Yes / The integrin family of cell surface receptors integrates cell-extracellular matrix interactions with the cell cytoskeleton and signalling across the cell membrane, resulting in an important role in cell adhesion, mobility and migration,
proliferation, and survival. Changes in the number and identity of integrin receptors are common in cancer cells resulting
in alteration of the ability of malignant cells to interact with the extracellular matrix, and promoting migration as well as
facilitating survival outside the tumour normal environment. Beta3 integrins are potentially involved in every step of the metastatic process and expression of both alphaIIbbeta3 and alphaVbeta3 is correlated with metastatic ability of tumour cells. The recognition of the RGD binding motif common to the disintegrins and natural integrin ligands such as fibrinogen allowed the development of small molecule beta3 integrin antagonists, progressing from linear peptides containing the RGD sequence to cyclic peptides with well-defined conformation, and hence to small molecule peptidomimetics with improved pharmacological
properties. In this review, we summarize the role of the beta3-subfamily of integrins when expressed in normal and tumour
tissue, the development of small-molecule antagonists of beta3 integrins and their potential anti-cancer applications / EPSRC, Yorkshire Cancer Research
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/4613 |
| Date | 06 1900 |
| Creators | Sheldrake, Helen M., Patterson, Laurence H. |
| Source Sets | Bradford Scholars |
| Language | English |
| Detected Language | English |
| Type | Article, Accepted Manuscript |
| Relation | http://www.bentham.org/ccdt/contabs/ccdt9-4.htm |
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