Small peptides as potent mimetics of the protein hormone erythropoietin

Science

Volumn 273, Issue 5274, 1996, Pages 458-463

  Wrighton, Nicholas C ^a   Farrell, Francis X ^b   Chang, Ray ^a   Kashyap, Arun K ^a   Barbone, Francis P ^b   Mulcahy, Linda S ^b   Johnson, Dana L ^b   Barrett, Ronald W ^a   Jolliffe, Linda K ^b   Dower, William J ^a  

^a AFFYMAX RESEARCH INSTITUTE   (United States)

^b Drug Discovery Raritan   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE PLACENTA ISOENZYME; BOVINE SERUM ALBUMIN; CYCLOPEPTIDE; ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; ERYTHROPOIETIN RECEPTOR; INTERLEUKIN 2 RECEPTOR; NERVE GROWTH FACTOR RECEPTOR; PHOSPHOLIPASE C; TUMOR NECROSIS FACTOR RECEPTOR;

AGONIST; AMINO ACID SEQUENCE; ARTICLE; BIOASSAY; CONTROLLED STUDY; ERYTHROPOIESIS; HUMAN; HUMAN CELL; MOLECULAR MIMICRY; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR AFFINITY; RECEPTOR BINDING;

EID: 9444236174     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5274.458     Document Type: Article

References (65)

