In a high proportion of human carcinomas overexpression of the EGFR (epidermal growth factor receptor), a receptor tyrosine kinase, represents a potential target for cancer treatment. EGFR is induced to dimerize through ligand binding which activates the tyrosine kinase activity of the receptor. This catalyses the transfer of ATP's γ-phosphate to hydroxyl groups of tyrosine residues on the receptor, creating binding sites that recruit downstream signalling proteins. New drugs, SMTKIs (small-molecule tyrosine kinase inhibitors), have been designed to inhibit the tyrosine kinase activity of the receptor, producing an anti-tumour effect. The development of surrogate markers to determine the drug activity of these new inhibitors would be of great benefit in drug evaluation and in the subsequent management of patient disease. This review describes current treatments of cancer using tyrosine kinase inhibitors and the use of proteomic analysis to identify possible markers of activity of these new drugs.
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December 2003
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Conference Article|
December 01 2003
Identification of surrogate markers for determining drug activity using proteomics
C.M. McClelland;
C.M. McClelland
1
Cancer Biology Laboratory, Research School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K.
1To whom correspondence should be addressed (e-mail cmm10@kent.ac.uk).
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W.J. Gullick
W.J. Gullick
Cancer Biology Laboratory, Research School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (6): 1488–1490.
Citation
C.M. McClelland, W.J. Gullick; Identification of surrogate markers for determining drug activity using proteomics. Biochem Soc Trans 1 December 2003; 31 (6): 1488–1490. doi: https://doi.org/10.1042/bst0311488
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