A bifunctional targeted peptide that blocks HER-2 tyrosine kinase and disables mitochondrial function in HER-2-positive carcinoma cells

Cancer Research

Volumn 65, Issue 15, 2005, Pages 6891-6900

  Fantin, Valeria R ^a   Berardi, Marcelo J ^b   Babbe, Holger ^a   Michelman, Montserrat V ^a   Manning, Charlene M ^a,c   Leder, Philip ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c GENZYME CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BIFUNCTIONAL HER 2 BLOCKING AND APOPTOSIS INDUCING PEPTIDE; BIOTIN; CHIMERIC PROTEIN; COMPLEMENTARY DNA; CYTOCHROME C; EPIDERMAL GROWTH FACTOR RECEPTOR 2; HYBRID PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE C GAMMA; PROTEIN KINASE B; STREPTAVIDIN; TRASTUZUMAB; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; BREAST CANCER; CARCINOMA CELL; CELL LYSATE; CELL PROLIFERATION; CONTROLLED STUDY; DRUG DISTRIBUTION; DRUG EFFICACY; DRUG TARGETING; ENDOCYTOSIS; FEMALE; FLOW CYTOMETRY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IN VITRO STUDY; INTERNALIZATION; MITOCHONDRION; MOUSE; NONHUMAN; ONCOGENE NEU; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; ANTINEOPLASTIC AGENTS; APOPTOSIS; BREAST NEOPLASMS; CELL GROWTH PROCESSES; CELL LINE, TUMOR; FEMALE; HUMANS; MICE; MICE, SCID; MITOCHONDRIA; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, ERBB-2; RECOMBINANT FUSION PROTEINS; XENOGRAFT MODEL ANTITUMOR ASSAYS;

EID: 23044434655     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-0395     Document Type: Article

References (48)