1. A. M. de Vos, M. Ultsch, A. A. Kossiakoff, Science 255, 306 (1992).
2. T. Clackson and J. A. Wells, ibid. 267, 383 (1995).
3. M. A. Gallop, R. W. Barrett, W. J. Dower, S. P. Fodor, E. M. Gordon, J. Med. Chem. 37, 1233 (1994).
4. E. M. Gordon, R. W. Barrett, W. J. Dower, S. P. Fodor, M. A. Gallop, ibid. p. 1385.
5. S. E. Cwirla, E. A. Peters, R. W. Barrett, W. J. Dower, Proc. Natl. Acad. Sci. U.S.A. 87, 6378 (1990).
6. J. J. Devlin, L. C. Panganiban, P. E. Devlin, Science 249, 404 (1990).
7. J. Greenwood, A. E. Willis, R. N. Perham, J. Mol. Biol. 220, 821 (1991).
8. J. K. Scott and G. P. Smith, Science 249, 386 (1990).
9. W. Jelkmann, Physiol. Rev. 72, 449 (1992).
10. S. B. Krantz, Blood 77, 419 (1991).
11. J. F. Bazan, Immunol. Today 11, 350 (1990).
12. N. A. Nicola, Ed., Guidebook to Cytokines and Their Receptors (Oxford Univ. Press, New York, 1994).
13. K. T. Landschulz, A. N. Noyes, O. Rogers, S. H. Boyer, Blood 73, 1476 (1989).
14. A. D. D'Andrea, H. F. Lodish, G. G. Wong, Cell 57, 277 (1989).
15. J. F. Bazan, Proc. Natl. Acad. Sci. U.S.A. 87, 6934 (1990).
16. D. Cosman, Cytokine 5, 95 (1993).
17. Single letter amino acid abbreviations: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, lle; K, Lys; L, Leu, M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
18. H. Youssoufian, G. Longmore, D. Neumann, A. Yoshimura, H. F. Lodish, Blood 81, 2223 (1993).
19. S. S. Watowich, D. J. Hilton, H. F. Lodish, Mol. Cell. Biol. 14, 3535 (1994).
20. J. S. Philo, K. H. Aoki, T. Arakawa, L. O. Narhi, J. Wen, Biochemistry 35, 1681 (1996).
21. B. C. Cunningham et al., Science 254, 821 (1991).
22. A. Yoshimura, G. Longmore, H. F. Lodish, Nature 348, 647 (1990).
23. F. W. Quelle and D. M. Wojchowski, J. Biol. Chem. 266, 609 (1991).
24. O. Miura, A. D'Andrea, D. Kabat, J. N. Ihle, Mol. Cell. Biol. 11, 4895 (1991).
25. B. A. Witthuhn et al., Cell 74, 227 (1993).
26. O. Miura et al., Blood 84, 1501 (1994).
27. D. Faulds and E. M. Sorkin, Drugs 38, 863 (1989).
28. P. Foa, Acta Haematol. 86, 162 (1991).
29. O. Livnah et al., Science, this issue (1996).
30. C. L. Martens et al., J. Biol. Chem. 270, 21129 (1995).
31. E. Whitehorn et al., Biotechnology 13, 1215 (1995).
32. S. D. Yanofsky et al., Proc. Natl. Acad. Sci. U.S.A. 93, 7381 (1996).
33. 2+ ions) and heat denaturation of receptor (65°C for 10 minutes - to release phagemids) had no effect on subsequent amplification of recovered phage particles and were thus omitted.
34. 9 individual recombinants.
35. N. C. Wrighton et al., unpublished data.
36. R. W. Barrett et al., Anal. Biochem. 204, 357 (1992).
37. The following conditions were used for affinity enrichment. Round 1 consisted of immediate acid elution after removal of unbound phage by washing (eluted phage were amplified for input into round 2). In rounds 2 and 3, bound phage were incubated with 100 nM EPO at 4°C for 15 minutes, washed, eluted and amplified. In round 4, the procedure was the same as in rounds 2 and 3, except that EPO incubation was at room temperature. In round 5, the EPO incubation was at room temperature for 30 minutes.
38. 8 phage per well was used in this assay. After the phage were bound to the immobilized receptor, the wells were washed with PBS and then either PBS or 100 nM EPO in PBS was added to duplicate wells and incubated for 15 minutes at 4°C, and again washed. The percentage of total ELISA signal (no EPO) remaining in wells receiving EPO was used to rank clones in potential order of affinity. Clone C2/11 was reduced almost to background in this assay.
39. M. P. Carroll et al., J. Biol. Chem. 266, 14964 (1991).
40. S. Ymer et al., Nature 317, 255 (1985).
41. F. X. Farrell et al., unpublished data.
42. T. Kitamura et al., J. Cell. Physiol 140, 323 (1989).
43. J. S. Greenberger, M. A. Sakakeeny, R. K. Humphries, C. J. Eaves, R. J. Eckner, Proc. Natl. Acad. Sci. U.S.A. 80, 2931 (1983).
44. G. C. Avanzi et al., Br. J. Haematol. 69, 359 (1988).
45. B. Lange et al., Blood 70, 192 (1987).
46. H. C. Freake, C. Marcocci, J. Iwasaki, I. Maclntyre, Biochem. Biophys. Res. Commun. 101, 1131 (1981).
47. H. Kodama, Y. Amagai, S. Kasai, S. Yamamoto, Jpn. J. Oral. Biol. 23, 899 (1981).
48. S. Rosen-Bronson, A. H. Johnson, R. J. Hartzman, D. D. Eckels, Immunogenetics 23, 368 (1986).
49. O. Miura et al., Blood 84, 4135 (1994).
50. J. E. Damen, L. Liu, R. L. Cutler, G. Krystal, ibid. 82, 2296 (1993).
51. F. I. Dusanter et al., J. Biol. Chem. 267, 10670 (1992).
52. A. G. Barbone, B. Aparicio, D. W. Anderson, J. Natarajan, D. M. Ritchie, J. Pharmacol. Biomed. Anal. 12, 515 (1994).
53. P. M. Cotes and D. R. Bangham, Nature 191, 1065 (1961).
54. D. L. Johnson et al., unpublished data.
55. P. Babu et al., unpublished data.
56. D. L. Johnson et al., Protein Express. Purif. 7, 104 (1996).
57. Human bone marrow samples were obtained from compensated, volunteer donors with informed consent.
58. StemCell Technologies, Vancouver, BC.
59. Recombinant human erythropoietin (120 U/μg) was obtained from Biopharmaceutical Development, R. W. Johnson Pharmaceutical Research Institute.
60. A. DeLean, P. J. Munson, D. Rodbard, Am. J. Physiol. 235, E97 (1978).
61. T. Mosmann, J. Immunol. Methods 65, 55 (1983).
62. All animal procedures were approved by the Institutional Animal Care and Use Committee of the R. W. Johnson Pharmaceutical Research Institute.
63. 59Fe).
64. L.-M. Guzman, D. Belin, M. J. Carson, J. Beckwith, J. Bacteriol. 177, 4121 (1995).
65. For technical help and advice we thank the following members of Affymax Research Institute: S. Cwirla, A. Davis, D. Duffin, E. Tate, E. Whitehorn, and those in the DNA core group. We also thank the following members of the R. W. Johnson Pharmaceutical Research Institute: J. Tullai, A. Barbone, J. Schnell, F. McMahon (technical assistance), Ortho Biotech Bioassay Group (exhypoxic bioassay), and K. Hoey (peptide synthesis).