Shannon Kevin M
Department of Pediatrics and Comprehensive Cancer Center, University of California, San Francisco, San Francisco, California 94143, USA.
Cancer Cell. 2002 Aug;2(2):99-102. doi: 10.1016/s1535-6108(02)00101-0.
The fusion tyrosine kinase Bcr-Abl plays a fundamental role in the pathogenesis of chronic myeloid leukemia (CML). Imatinib, a potent inhibitor of Bcr-Abl, has shown impressive clinical activity in CML patients. However, primary and acquired resistance occurs in many patients and is associated with reactivation of Bcr-Abl in primary leukemia cells. Studies reported over the past year have begun to elucidate the molecular basis of imatinib resistance, which may involve amplification of BCR-ABL or, more commonly, mutations that introduce amino acid substitutions into the Bcr-Abl kinase. Biochemical analysis and molecular modeling indicate that these mutant proteins retain kinase activity but are less sensitive to inhibition due to structural changes that perturb drug binding. These studies establish a paradigm for elucidating resistance to targeted therapeutics.
融合酪氨酸激酶Bcr-Abl在慢性髓性白血病(CML)的发病机制中起关键作用。伊马替尼是一种有效的Bcr-Abl抑制剂,已在CML患者中显示出令人瞩目的临床活性。然而,许多患者会出现原发性和获得性耐药,这与原发性白血病细胞中Bcr-Abl的重新激活有关。过去一年报道的研究已开始阐明伊马替尼耐药的分子基础,这可能涉及BCR-ABL的扩增,或更常见的是在Bcr-Abl激酶中引入氨基酸替代的突变。生化分析和分子建模表明,这些突变蛋白保留激酶活性,但由于干扰药物结合的结构变化而对抑制作用不太敏感。这些研究建立了一个阐明对靶向治疗耐药性的范例。