-2) plus cisplatin in patients with HER-2/neu overexpressing metastatic breast cancer. Proc Am Soc Clin Oncol 1995;14:103.
82. HER2/neu-overexpressing metastatic breast cancer. J Clin Oncol 1996;14;737-744.
83. HER2 signal transduction in breast cancer cells. J Biol Chem 1991;266:14300-14305.
84. Hawerth I, Wels W, Marte B et al. Monoclonal antibodies against the extracellular domain of the erbB-2 receptor function as partial ligand agonists. J Biol Chem 1992;267:15160-15167.
85. Wada T, Myers J, Kokai Y et al. Anti-receptor antibodies reverse the phenotype of cells transformed by two interacting protooncogene encoded receptor proteins. Oncogene 1990;5:489-495.