Human tumour-associated cell adhesion protein MN/CA IX: identification of M75 epitope and of the region mediating cell adhesion
| Autor: | J Velek, Jaromir Pastorek, Zuzana Závadová, Jan Zavada, J Jez̆ek, Z Biesová |
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| Jazyk: | angličtina |
| Rok vydání: | 2000 |
| Předmět: |
Cancer Research
Phage display drug design carbonic anhydrase Molecular Sequence Data Enzyme-Linked Immunosorbent Assay Biology Epitope Chromatography Affinity cell adhesion molecules Cell surface receptor Cell Adhesion Tumor Cells Cultured Humans Amino Acid Sequence Binding site Cell adhesion chemistry.chemical_classification Cell adhesion molecule tumour immunology Regular Article Molecular biology Amino acid Neoplasm Proteins Epitope mapping Oncology chemistry Biochemistry phage display Epitope Mapping |
| Zdroj: | British Journal of Cancer |
| ISSN: | 1532-1827 0007-0920 |
| Popis: | MN/CA IX is a cell surface protein, strongly associated with several types of human carcinomas. It exerts activity of carbonic anhydrase and capacity of binding to cell surface receptors. In the present work, we used affinity purified MN/CA IX protein to demonstrate that the cells adhere to immobilized MN/CA IX and that the monoclonal antibody M75 abrogates cell attachment to MN/CA IX. Using synthetic oligopeptides, we identified M75 epitope and located it in the proteoglycan domain, which contains a sixfold tandem repeat of six amino acids GEEDLP. From phage display library of random heptapeptides we identified and chemically synthesized those which compete for the epitope with M75 and inhibit adhesion of cells to MN/CA IX. These heptapeptides might serve as lead compounds for drug design. © 2000 Cancer Research Campaign |
| Databáze: | OpenAIRE |
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