Aptamer selection for the inhibition of cell adhesion with fibronectin as target

Bioorganic and Medicinal Chemistry Letters

Volumn 14, Issue 15, 2004, Pages 4001-4004

  Ogawa, Atsushi ^a   Tomita, Naotoshi ^a   Kikuchi, Naoko ^a   Sando, Shinsuke ^a   Aoyama, Yasuhiro ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Aptamer; Cell adhesion; Fibronectin; RGD; SELEX

Indexed keywords

FIBRONECTIN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL ADHESION; CONTROLLED STUDY; EPITOPE MAPPING; GENE SEQUENCE; NONHUMAN; RANDOMIZATION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CELL ADHESION; CELL LINE; CRICETINAE; FIBRONECTINS; KIDNEY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PROTEIN CONFORMATION;

EID: 3042636195     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2004.05.042     Document Type: Article

References (36)

1. Ellington A.D., Szostak J.W. Nature. 346:1990;818-822
2. Tuerk C., Gold L. Science. 249:1990;505-510
3. Joyce G.F. Sci. Am. 267:1992;90-97
4. For recent reviews, see: Breaker R.R. Chem. Rev. 97:1997;371-390
5. Wilson D.S., Szostak J.W. Annu. Rev. Biochem. 68:1999;611-647
6. Famulok M., Mayer G., Blind M. Acc. Chem. Res. 33:2000;591-599
7. Rimmele M. ChemBioChem. 4:2003;963-971
8. For selected recent papers, see: Blind M., Kolanus W., Famulok M. Proc. Natl. Acad. Sci. U.S.A. 96:1999;3606-3610
9. Fukusaki E., Hasunuma T., Kajiyama S., Okazawa A., Itoh T.J., Kobayashi A. Bioorg. Med. Chem. Lett. 11:2001;2927-2930
10. Ohmichi T., Maki A., Kool E.T. Proc. Natl. Acad. Sci. U.S.A. 99:2002;54-59
11. Fahlman R.P., Sen D. J. Am. Chem. Soc. 124:2002;4610-4616
12. Ordoukhanian P., Joyce G.F. J. Am. Chem. Soc. 124:2002;12499-12506
13. Kuzuya A., Mizoguchi R., Morisawa F., Machida K., Komiyama M. J. Am. Chem. Soc. 124:2002;6887-6894
14. Mei S.H.J., Liu Z., Brennan J.D., Li Y. J. Am. Chem. Soc. 125:2003;412-420
15. Buskirk A.R., Kehayova P.D., Landrigan A., Liu D.R. Chem. Biol. 10:2003;533-540
16. Masud M.M., Kuwahara M., Ozaki H., Sawai H. Bioorg. Med. Chem. 12:2004;1111-1120
17. Refs. [2a, c] and references cited therein. Selected other examples are: Jellinek D., Lynott C.K., Rifkin D.B., Janjic N. Proc. Natl. Acad. Sci. U.S.A. 90:1993;11227-11231
18. O'Conell D., Koenig A., Jennings S., Hicke B., Han H.-L., Fitzwater T., Chang Y.-F., Varki N., Parma D., Varki A. Proc. Natl. Acad. Sci. U.S.A. 93:1996;5883-5887
19. Weiss S., Proske D., Neumann M., Groschup M.H., Kretzschmar H.A., Famulok M., Winnacker E.L. J. Virol. 71:1997;8790-8797
20. Xu W., Ellington A.D. Proc. Nat. Acad. Sci. U.S.A. 93:1996;7475-7480
21. Kimoto M., Shirouzu M., Mizutani S., Koide H., Kaziro Y., Hirao I., Yokoyama S. Eur. J. Biochem. 269:2002;697-704
22. For recent reviews on fibronectin, see: Romberger D.J. Int. J. Biochem. Cell. Biol. 29:1997;939-943
23. Ruoslahti E. Adv. Cancer Res. 76:1999;1-20
24. Danen E.H.J., Yamada K.M. J. Cell. Phys. 189:2001;1-13
25. For fibronectin-integrin interactions, see: Rouslahti E. Annu. Rev. Cell. Dev. Biol. 12:1996;697-715
26. Xiong J.-P., Stehle T., Zhang R., Joachimiak A., Frech M., Goodman S.L., Arnaout M.A. Science. 296:2002;151-155
27. The ODN library was prepared on an Applied Biosystems 392 DNA/RNA synthesizer, deprotected, and purified with Poly-pak II Cartridge (GREN RESEARCH)
28. Decapeptide was immobilized on an NHS-activated agarose gel column (Amersham, NHS=N-hydroxysuccinimide) according to the manufacturer's instruction to give an RGD-peptide affinity column
29. Asymmetric PCR was carried out using PCR Master Mix Kit (Qiagen) with 6.7 μM 5′-primer and 0.2 μM 3′-primer. Each PCR consisted of 30 cycles of denaturation at 94°C for 45 s, primer annealing at 60°C for 1 min, and extension at 72°C for 1 min
30. 2) followed by washing with PBS(+) (3 × 300 μL). Selection in subsequent cycles utilized severer conditions, that is, shorter incubation times (1.5, 0.5, 0.5, and 0.25 h for the second, third, fourth, and fifth cycles, respectively) with more washings (5 × 300 μL for the third, fourth, and fifth cycles)
31. Fibronectin (Sigma) was immobilized on a chip CM5 (carboxymethylated dextran, BIAcore) using an amine-coupling kit (BIAcore) under continuous flow (10 μL/min) of 10 mM HEPES buffer (pH 7.4) containing NaCl (150 mM). A solution (70 μL) of N-hydroxysuccinimide (50 mM) and 1-(3- dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (200 mM) was injected to activate the carboxymethylated dextran surface. A solution (100 μL) of fibronectin (1 mg/mL in aqueous sodium acetate, pH 5.0) was then injected onto the activated surface at a flow rate of 1 μL/min, followed by blocking with 70 μL of ethanolamine hydrochloride (1.0 M, pH 8.5) and washing with 10 × 10 μL of 50 mM NaOH to afford a fibronectin-coated CM5 chip (ΔRU, ∼10, 000)
32. A 50 μL PBS(+) solution of a cloned aptamer (10 μM) was incubated in a fibronectin-coated 96-well plate at 4°C overnight. After removing the solution, the plate was washed with 2 × 100 μL of PBS(+) and then BHK cells were seeded on the plate at 37°C. After incubation for 2 h, microscopic observation was made for the cell shape and numbers of adherent/floating cells in each well with an Olympus IX70 optical microscope
33. No cell adsorption was detected when a fibronectin-free plate was used
34. For the RGD peptide-based cell-adhesion inhibitors, see, for example: Schütt M., Kruoka S.S., Milbradt A.G., Deindl S., Sinner E.-V., Oesterhelt D., Renner C., Moroder L. Chem. Biol. 10:2003;487-490
35. For SELEX studies on cell-adhesion modulators, see, for example: Ulrich H., Magdesian M.H., Alves M.J.M., Colli W. J. Biol. Chem. 277:2002;20756-20762
36. Jeong S., Eom T.-Y., Kim S.-J., Lee S.-W., Yu J. Biochem. Biophys. Res. Commun. 281:2001;237-243