Human tumour-associated cell adhesion protein MN/CA IX: identification of M75 epitope and of the region mediating cell adhesion
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10839295
PubMed Central
PMC2363230
DOI
10.1054/bjoc.2000.1111
PII: S000709200091111X
Knihovny.cz E-resources
- MeSH
- Cell Adhesion * MeSH
- Chromatography, Affinity MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Humans MeSH
- Epitope Mapping * MeSH
- Molecular Sequence Data MeSH
- Cell Adhesion Molecules chemistry immunology metabolism MeSH
- Tumor Cells, Cultured MeSH
- Neoplasm Proteins chemistry immunology metabolism MeSH
- Amino Acid Sequence MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Cell Adhesion Molecules MeSH
- Neoplasm Proteins MeSH
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.
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