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The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

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Binding of alpha-1-acid glycoprotein to imatinib following increased dosage of drug

Smith, K.D. and Paterson, S. (2005) Binding of alpha-1-acid glycoprotein to imatinib following increased dosage of drug. Haematologica, 90. pp. 9-10. ISSN 0390-6078

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Abstract

Imatinib mesylate (Glivec®, Novartis Pharma) is a highlyefficacious tyrosine kinase inhibitor, designed for treatment of chronic myeloid leukaemia (CML), by virtue of its ability to inhibit the oncogenic signalling of the BCR-ABL protein believed to be the causative abnormality of the disease. However, resistance is observed in a subset of CML patients, which could be due to mutations in BCR-ABL that prohibit binding of imatinib or overexpression of the BCR-ABL gene (Paterson et al, 2003). Alternatively, circulating serum proteins have been proposed as an alternative mechanism that reduces imatinib efficacy through non specific binding to the drug. In particular, it has been suggested that the protein a-1-acid glycoprotein (AGP) can bind to imatinib in the plasma and hence decrease the free, and therefore active, concentration of the drug (Gambacorti-Passerini et al, 2000).