1. Neve RM, Lane HA, Hynes NE. The role of overexpressed HER2 in transformation. Ann Oncol 2001;12: S9-13.
2. Hynes NE, Stern DF. The biology of erbB-2/neu/HER-2 and its role in cancer. Biochim Biophys Acta 1994;1198: 165-84.
3. Rubin I, Yarden Y. The basic biology of HER2. Ann Oncol 2001;12:83-8.
4. Stern DF. Tyrosine kinase signalling in breast cancer: ErbB family receptor tyrosine kinases. Breast Cancer Res 2000;2:176-83.
5. Slamon DJ, Leyland-Jones B, Shak S, et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N Engl J Med 2001;344:783-92.
6. Arteaga CL. Inhibiting tyrosine kinases: successes and limitations. Cancer Biol Ther 2003;2:S79-83.
7. Albanell J, Baselga J. Unraveling resistance to trastuzumab (Herceptin): insulin-like growth factor-1 receptor, a new suspect. J Natl Cancer Inst 2001;93:1830-2.
8. Holbro T, Hynes NE. ErbB receptors: directing key signaling networks throughout life. Annu Rev Pharmacol Toxicol 2004;44:195-217.
9. Smith BL, Chin D, Maltzman W, Crosby K, Hortobagyi GN, Bacus SS. The efficacy of Herceptin therapies is influenced by the expression of other erbB receptors, their ligands and the activation of downstream signalling proteins. Br J Cancer 2004;91:1190-4.
10. Nahta R, Takahashi T, Ueno NT, Hung MC, Esteva FJ. P27(kip1) down-regulation is associated with trastuzumab resistance in breast cancer cells. Cancer Res 2004;64:3981-6.
11. Nagata Y, Lan KH, Zhou X, et al. PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients. Cancer Cell 2004;6:117-27.
12. Miller KD. The role of ErbB inhibitors in trastuzumab resistance. Oncologist 2004;9 Suppl 3:16-9.
13. Park BW, Zhang HT, Wu C, et al. Rationally designed anti-HER2/neu peptide mimetic disables P185HER2/neu tyrosine kinases in vitro and in vivo. Nat Biotechnol 2000;18:194-8.
14. Berezov A, Zhang HT, Greene MI, Murali R. Disabling erbB receptors with rationally designed exocyclic mimetics of antibodies: structure-function analysis. J Med Chem 2001;44:2565-74.
15. Javadpour MM, Juban MM, Lo WC, et al. De novo antimicrobial peptides with low mammalian cell toxicity. J Med Chem 1996;39:3107-13.
16. Ellerby HM, Martin SJ, Ellerby LM, et al. Establishment of a cell-free system of neuronal apoptosis: comparison of premitochondrial, mitochondrial, and postmitochondrial phases. J Neurosci 1997;17:6165-78.
17. del Rio G, Castro-Obregon S, Rao R, Ellerby HM, Bredesen DE. APAP, a sequence-pattern recognition approach identifies substance P as a potential apoptotic peptide. FEBS Lett 2001;494:213-9.
18. Ellerby HM, Arap W, Ellerby LM, et al. Anti-cancer activity of targeted pro-apoptotic peptides. Nat Med 1999;5:1032-8.
19. Kolonin MG, Saha PK, Chan L, Pasqualini R, Arap W. Reversal of obesity by targeted ablation of adipose tissue. Nat Med 2004;10:625-32.
20. Matsuzaki K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim Biophys Acta 1998;1376:391-400.
21. Yakes FM, Chinratanalab W, Ritter CA, King W, Seelig S, Arteaga CL. Herceptin-induced inhibition of phosphatidylinositol-3 kinase and Akt is required for antibody-mediated effects on p27, cyclin D1, and antitumor action. Cancer Res 2002;62:4132-41.
22. Bessalle R, Kapitkovsky A, Gorea A, Shalit I, Fridkin M. All-D-magainin: chirality, antimicrobial activity and proteolytic resistance. FEBS Lett 1990;274:151-5.
23. Coussens L, Yang-Feng TL, Liao YC, et al. Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene. Science 1985;230:1132-9.
24. Fantin VR, Berardi MJ, Scorrano L, Korsmeyer SJ, Leder P. A novel mitochondriotoxic small molecule that selectively inhibits tumor cell growth. Cancer Cell 2002; 2:29-42.
25. Costantini P, Petronilli V, Colonna R, Bernardi P. On the effects of paraquat on isolated mitochondria. Evidence that paraquat causes opening of the cyclosporin A-sensitive permeability transition pore synergistically with nitric oxide. Toxicology 1995;99:77-88.
26. Thomas DA, Scorrano L, Putcha GV, Korsmeyer SJ, Ley TJ. Granzyme B can cause mitochondrial depolarization and cell death in the absence of BID, BAX BAK. Proc Natl Acad Sci U S A 2001;98:14985-90.
27. Fantin VR, Leder P. F16, a mitochondriotoxic compound, triggers apoptosis or necrosis depending on the genetic background of the target carcinoma cell. Cancer Res 2004;64:329-36.
28. Griffiths G. Fine structure immunocytochemistry. Heidelberg (Germany): Spinger Verlag, 1993.
29. Moulder SL, Yakes FM, Muthuswamy SK, Bianco R, Simpson JF, Arteaga CL. Epidermal growth factor receptor (HER1) tyrosine kinase inhibitor ZD1839 (Iressa) inhibits HER2/neu (erbB2)-overexpressing breast cancer cells in vitro and in vivo. Cancer Res 2001;61:8887-95.
30. Shah BH, Alberto Olivares-Reyes J, Yesilkaya A, Catt KJ. Independence of angiotensin 11-induced MAP kinase activation from angiotensin type 1 receptor internalization in clone 9 hepatocytes. Mol Endocrinol 2002;16: 610-20.
31. Waterman H, Yarden Y. Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases. FEBS Lett 2001;490:142-52.
32. Motoyama AB, Hynes NE, Lane HA. The efficacy of ErbB receptor-targeted anticancer therapeutics is influenced by the availability of epidermal growth factor-related peptides. Cancer Res 2002;62:3151-8.
33. Green D, Kroemer G. The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol 1998;8:267-71.
34. Scorrano L, Korsmeyer SJ. Mechanisms of cytochrome c release by proapoptotic BCL-2 family members. Biochem Biophys Res Commun 2003;304:437-44.
35. Avrantinis SK, Stafford RL, Tian X, Weiss GA. Dissecting the streptavidin-biotin interaction by phage-displayed shotgun scanning. Chembiochem 2002;3: 1229-34.
36. Newmeyer DD, Ferguson-Miller S. Mitochondria. Releasing power for life and unleashing the machineries of death. Cell 2003;112:481-90.
37. Costantini P, Jacotot E, Decaudin D, Kroemer G. Mitochondrion as a novel target of anticancer chemotherapy. J Natl Cancer Inst 2000;92:1042-53.
38. Don AS, Hogg PJ. Mitochondria as cancer drug targets. Trends Mol Med 2004;10:372-8.
39. Cory S, Adams JM. The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2002; 2:547-56.
40. Kolenko V, Uzzo RG, Bukowski R, et al. Dead or dying: necrosis versus apoptosis in caspase-deficient human renal cell carcinoma. Cancer Res 1999;59:2838-42.
41. Vogelstein B, Lane D, Levine AJ. Surfing the p53 network. Nature 2000;408:307-10.
42. Cho YW, Kim JD, Park K. Polycation gene delivery systems: escape from endosomes to cytosol. J Pharm Pharmacol 2003;55:721-34.
43. Tachibana R, Harashima H, Shono M, et al. Intracellular regulation of macromolecules using pH-sensitive liposomes and nuclear localization signal: qualitative and quantitative evaluation of intracellular trafficking. Biochem Biophys Res Commun 1998;251:538-44.
44. Altman JD, Moss PA, Goulder PJ, et al. Phenotypic analysis of antigen-specific T lymphocytes. Science 1996; 274:94-6.
45. Grimm KM, Trigona WL, Heidecker GJ, et al. An enhanced and scalable process for the purification of SIV Gag-specific MHC tetramer. Protein Expr Purif 2001; 23:270-81.
46. Ross J, Gray K, Schenkein D, et al. Antibody-based therapeutics in oncology. Expert Rev Anticancer Ther 2003;3:107-21.
47. Mandler R, Kobayashi H, Hinson ER, Brechbiel MW, Waldmann TA. Herceptin-geldanamycin immunoconjugates: pharmacokinetics, biodistribution, and enhanced antitumor activity. Cancer Res 2004;64:1460-7.
48. Gilbert CW, McGowan EB, Seery GB, Black KS, Pegram MD. Targeted prodrug treatment of HER-2-positive breast tumor cells using trastuzumab and paclitaxel linked by A-Z-CINN Linker. J Exp Ther Oncol 2003;3:27-35.