The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Tenascin-C Aptamers Are Generated Using Tumor Cells and Purified Protein
Open accessAbstract
Tenascin-C (TN-C) is an extracellular matrix protein that is overexpressed during tissue remodeling processes, including tumor growth. To identify an aptamer for testing as a tumor-selective ligand, SELEX (systematic evolution of ligands by exponential enrichment) procedures were performed using both TN-C and TN-C-expressing U251 glioblastoma cells. The different selection techniques yielded TN-C aptamers that are related in sequence. In addition, a crossover procedure that switched from tumor cell to purified protein selections was effective in isolating two high-affinity TN-C aptamers. When targeting tumor cells in vitro, the observed propensity of naive oligonucleotide pools to evolve TN-C aptamers may be due to the abundance of this protein. In vivo, TN-C abundance may also be well suited for aptamer accumulation in the tumor milieu. A size-minimized and nuclease-stabilized aptamer, TTA1, binds to the fibrinogen-like domain of TN-C with an equilibrium dissociation constant (K(d)) of 5 x 10(-9) m. At 13 kDa, this aptamer is intermediate in size between peptides and single chain antibody fragments, both of which are superior to antibodies for tumor targeting because of their smaller size. TTA1 defines a new class of ligands that are intended for targeted delivery of radioisotopes or chemical agents to diseased tissues.
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Cited by
Keefe, A. D., Pai, S., & Ellington, A. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3141 · Cited by 2,289
SELEX—A (r)evolutionary method to generate high-affinity nucleic acid ligands
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Aptamers: An Emerging Class of Therapeutics
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Self-citation
Metadata
- Authors
- Hicke, B. J., Marion, C., Chang, Y.-F., Gould, T., Lynott, C. K., Parma, D., Schmidt, P. G., & Warren, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-12
- Volume
- 276
- Issue
- 52
- Pages
- 48644-48654
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038167103
- Cited by
- 324
- References
- 49
- FWCI
- 2.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
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